KR102348939B1 - 면역글로불린 a 신증을 앓고 있는 인간 대상체에서 단백뇨를 감소시키는 방법 - Google Patents

면역글로불린 a 신증을 앓고 있는 인간 대상체에서 단백뇨를 감소시키는 방법 Download PDF

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Publication number: KR102348939B1
Authority: KR; South Korea
Prior art keywords: masp; antibody; fibrosis; seq; inhibitory
Prior art date: 2016-10-13

Application number

KR1020197012865A

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English (en)

Korean (ko)

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KR20190063475A (ko

Inventor

니겔 존 브룬스킬

그레고리 에이. 데모풀로스

톰 두들러

한스-윌헬름 슈웨블

Original Assignee

유니버시티 오브 레스터

오메로스 코포레이션

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2016-10-13

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2017-10-12

Publication date

2022-01-12

2017-01-05 Priority claimed from US15/399,524 external-priority patent/US10736960B2/en

2017-03-27 Priority claimed from US15/470,647 external-priority patent/US20170253667A1/en

2017-10-12 Application filed by 유니버시티 오브 레스터, 오메로스 코포레이션 filed Critical 유니버시티 오브 레스터

2019-06-07 Publication of KR20190063475A publication Critical patent/KR20190063475A/ko

2022-01-12 Application granted granted Critical

2022-01-12 Publication of KR102348939B1 publication Critical patent/KR102348939B1/ko

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KR1020197012865A 2016-10-13 2017-10-12 면역글로불린 a 신증을 앓고 있는 인간 대상체에서 단백뇨를 감소시키는 방법 KR102348939B1 (ko)

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US201662407979P	2016-10-13	2016-10-13
US62/407,979		2016-10-13
US15/399,524 US10736960B2 (en)	2016-01-05	2017-01-05	Methods for inhibiting fibrosis in a subject in need thereof
US15/399,524		2017-01-05
US15/470,647 US20170253667A1 (en)	2016-01-05	2017-03-27	Methods for inhibiting fibrosis in a subject in need thereof
US15/470,647		2017-03-27
US201762527926P	2017-06-30	2017-06-30
US62/527,926		2017-06-30
PCT/US2017/056386 WO2018071701A1 (en)	2016-10-13	2017-10-12	Methods for reducing proteinuria in a human subject suffering from immunoglobulin a nephropathy

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SG (1)	SG11201902941UA (he)
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Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN111419860A (zh) *	2020-03-19	2020-07-17	长春市儿童医院	一种肾小球分叶状肾病造模方法
CN115215937B (zh) *	2021-04-15	2023-05-26	上海麦济生物技术有限公司	抗人masp-2抗体及其制备方法和应用
EP4444758A2 (en)	2021-12-10	2024-10-16	Omeros Corporation	Therapeutic antibodies that bind to the serine protease domain of masp-2 and uses thereof
CN117016486B (zh) *	2023-07-20	2024-05-14	上海澎立生技医药研究有限公司	一种IgA肾病合并膜性肾病的动物模型构建方法

Citations (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JP2009532943A (ja)	2006-03-31	2009-09-10	イーストマンコダックカンパニー	多階調中間調スクリーン生成方法
JP2009532493A (ja)	2006-04-03	2009-09-10	ユニバーシティオブレスター	Ｍａｓｐ−２依存性の補体活性化に関連する状態を処置するための方法
WO2015058143A1 (en) *	2013-10-17	2015-04-23	Omeros Corporation	Methods for treating conditions associated with masp-2 dependent complement activation
US20150239985A1 (en)	2011-04-08	2015-08-27	Omeros Corporation	Methods for Treating Conditions Associated with MASP-2 Dependent Complement Activation

Family Cites Families (10)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
HUE024996T2 (en) *	2003-05-12	2016-01-28	Helion Biotech Aps	Anti-MASP-2 antibodies
US20140056873A1 (en) *	2004-06-10	2014-02-27	University Of Leicester	Methods for Treating Conditions Associated with MASP-2 Dependent Complement Activation
US8840893B2 (en) *	2004-06-10	2014-09-23	Omeros Corporation	Methods for treating conditions associated with MASP-2 dependent complement activation
MX344322B (es) *	2009-10-16	2016-12-13	Omeros Corp	Uso de una composición que comprende un agente inhibidor de masp-2 efectivo para inhibir o prevenir la aparición de agregados en la vaculatura de un sujeto que sufre de un desorden de coagulación mediado por complemento.
WO2012100262A1 (en) *	2011-01-21	2012-07-26	Fibrogen, Inc.	Therapeutic method using anti - ctgf antibody
US9644035B2 (en) *	2011-04-08	2017-05-09	Omeros Corporation	Methods for treating conditions associated with MASP-2 dependent complement activation
AU2012250627B2 (en) *	2011-05-04	2016-01-07	Omeros Corporation	Compositions for inhibiting MASP-2 dependent complement acitivation
ES2964340T3 (es) *	2013-03-15	2024-04-05	Omeros Corp	Métodos para generar anticuerpos portadores de péptidos bioactivos y composiciones que comprenden los mismos
EA201891570A1 (ru) *	2016-01-05	2018-12-28	Юниверсити Оф Лестер	Способ подавления фиброза у нуждающегося в этом субъекта
JOP20170170B1 (ar) *	2016-08-31	2022-09-15	Omeros Corp	صيغ لجسم مضاد تثبيطية لـ masp-2 بتركيز عالي ولزوجة منخفضة وأطقم، وطرق

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Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JP2009532943A (ja)	2006-03-31	2009-09-10	イーストマンコダックカンパニー	多階調中間調スクリーン生成方法
JP2009532493A (ja)	2006-04-03	2009-09-10	ユニバーシティオブレスター	Ｍａｓｐ−２依存性の補体活性化に関連する状態を処置するための方法
US20150239985A1 (en)	2011-04-08	2015-08-27	Omeros Corporation	Methods for Treating Conditions Associated with MASP-2 Dependent Complement Activation
WO2015058143A1 (en) *	2013-10-17	2015-04-23	Omeros Corporation	Methods for treating conditions associated with masp-2 dependent complement activation

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Publication number	Publication date
ZA201902933B (en)	2023-05-31
CN110177557A (zh)	2019-08-27
IL265981A (he)	2019-06-30
MX2019004074A (es)	2019-06-10
CA3039927A1 (en)	2018-04-19
JP6893554B2 (ja)	2021-06-23
SG11201902941UA (en)	2019-05-30
JP2019534271A (ja)	2019-11-28
AU2017342428B2 (en)	2021-02-04
JOP20190068A1 (ar)	2019-04-01
CA3210384A1 (en)	2018-04-19
CN116726163A (zh)	2023-09-12
EP3525798A1 (en)	2019-08-21
EP3525798A4 (en)	2020-07-08
CL2019000909A1 (es)	2019-06-14
CL2019003485A1 (es)	2020-04-13
KR20190063475A (ko)	2019-06-07
NZ753260A (en)	2021-11-26
MA46541A (fr)	2019-08-21
PH12019500711A1 (en)	2019-11-18
WO2018071701A1 (en)	2018-04-19
AU2017342428A1 (en)	2019-05-23
GEP20247587B (en)	2024-01-25
CA3039927C (en)	2023-10-10
UA126908C2 (uk)	2023-02-22
BR112019007426A2 (pt)	2019-07-02

Publication	Publication Date	Title
AU2020201804B2 (en)	2022-06-16	Methods for inhibiting fibrosis in a subject in need thereof
US20210355236A1 (en)	2021-11-18	Methods for inhibiting fibrosis in a subject in need thereof
US20210079116A1 (en)	2021-03-18	Methods for reducing proteinuria in a human subject suffering from immunoglobulin a nephropathy
JP2024153761A (ja)	2024-10-29	コロナウイルス誘発性急性呼吸窮迫症候群の処置および／または予防のためにｍａｓｐ－２を阻害する方法
KR102348939B1 (ko)	2022-01-12	면역글로불린 a 신증을 앓고 있는 인간 대상체에서 단백뇨를 감소시키는 방법
EA043102B1 (ru)	2023-04-25	Способ уменьшения протеинурии у человека, страдающего от иммуноглобулин а нефропатии
OA19229A (en)	2020-04-24	Methods for reducing proteinuria in a human subject suffering from immunoglobulin a nephropathy.

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