Structural Preordering in the N-Terminal Region of Ribosomal Protein S4 Revealed by Heteronuclear NMR Spectroscopy-Reference-Cited by-同舟云学术

Structural Preordering in the N-Terminal Region of Ribosomal Protein S4 Revealed by Heteronuclear NMR Spectroscopy

Published:2000-10-11 Issue:44 Volume:39 Page:13602-13613
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sayers Eric W.¹,Gerstner Resi B.¹,Draper David E.¹,Torchia Dennis A.¹

Affiliation:

1. Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, Molecular Structural Biology Unit, National Institute of Dental and Craniofacial Research, National Institutes of Health, 30 Convent Drive, MSC 4307, Bethesda, Maryland 20892-4307

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0013391

Reference60 articles.

1. Localization of the binding site for protein S4 on 16 S ribosomal RNA by chemical and enzymatic probing and primer extension

2. S4-16 S ribosomal RNA complex

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. Structure and disorder: protein functions depend on this new binary transforming lock-and-key into structure-function continuum;Structure and Intrinsic Disorder in Enzymology;2023

2. Per aspera ad chaos: a personal journey to the wonderland of intrinsic disorder;Biochemical Journal;2021-08-10

3. Target-binding behavior of IDPs via pre-structured motifs;Progress in Molecular Biology and Translational Science;2021

4. Clusters of bacterial RNA polymerase are biomolecular condensates that assemble through liquid–liquid phase separation;Proceedings of the National Academy of Sciences;2020-07-16

5. Expanding the understanding of the heterogeneous nature of melanoma with bioinformatics and disorder-based proteomics;International Journal of Biological Macromolecules;2020-05