2021RUB01 - Allegato 16 - DR commissione

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【博士申请】帕多瓦大学2021/2022博士标准选拔章程已公布

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帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接:https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

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帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

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帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接:https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

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帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

[safe_summary] => ) ) ) [field_date_box_lancio_news] => Array ( [und] => Array ( [0] => Array ( [value] => 2021-04-08T00:00:00 [timezone] => Europe/Paris [timezone_db] => Europe/Paris [date_type] => date ) ) ) [field_etichetta_box_lancio_news] => Array ( ) [field_img_box_lancio_news] => Array ( [und] => Array ( [0] => Array ( [fid] => 65743 [uid] => 1 [filename] => Panoramica_cortile1.jpg [uri] => public://Panoramica_cortile1.jpg [filemime] => image/jpeg [filesize] => 62562 [status] => 1 [timestamp] => 1537354950 [type] => image [field_file_image_alt_text] => Array ( ) [field_file_image_title_text] => Array ( ) [field_folder] => Array ( [und] => Array ( [0] => Array ( [tid] => 2048 ) ) ) [metadata] => Array ( [height] => 410 [width] => 728 ) [height] => 410 [width] => 728 [is_default] => 1 [alt] => [title] => ) ) ) [field_link_alla_news] => Array ( ) [field_link_esterno_news] => Array ( [und] => Array ( [0] => Array ( [value] => [format] => [safe_value] => ) ) ) [field_pagina_associata] => Array ( ) [field_link_etichetta] => Array ( ) [field_abstract_news] => Array ( ) [field_allegato_news] => Array ( ) [field_categorie_news] => Array ( [und] => Array ( [0] => Array ( [tid] => 2307 ) ) ) [field_pub_date] => Array ( [und] => Array ( [0] => Array ( [value] => 2021-04-08T00:00:00 [value2] => 2024-04-24T00:00:00 [timezone] => Europe/Paris [timezone_db] => Europe/Paris [date_type] => date ) ) ) [field_layout_news] => Array ( [und] => Array ( [0] => Array ( [value] => single ) ) ) [field_testo_opzionale_news] => Array ( ) [field_url_en_page] => Array ( ) [field_url_en_page_label] => Array ( ) [path] => Array ( [pathauto] => 1 ) [name] => chinaoffice [picture] => 0 [data] => b:0; [num_revisions] => 1 [current_revision_id] => 351145 [is_current] => 1 [is_pending] => [revision_moderation] => [entity_view_prepared] => 1 ) [#items] => Array ( [0] => Array ( [value] =>

帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接:https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

[summary] => [format] => 2 [safe_value] =>

帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

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帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

) ) [field_img_box_lancio_news] => Array ( [#theme] => field [#weight] => 0 [#title] => Immagine [#access] => 1 [#label_display] => above [#view_mode] => teaser [#language] => und [#field_name] => field_img_box_lancio_news [#field_type] => image [#field_translatable] => 0 [#entity_type] => node [#bundle] => box_lancio_news [#object] => stdClass Object ( [vid] => 351145 [uid] => 5493 [title] => 【博士申请】帕多瓦大学2021/2022博士标准选拔章程已公布 [log] => [status] => 1 [comment] => 0 [promote] => 1 [sticky] => 0 [nid] => 76869 [type] => box_lancio_news [language] => it [created] => 1617895245 [changed] => 1617895245 [tnid] => 0 [translate] => 0 [revision_timestamp] => 1617895245 [revision_uid] => 5493 [body] => Array ( [und] => Array ( [0] => Array ( [value] =>

帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接:https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

[summary] => [format] => 2 [safe_value] =>

帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

[safe_summary] => ) ) ) [field_date_box_lancio_news] => Array ( [und] => Array ( [0] => Array ( [value] => 2021-04-08T00:00:00 [timezone] => Europe/Paris [timezone_db] => Europe/Paris [date_type] => date ) ) ) [field_etichetta_box_lancio_news] => Array ( ) [field_img_box_lancio_news] => Array ( [und] => Array ( [0] => Array ( [fid] => 65743 [uid] => 1 [filename] => Panoramica_cortile1.jpg [uri] => public://Panoramica_cortile1.jpg [filemime] => image/jpeg [filesize] => 62562 [status] => 1 [timestamp] => 1537354950 [type] => image [field_file_image_alt_text] => Array ( ) [field_file_image_title_text] => Array ( ) [field_folder] => Array ( [und] => Array ( [0] => Array ( [tid] => 2048 ) ) ) [metadata] => Array ( [height] => 410 [width] => 728 ) [height] => 410 [width] => 728 [is_default] => 1 [alt] => [title] => ) ) ) [field_link_alla_news] => Array ( ) [field_link_esterno_news] => Array ( [und] => Array ( [0] => Array ( [value] => [format] => [safe_value] => ) ) ) [field_pagina_associata] => Array ( ) [field_link_etichetta] => Array ( ) [field_abstract_news] => Array ( ) [field_allegato_news] => Array ( ) [field_categorie_news] => Array ( [und] => Array ( [0] => Array ( [tid] => 2307 ) ) ) [field_pub_date] => Array ( [und] => Array ( [0] => Array ( [value] => 2021-04-08T00:00:00 [value2] => 2024-04-24T00:00:00 [timezone] => Europe/Paris [timezone_db] => Europe/Paris [date_type] => date ) ) ) [field_layout_news] => Array ( [und] => Array ( [0] => Array ( [value] => single ) ) ) [field_testo_opzionale_news] => Array ( ) [field_url_en_page] => Array ( ) [field_url_en_page_label] => Array ( ) [path] => Array ( [pathauto] => 1 ) [name] => chinaoffice [picture] => 0 [data] => b:0; [num_revisions] => 1 [current_revision_id] => 351145 [is_current] => 1 [is_pending] => [revision_moderation] => [entity_view_prepared] => 1 ) [#items] => Array ( [0] => Array ( [fid] => 65743 [uid] => 1 [filename] => Panoramica_cortile1.jpg [uri] => public://Panoramica_cortile1.jpg [filemime] => image/jpeg [filesize] => 62562 [status] => 1 [timestamp] => 1537354950 [type] => image [field_file_image_alt_text] => Array ( ) [field_file_image_title_text] => Array ( ) [field_folder] => Array ( [und] => Array ( [0] => Array ( [tid] => 2048 ) ) ) [metadata] => Array ( [height] => 410 [width] => 728 ) [height] => 410 [width] => 728 [is_default] => 1 [alt] => [title] => ) ) [#formatter] => image [0] => Array ( [#theme] => image_formatter [#item] => Array ( [fid] => 65743 [uid] => 1 [filename] => Panoramica_cortile1.jpg [uri] => public://Panoramica_cortile1.jpg [filemime] => image/jpeg [filesize] => 62562 [status] => 1 [timestamp] => 1537354950 [type] => image [field_file_image_alt_text] => Array ( ) [field_file_image_title_text] => Array ( ) [field_folder] => Array ( [und] => Array ( [0] => Array ( [tid] => 2048 ) ) ) [metadata] => Array ( [height] => 410 [width] => 728 ) [height] => 410 [width] => 728 [is_default] => 1 [alt] => [title] => ) [#image_style] => [#path] => ) ) [links] => Array ( [#theme] => links__node [#pre_render] => Array ( [0] => drupal_pre_render_links ) [#attributes] => Array ( [class] => Array ( [0] => links [1] => inline ) ) [node] => Array ( [#theme] => links__node__node [#links] => Array ( [node-readmore] => Array ( [title] => Read more about 【博士申请】帕多瓦大学2021/2022博士标准选拔章程已公布 [href] => node/76869 [html] => 1 [attributes] => Array ( [rel] => tag [title] => 【博士申请】帕多瓦大学2021/2022博士标准选拔章程已公布 ) ) ) [#attributes] => Array ( [class] => Array ( [0] => links [1] => inline ) ) ) ) [field_date_box_lancio_news] => Array ( [#theme] => field [#weight] => 1 [#title] => Data [#access] => 1 [#label_display] => above [#view_mode] => teaser [#language] => und [#field_name] => field_date_box_lancio_news [#field_type] => date [#field_translatable] => 0 [#entity_type] => node [#bundle] => box_lancio_news [#object] => stdClass Object ( [vid] => 351145 [uid] => 5493 [title] => 【博士申请】帕多瓦大学2021/2022博士标准选拔章程已公布 [log] => [status] => 1 [comment] => 0 [promote] => 1 [sticky] => 0 [nid] => 76869 [type] => box_lancio_news [language] => it [created] => 1617895245 [changed] => 1617895245 [tnid] => 0 [translate] => 0 [revision_timestamp] => 1617895245 [revision_uid] => 5493 [body] => Array ( [und] => Array ( [0] => Array ( [value] =>

帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接:https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

[summary] => [format] => 2 [safe_value] =>

帕多瓦大学成立于1222年(南宋时期),是世界最古老的顶尖大学之一。帕多瓦大学是意大利 “拥有最高质量研究成果的大学”,学术文章引用量在欧洲顶级大学中位居的前10%。帕多瓦大学博士时长3年,无学费,每年须缴纳大区税费。

帕多瓦大学2021/2022博士标准选拔细则已公布。该选拔针对全球学生进行,报名截止日期为2021年5月12日13时(意大利时间)

国籍:无限制

报名方式:网申

网申截止时间:2021年5月12日13时(意大利时间)

网申步骤

1. 请首先点击https://www.unipd.it/en/phd-programmes-calls-and-admissions 查看有关2021/2022帕多瓦大学博士选拔的相关文件,包括专业、名额设置、选拔标准、网申指引等信息。

2.  在网申平台注册账号,按网申指引在截止日期前网上提交申请材料。

网申指引链接https://pica.cineca.it/unipd/dottorati37

选拔方式:各博士专业评审委员会首先对在截止日期内成功提交的申请人进行材料审核。通过初审的申请者会收到面试邀请邮件或在各专业细则中标明相应网址上登出通过初选者名单、面试时间。面试通过学生将收到帕多瓦大学的录取书,满足相应要求并在2021年9月30日前完成注册手续即可入读。

费用:帕多瓦大学博士无学费,但必须缴纳大区税。帕多瓦大学为优秀申请者提供奖学金机会(根据各专业实际情况而定)及提供外部资助申请机会。

网申注意事项:

1.申请者在网申过程中会要求填写为申请者书写推荐信专家的邮箱。专家收到学校邮件后按照指示上传推荐信即可。申请人在网申阶段自行上传推荐信视为无效。

2.已申请帕多瓦大学—中国国家留学基金委奖学金项目学生不影响同时报名帕多瓦大学博士标准选拔。若均获得录取,只能接受其中一个录取方式。 

帕多瓦大学是意大利“拥有最高研究成果的大学”,如果想了解更多帕多瓦大学博士生的相关实用信息,我校博士处为大家准备了《国际博士生指南》,告诉你如何能够提升在帕多瓦大学读博体验。

《国际博士生指南》下载链接:https://www.unipd.it/en/phd-guide

 

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RICERCA UNIPD - MALATTIE MITOCONDRIALI E NUOVA FARMACOLOGIA. LA PIOCIANINA È EFFICACE PER RECUPERARE L'ATTIVITÀ MOTORIA

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Iscrizione contemporanea a più corsi universitari

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Procedura di immatricolazione con abbreviazione di carriera

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Procedura di chiusura della carriera per corsi singoli e nuova immatricolazione

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Trasparenza - Dati adesione sciopero 2021

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New experimental screening protocols to understand the mechanisms behind thrombosis

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The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

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The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

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The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

[summary] => [format] => 2 [safe_value] =>

The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

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The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

[summary] => [format] => 2 [safe_value] =>

The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

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The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).

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The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

[summary] => [format] => 2 [safe_value] =>

The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

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The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

[summary] => [format] => 2 [safe_value] =>

The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

[safe_summary] => ) ) ) [field_date_box_lancio_news] => Array ( [und] => Array ( [0] => Array ( [value] => 2021-04-08T00:00:00 [timezone] => Europe/Paris [timezone_db] => Europe/Paris [date_type] => date ) ) ) [field_etichetta_box_lancio_news] => Array ( ) [field_img_box_lancio_news] => Array ( [und] => Array ( [0] => Array ( [fid] => 92050 [uid] => 2032 [filename] => adobestock_trombo.jpg [uri] => public://adobestock_trombo_0.jpg [filemime] => image/jpeg [filesize] => 21868 [status] => 1 [timestamp] => 1617885126 [type] => image [field_file_image_alt_text] => Array ( ) [field_file_image_title_text] => Array ( ) [field_folder] => Array ( [und] => Array ( [0] => Array ( [tid] => 2048 ) ) ) [metadata] => Array ( [height] => 227 [width] => 677 ) [height] => 227 [width] => 677 [alt] => thrombosis [title] => ) ) ) [field_link_alla_news] => Array ( ) [field_link_esterno_news] => Array ( [und] => Array ( [0] => Array ( [value] => [format] => [safe_value] => ) ) ) [field_pagina_associata] => Array ( ) [field_link_etichetta] => Array ( ) [field_abstract_news] => Array ( [und] => Array ( [0] => Array ( [value] => Researchers from the University of Padua, along with an international team, have created new experimental protocols to understand the mechanisms of thrombosis. Taking a step forward in understanding the mechanism behind thrombotic disorders and the development of new drug treatments. [format] => [safe_value] => Researchers from the University of Padua, along with an international team, have created new experimental protocols to understand the mechanisms of thrombosis. Taking a step forward in understanding the mechanism behind thrombotic disorders and the development of new drug treatments. ) ) ) [field_allegato_news] => Array ( ) [field_categorie_news] => Array ( [und] => Array ( [0] => Array ( [tid] => 2296 ) ) ) [field_pub_date] => Array ( [und] => Array ( [0] => Array ( [value] => 2021-04-08T00:00:00 [value2] => 2022-04-08T00:00:00 [timezone] => Europe/Paris [timezone_db] => Europe/Paris [date_type] => date ) ) ) [field_layout_news] => Array ( [und] => Array ( [0] => Array ( [value] => single ) ) ) [field_testo_opzionale_news] => Array ( ) [field_url_en_page] => Array ( ) [field_url_en_page_label] => Array ( ) [path] => Array ( [pathauto] => 1 ) [name] => francesca.forzan [picture] => 0 [data] => b:0; [num_revisions] => 1 [current_revision_id] => 351109 [is_current] => 1 [is_pending] => [revision_moderation] => [entity_view_prepared] => 1 ) [#items] => Array ( [0] => Array ( [value] => Researchers from the University of Padua, along with an international team, have created new experimental protocols to understand the mechanisms of thrombosis. Taking a step forward in understanding the mechanism behind thrombotic disorders and the development of new drug treatments. [format] => [safe_value] => Researchers from the University of Padua, along with an international team, have created new experimental protocols to understand the mechanisms of thrombosis. Taking a step forward in understanding the mechanism behind thrombotic disorders and the development of new drug treatments. ) ) [#formatter] => text_default [0] => Array ( [#markup] => Researchers from the University of Padua, along with an international team, have created new experimental protocols to understand the mechanisms of thrombosis. Taking a step forward in understanding the mechanism behind thrombotic disorders and the development of new drug treatments. ) ) [links] => Array ( [#theme] => links__node [#pre_render] => Array ( [0] => drupal_pre_render_links ) [#attributes] => Array ( [class] => Array ( [0] => links [1] => inline ) ) [node] => Array ( [#theme] => links__node__node [#links] => Array ( [node-readmore] => Array ( [title] => Read more about New experimental screening protocols to understand the mechanisms behind thrombosis [href] => node/76859 [html] => 1 [attributes] => Array ( [rel] => tag [title] => New experimental screening protocols to understand the mechanisms behind thrombosis ) ) ) [#attributes] => Array ( [class] => Array ( [0] => links [1] => inline ) ) ) ) [field_date_box_lancio_news] => Array ( [#theme] => field [#weight] => 1 [#title] => Data [#access] => 1 [#label_display] => above [#view_mode] => teaser [#language] => und [#field_name] => field_date_box_lancio_news [#field_type] => date [#field_translatable] => 0 [#entity_type] => node [#bundle] => box_lancio_news [#object] => stdClass Object ( [vid] => 351109 [uid] => 2032 [title] => New experimental screening protocols to understand the mechanisms behind thrombosis [log] => [status] => 1 [comment] => 0 [promote] => 1 [sticky] => 0 [nid] => 76859 [type] => box_lancio_news [language] => it [created] => 1617885126 [changed] => 1617885126 [tnid] => 0 [translate] => 0 [revision_timestamp] => 1617885126 [revision_uid] => 2032 [body] => Array ( [und] => Array ( [0] => Array ( [value] =>

The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

[summary] => [format] => 2 [safe_value] =>

The study entitled Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen  is the result of the collaboration between the Quantitative Proteomics Laboratory of Prof. Ruedi Aebersold (ETH, Zurich, Switzerland) and the Laboratory of Protein Chemistry and Molecular Hematology of Prof. Vincenzo De Filippis (University of Padua).  Their finding has created a new experimental screening protocol to understand the mechanisms behind thrombosis.

The findings were published in “Nature Communication" and are considered the first step in designing and synthesizing new protease inhibitors with potential drug related applications for several pathologies, including thrombosis. Soon, a blood test or saliva sample will be enough to screen the protease profile with a single test to see if a subjects protease are working correctly, or if one or more show abnormal activity that can cause the disorder.

The biochemical mechanisms determining the physiological coagulation of blood, which prevents blood loss, can occur following vessel (artery or vein) damage caused, for example, by trauma. Blood clot formation, which mainly consists of fibrin and platelets that temporarily “plugs” the damaged vessel. Other processes then trigger how the body will repair the damaged vasculature. It is not clear why, but some clots generate without the onset of a vessel lesion, yet they still cause blood loss. Under these conditions, the formation of a blood clot can obstruct the blood vessel and prevent blood from "downstream" and adequately nourishing tissue, thus leading to the onset of thrombotic disorders such as a heart attack or stroke.

Physiological and pathological conditions that form a blood clot are not easily generated, as a sequence (like a cascade of events) of about twenty proteins are involved and as well as substrates, which are enzyme proteases capable of "breaking down" other proteins. These proteins then become active proteases thus breaking down and activating other proteins, until they generate a clot. There is therefore a sequence of events, which takes the name of "coagulation cascade."

This work has developed a new experimental screening protocol to characterize the substrate specificity of the proteases of the coagulation cascade, i.e. the identification of the specific amino acid sequence that is "broken down" by the various proteases involved in the blood coagulation process.

The focus of the study is on the characterization of a dozen proteases of the coagulation cascade that, under different conditions, generate more than 100,000 unique fragments. Developing this approach is essential to understand the mechanisms of thrombotic disorders, with the goal of creating new drug treatments. Currently, these disorders represent the major cause of death and hospitalization in the industrialized world.

Additionally, the identification of substrates can represent the first step in the design and synthesis of new protease inhibitors that hold potential pharmacological applications in many of the aforementioned disorders. The novel approach is the possibility of using advanced mass spectrometry techniques to identify, not for one, but thousands of substrates for each protease under study within a few hours.

Prof Vincenzo De Filippis explains, “With this in mind, one day we will be able to take a blood or a saliva sample, and conduct a single test to profile the proteases to know if they are working correctly or if one or more show abnormal activity, which can cause disease. This profile will be essential in identifying risk factors for serious illness (e.g. thrombotic disorders) in advance and offering the best available care for each patient using personalized therapeutic approaches.

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Bando WCRI Decreto di proroga scadenza presentazione Business Plan DR n. 1300/2021 del 08/04/2021

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2020RUA06 - Allegato 4 - DR approvazione atti

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