Pseudokinases repurpose flexibility signatures associated with the protein kinase fold for noncatalytic roles-Reference-Cited by-同舟云学术

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Pseudokinases repurpose flexibility signatures associated with the protein kinase fold for noncatalytic roles

Published:2021-11-18 Issue:3 Volume:90 Page:747-764
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Paul Anindita¹^ORCID,Subhadarshini Seemadri¹,Srinivasan Narayanaswamy¹^ORCID

Affiliation:

1. Molecular Biophysics Unit Indian Institute of Science Bangalore Karnataka India

Funder

Department of Biotechnology, Ministry of Science and Technology, India

Department of Science and Technology, Ministry of Science and Technology, India

Ministry of Human Resource Development

University Grants Commission of Bangladesh

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.26271

Reference96 articles.

1. The secret life of kinases: functions beyond catalysis

2. Structural Basis for the Non-catalytic Functions of Protein Kinases

3. The Protein Kinase Complement of the Human Genome

4. The mouse kinome: Discovery and comparative genomics of all mouse protein kinases

5. Signalling through kinase-defective domains: the prevalence of atypical receptor-like kinases in plants

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1. Normal Mode Analysis Elicits Conformational Shifts in Proteins at Both Proximal and Distal Regions to the Phosphosite Stemming from Single-Site Phosphorylation;ACS Omega;2024-05-30

2. Single-Site Phosphorylation Elicits Structural, Dynamic, and Accessibility Changes in Proteins at both Proximal and Distal Regions to the Phosphosite;2023-12-01

3. Pseudokinase NRP1 facilitates endocytosis of transferrin in the African trypanosome;Scientific Reports;2022-11-03

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