Exploring Protein Intrinsic Disorder with MobiDB

2020 ◽  
pp. 127-143
Author(s):  
Alexander Miguel Monzon ◽  
András Hatos ◽  
Marco Necci ◽  
Damiano Piovesan ◽  
Silvio C. E. Tosatto
Keyword(s):  
Intrinsic Disorder ◽  
Protein Intrinsic Disorder

scholarly journals Hidden Structural Codes in Protein Intrinsic Disorder

2018 ◽  
Vol 114 (3) ◽  
pp. 592a
Author(s):  
Gonzalo de Prat Gay
Keyword(s):  
Intrinsic Disorder ◽  
Protein Intrinsic Disorder

Troponins, intrinsic disorder, and cardiomyopathy

2016 ◽  
Vol 397 (8) ◽  
pp. 731-751 ◽  
Author(s):  
Insung Na ◽  
Min J. Kong ◽  
Shelby Straight ◽  
Jose R. Pinto ◽  
Vladimir N. Uversky
Keyword(s):  
Posttranslational Modifications ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Troponin T ◽  
Intrinsic Disorder ◽  
Functional Changes ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Structural And Functional Properties ◽  
Protein Intrinsic Disorder

Abstract Cardiac troponin is a dynamic complex of troponin C, troponin I, and troponin T (TnC, TnI, and TnT, respectively) found in the myocyte thin filament where it plays an essential role in cardiac muscle contraction. Mutations in troponin subunits are found in inherited cardiomyopathies, such as hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM). The highly dynamic nature of human cardiac troponin and presence of numerous flexible linkers in its subunits suggest that understanding of structural and functional properties of this important complex can benefit from the consideration of the protein intrinsic disorder phenomenon. We show here that mutations causing decrease in the disorder score in TnI and TnT are significantly more abundant in HCM and DCM than mutations leading to the increase in the disorder score. Identification and annotation of intrinsically disordered regions in each of the troponin subunits conducted in this study can help in better understanding of the roles of intrinsic disorder in regulation of interactomes and posttranslational modifications of these proteins. These observations suggest that disease-causing mutations leading to a decrease in the local flexibility of troponins can trigger a whole plethora of functional changes in the heart.

Functional roles of intrinsic disorder in CRISPR-associated protein Cas9

2017 ◽  
Vol 13 (9) ◽  
pp. 1770-1780 ◽  
Author(s):  
Zhihua Du ◽  
Vladimir N. Uversky
Keyword(s):  
Dna Binding ◽  
Intrinsic Disorder ◽  
Dna Binding Proteins ◽  
Functional Roles ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
P Protein ◽  
Protein Intrinsic Disorder ◽  
Rna And Dna ◽  
Different Origin

Protein intrinsic disorder is an important characteristic commonly detected in multifunctional or RNA- and DNA-binding proteins. We show here that the CRISPR-associated Cas9 proteins of different origin contain functionally important intrinsically disordered regions.

scholarly journals Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii

2013 ◽  
Vol 9 (4) ◽  
pp. 645 ◽  
Author(s):  
Bin Xue ◽  
Victoria Jeffers ◽  
William J. Sullivan ◽  
Vladimir N. Uversky
Keyword(s):  
Toxoplasma Gondii ◽  
Intrinsic Disorder ◽  
Protein Intrinsic Disorder

HSF Transcription Factor Family, Heat Shock Response, and Protein Intrinsic Disorder

2012 ◽  
Vol 13 (1) ◽  
pp. 86-103 ◽  
Author(s):  
Sandy D. Westerheide ◽  
Rachel Raynes ◽  
Chase Powell ◽  
Bin Xue ◽  
Vladimir N. Uversky
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Intrinsic Disorder ◽  
Transcription Factor Family ◽  
Shock Response ◽  
Protein Intrinsic Disorder
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