Intrinsically disordered regions mediate macromolecular assembly of the Slit diaphragm proteins associated with Nephrotic syndrome-Reference-Cited by-同舟云学术

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Intrinsically disordered regions mediate macromolecular assembly of the Slit diaphragm proteins associated with Nephrotic syndrome

Published:2019-01-30 Issue:8 Volume:45 Page:603-613
ISSN:0892-7022
Container-title:Molecular Simulation
language:en
Short-container-title:Molecular Simulation

Author:

Mulukala Narasimha Sandeep K.¹,Kar Prajna Parimita²,Vadrevu Ramakrishna³,Pasupulati Anil K.¹

Affiliation:

1. Department of Biochemistry, University of Hyderabad, Hyderabad, India

2. Laboratory of Molecular Interactions, National Institute of Animal Biotechnology, Hyderabad, India

3. Department of Biological Sciences, BITS-Pilani, Hyderabad Campus, Hyderabad, India

Funder

Indian Council of Medical Research

Science and Engineering Research Board

Publisher

Informa UK Limited

Subject

Condensed Matter Physics,General Materials Science,General Chemical Engineering,Modeling and Simulation,Information Systems,General Chemistry

Link

https://www.tandfonline.com/doi/pdf/10.1080/08927022.2019.1570508

Reference33 articles.

1. Molecular basis of the glomerular filtration: Nephrin and the emerging protein complex at the podocyte slit diaphragm

2. In silicoStructural characterization of podocin and assessment of nephrotic syndrome-associated podocin mutants

3. A Single-Gene Cause in 29.5% of Cases of Steroid-Resistant Nephrotic Syndrome

Cited by 7 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Biophysical characterization and insights into the oligomeric nature of CD2-associated protein;International Journal of Biochemistry and Molecular Biology;2024

2. Evolutionary conservation of intrinsically unstructured regions in slit-diaphragm proteins;PLOS ONE;2021-07-21

3. Detrimental effects of hypoxia on glomerular podocytes;Journal of Physiology and Biochemistry;2021-04-09

4. Molecular Evolution of Podocyte Slit-diaphragm Proteins;2020-11-04

5. Structural features and oligomeric nature of human podocin domain;Biochemistry and Biophysics Reports;2020-09

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