Mutual Folding Induced by Binding Database
Names
More detailed information about this field from each metasource.
Mutual Folding Induced by Binding Database
metasource: Fairsharing.org
version: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
MFIB
metasource: Fairsharing.org
version: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Names
More detailed information about this field from each metasource.
Mutual Folding Induced by Binding Database
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
MFIB
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Names
More detailed information about this field from each metasource.
Mutual Folding Induced by Binding Database
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
MFIB
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Mutual Folding Induced by Binding (MFIB) is a repository of protein complexes for which the folding of each constituent protein chain is coupled to the interaction forming the complex. This means that while the complexes are stable enough to have their structures solved by conventional structure determination methods (such as X-ray or NMR), the proteins or protein regions involved in the interaction do not have a stable structure in their free monomeric form (i.e. they are intrinsically disordered/unstructured).
Description
More detailed information about this field from each metasource.
Mutual Folding Induced by Binding (MFIB) is a repository of protein complexes for which the folding of each constituent protein chain is coupled to the interaction forming the complex. This means that while the complexes are stable enough to have their structures solved by conventional structure determination methods (such as X-ray or NMR), the proteins or protein regions involved in the interaction do not have a stable structure in their free monomeric form (i.e. they are intrinsically disordered/unstructured).
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Webpage:
http://mfib.enzim.ttk.mta.huWebpage
More detailed information about this field from each metasource.
http://mfib.enzim.ttk.mta.hu
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Licence:
Name: MFIB Free for academic and non-profit useLicence name
More detailed information about this field from each metasource.
MFIB Free for academic and non-profit use
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Licence URL
More detailed information about this field from each metasource.
http://mfib.enzim.ttk.mta.hu/help.php
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Publications:
Publications
More detailed information about this field from each metasource.
MFIB: a repository of protein complexes with mutual folding induced by binding
PMID: 29036655
metasource: Fairsharing.org
version: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Publications
More detailed information about this field from each metasource.
MFIB: a repository of protein complexes with mutual folding induced by binding
PMID: 29036655
metasource: Fairsharing.org
version: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
-
MFIB: a repository of protein complexes with mutual folding induced by binding
PubMed citations: 34.
34 articles citing: MFIB: a repository of protein complexes with mutual folding induced by binding
Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions. PMID:35883444
IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures. PMID:35883018
Genetic variation associated with condensate dysregulation in disease. PMID:35809564
Predicting Protein Conformational Disorder and Disordered Binding Sites. PMID:35507260
Deep learning in prediction of intrinsic disorder in proteins. PMID:35356546
Characterization of intrinsically disordered regions in proteins informed by human genetic diversity. PMID:35275927
Databases for intrinsically disordered proteins. PMID:35102880
Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins. PMID:34948202
IUPred3: prediction of protein disorder enhanced with unambiguous experimental annotation and visualization of evolutionary conservation. PMID:34048569
Critical assessment of protein intrinsic disorder prediction. PMID:33875885
Mutations of Intrinsically Disordered Protein Regions Can Drive Cancer but Lack Therapeutic Strategies. PMID:33806614
PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins. PMID:33305318
A Suggestion of Converting Protein Intrinsic Disorder to Structural Entropy Using Shannon's Information Theory. PMID:33267305
MobiDB: intrinsically disordered proteins in 2021. PMID:33237329
The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes. PMID:33119751
Chasing coevolutionary signals in intrinsically disordered proteins complexes. PMID:33087759
Identification of Intrinsic Disorder in Complexes from the Protein Data Bank. PMID:32743159
Exploring Protein Intrinsic Disorder with MobiDB. PMID:32696355
How to Annotate and Submit a Short Linear Motif to the Eukaryotic Linear Motif Resource. PMID:32696353
Experimentally Determined Long Intrinsically Disordered Protein Regions Are Now Abundant in the Protein Data Bank. PMID:32599863
Conditional Disorder in Small Heat-shock Proteins. PMID:32081587
Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins. PMID:32020911
Macromolecular Interactions of Disordered Proteins. PMID:31941113
Modeling beta-sheet peptide-protein interactions: Rosetta FlexPepDock in CAPRI rounds 38-45. PMID:31891416
DisProt: intrinsic protein disorder annotation in 2020. PMID:31713636
Sequence and Structure Properties Uncover the Natural Classification of Protein Complexes Formed by Intrinsically Disordered Proteins via Mutual Synergistic Folding. PMID:31683980
Analysis of Heterodimeric "Mutual Synergistic Folding"-Complexes. PMID:31623284
Where differences resemble: sequence-feature analysis in curated databases of intrinsically disordered proteins. PMID:30576490
The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer. PMID:30563168
Physical Background of the Disordered Nature of "Mutual Synergetic Folding" Proteins. PMID:30373142
Decision-Tree Based Meta-Strategy Improved Accuracy of Disorder Prediction and Identified Novel Disordered Residues Inside Binding Motifs. PMID:30301243
IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding. PMID:29860432
DIBS: a repository of disordered binding sites mediating interactions with ordered proteins. PMID:29385418
MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins. PMID:29136219
Tags:
Tags
More detailed information about this field from each metasource.
intrinsically disordered proteins
metasource: Fairsharing.org
version: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
protein interaction
metasource: Fairsharing.org
version: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
protein structure
metasource: Fairsharing.org
version: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Tags
More detailed information about this field from each metasource.
intrinsically disordered proteins
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
protein interaction
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
protein structure
metasource: Fairsharing.orgversion: FAIRsharing.org: MFIB; Mutual Folding Induced by Binding Database; DOI: https://doi.org/10.25504/FAIRsharing.bwswdf; Last edited: April 27, 2021, 7:37 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
intrinsically disordered proteins protein interaction protein structure
Need help integrating and/or managing biomedical data?