Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Sequential assignment and secondary structure-Reference-Cited by-同舟云学术

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Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Sequential assignment and secondary structure

Published:1993-10-01 Issue:42 Volume:32 Page:11345-11351
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cerf Corinne,Lippens Guy,Muyldermans Serge,Segers Alain,Ramakrishnan V.,Wodak Shoshana J.,Hallenga Klaas,Wyns Lode

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00093a011

Cited by 55 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. Proteasome‐dependent degradation of histone H1 subtypes is mediated by its C‐terminal domain;Protein Science;2024-04-09

2. Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes;Journal of Molecular Biology;2023-10

3. Combining molecular dynamics simulations and scoring method to computationally model ubiquitylated linker histones in chromatosomes;PLOS Computational Biology;2023-08-01

4. Proteasome-dependent degradation of histone H1 subtypes is mediated by its C-terminal domain;2023-06-18

5. Histone H3 tail modifications regulate structure and dynamics of the H1 C-terminal domain within nucleosomes;2023-05-12

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