Chemical Shift Mapped DNA-Binding Sites and 15N Relaxation Analysis of the C-Terminal KH Domain of Heterogeneous Nuclear Ribonucleoprotein K-Reference-Cited by-同舟云学术

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Chemical Shift Mapped DNA-Binding Sites and 15N Relaxation Analysis of the C-Terminal KH Domain of Heterogeneous Nuclear Ribonucleoprotein K

Published:2000-04-27 Issue:20 Volume:39 Page:6022-6032
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Baber James L.¹,Levens David¹,Libutti Daniel¹,Tjandra Nico¹

Affiliation:

1. Laboratory of Biophysical Chemistry, Building 3, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-0380, and Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi000105e

Reference75 articles.

1. Heterogeneous Nuclear Ribonucleoprotein K Is a DNA-binding Transactivator

2. Diverse molecular interactions of the hnRNP K protein

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2. DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids;2024-07-08

3. DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids;2024-04-02

4. KH domains with impaired nucleic acid binding as a tool for functional analysis;Nucleic Acids Research;2012-04-30

5. Characterization of binding-induced changes in dynamics suggests a model for sequence-nonspecific binding of ssDNA by replication protein A;Protein Science;2009-04-13

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