The Intermediate Chain of Cytoplasmic Dynein Is Partially Disordered and Gains Structure upon Binding to Light-Chain LC8-Reference-Cited by-同舟云学术

The Intermediate Chain of Cytoplasmic Dynein Is Partially Disordered and Gains Structure upon Binding to Light-Chain LC8

Published:2004-11-13 Issue:49 Volume:43 Page:15595-15603
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Nyarko Afua¹,Hare Michael¹,Hays Thomas S.¹,Barbar Elisar¹

Affiliation:

1. Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331, Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio 45701, and Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota 55455

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi048451%2B

Reference57 articles.

1. Cytoplasmic dynein plays a role in mammalian mitotic spindle formation.

2. Dynein: An ancient motor protein involved in multiple modes of transport

Cited by 66 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. Structure and Function of Dynein’s Non-Catalytic Subunits;Cells;2024-02-11

2. Linker Length Drives Heterogeneity of Multivalent Complexes of Hub Protein LC8 and Transcription Factor ASCIZ;Biomolecules;2023-02-21

3. Methods for measuring structural disorder in proteins;Structure and Intrinsic Disorder in Enzymology;2023

4. Multivalent Angiomotin‐like 1 and Yes‐associated protein form a dynamic complex;Protein Science;2022-04-09

5. A motor independent requirement for dynein light chain in Caenorhabditis elegans meiotic synapsis;Genetics;2021-11-12