Co-opting disorder into order: Intrinsically disordered proteins and the early evolution of complex multicellularity-Reference-Cited by-同舟云学术

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Co-opting disorder into order: Intrinsically disordered proteins and the early evolution of complex multicellularity

Published:2022-03 Issue: Volume:201 Page:29-36
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Kulkarni Prakash,Behal Amita,Mohanty Atish,Salgia Ravi,Nedelcu Aurora M.,Uversky Vladimir N.

Funder

Natural Sciences and Engineering Research Council of Canada

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference104 articles.

1. Intrinsic disorderprotein-protein interactions, and disease;Uversky;Adv Protein Chem Struct Biol,2018

2. DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus;Hemmings;J. Neurosci.,1984

3. Prothymosin alpha: a biologically active protein with random coil conformation;Gast;Biochemistry,1995

4. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded;Weinreb;Biochemistry,1996

5. Thousands of proteins likely to have long disordered regions;Romero;Pac. Symp. Biocomput.,1998

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1. Intrinsic Disorder and Other Malleable Arsenals of Evolved Protein Multifunctionality;Journal of Molecular Evolution;2024-08-30

2. Characterization of Intrinsically Disordered Proteins in Healthy and Diseased States by Nuclear Magnetic Resonance;Reviews on Recent Clinical Trials;2024-08

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