Nephrin expression in human epidermal keratinocytes and its implication in poor wound closure-Reference-Cited by-同舟云学术

Nephrin expression in human epidermal keratinocytes and its implication in poor wound closure

Published:2022-06-23 Issue:7 Volume:36 Page:
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:The FASEB Journal

Author:

Kim Ji Young¹,Lee Eun Jung¹²,Seo Jimyung¹³,Lee Yangsin⁴,Ahn Yuri¹,Park Sujin¹,Bae Yu Jeong¹,Lee Jinu⁵,Lim Beom Jin⁶,Kim Doyoung¹,Cho Jin Won⁴⁷,Oh Sang Ho¹^ORCID

Affiliation:

1. Department of Dermatology and Cutaneous Biology Research Institute Severance Hospital, Yonsei University College of Medicine Seoul South Korea

2. Graduate School of Medical Science, Brain Korea 21 Project Yonsei University College of Medicine Seoul South Korea

3. Graduate School of Medical Science and Engineering Korea Advanced Institute of Science and Engineering Daejeon South Korea

4. Glycosylation Network Research Center Yonsei University Seoul South Korea

5. College of Pharmacy, Yonsei Institute of Pharmaceutical Sciences Yonsei University Incheon South Korea

6. Department of Pathology Yonsei University College of Medicine Seoul South Korea

7. Department of Systems Biology, College of Life Science and Biotechnology Yonsei University Seoul South Korea

Funder

Korean Dermatological Association

National Research Foundation of Korea

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.202100455RR

Reference57 articles.

1. Positionally Cloned Gene for a Novel Glomerular Protein—Nephrin—Is Mutated in Congenital Nephrotic Syndrome

2. Interaction with Podocin Facilitates Nephrin Signaling

3. Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin

4. Neph1 and nephrin interaction in the slit diaphragm is an important determinant of glomerular permeability

5. CD2AP Localizes to the Slit Diaphragm and Binds to Nephrin via a Novel C-Terminal Domain

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