scholarly article | Q13442814 |
P50 | author | Jianyi Yang | Q50864275 |
Vladimir N. Uversky | Q59698496 | ||
Lukasz Kurgan | Q39632517 | ||
P2093 | author name string | Gang Hu | |
Zhonghua Wu | |||
Zhenling Peng | |||
P2860 | cites work | Prediction of protein binding regions in disordered proteins | Q21145360 |
Intrinsically unstructured proteins and their functions | Q22061731 | ||
Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life | Q22061741 | ||
The Protein Data Bank | Q24515306 | ||
DisProt: the Database of Disordered Proteins | Q24675789 | ||
SIFTS: Structure Integration with Function, Taxonomy and Sequences resource | Q27614957 | ||
Intrinsically disordered protein | Q28191444 | ||
Disordered proteinaceous machines | Q28652765 | ||
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm | Q29615865 | ||
IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content | Q29615888 | ||
Intrinsic disorder and protein function | Q29616415 | ||
Natively unfolded proteins: a point where biology waits for physics | Q29616416 | ||
The protein trinity--linking function and disorder. | Q52055900 | ||
Disorder and sequence repeats in hub proteins and their implications for network evolution. | Q52673882 | ||
Signal transduction via unstructured protein conduits. | Q53491312 | ||
Accurate prediction of disorder in protein chains with a comprehensive and empirically designed consensus | Q56992931 | ||
NOT THAT RIGID MIDGETS AND NOT SO FLEXIBLE GIANTS: ON THE ABUNDANCE AND ROLES OF INTRINSIC DISORDER IN SHORT AND LONG PROTEINS | Q56993044 | ||
Coupling of folding and binding for unstructured proteins | Q29616417 | ||
Activities at the Universal Protein Resource (UniProt) | Q29617787 | ||
The interplay between structure and function in intrinsically unstructured proteins. | Q30350853 | ||
Algorithmic approaches to protein-protein interaction site prediction. | Q30372092 | ||
The unfoldomics decade: an update on intrinsically disordered proteins. | Q30372413 | ||
Understanding protein non-folding. | Q30385084 | ||
Data mining in bioinformatics using Weka | Q30920089 | ||
Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes | Q33252616 | ||
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners | Q33325589 | ||
What's in a name? Why these proteins are intrinsically disordered: Why these proteins are intrinsically disordered | Q33656573 | ||
Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes | Q33737866 | ||
What does it mean to be natively unfolded? | Q34488954 | ||
Intrinsic disorder in scaffold proteins: getting more from less | Q34594105 | ||
Identification and functions of usefully disordered proteins | Q34989882 | ||
Folding and assembly of oligomeric proteins in Escherichia coli | Q35303063 | ||
The relationship between proteome size, structural disorder and organism complexity | Q35907671 | ||
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling | Q36226283 | ||
Mechanism and evolution of protein dimerization | Q36280901 | ||
BioLiP: a semi-manually curated database for biologically relevant ligand-protein interactions | Q36491539 | ||
Conservation of intrinsic disorder in protein domains and families: II. functions of conserved disorder | Q36869604 | ||
Intrinsic disorder in transcription factors | Q36882145 | ||
TOP-IDP-scale: a new amino acid scale measuring propensity for intrinsic disorder | Q37178764 | ||
ANCHOR: web server for predicting protein binding regions in disordered proteins. | Q37381486 | ||
The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome | Q37462521 | ||
Intrinsic disorder-based protein interactions and their modulators | Q38061459 | ||
Unusual biophysics of intrinsically disordered proteins | Q38069936 | ||
On the use of knowledge-based potentials for the evaluation of models of protein-protein, protein-DNA, and protein-RNA interactions. | Q38195952 | ||
Protein function prediction using domain families | Q38491331 | ||
Domain-based and family-specific sequence identity thresholds increase the levels of reliable protein function transfer | Q40011178 | ||
Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life | Q42211815 | ||
What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae? | Q42625650 | ||
ESpritz: accurate and fast prediction of protein disorder | Q44385437 | ||
A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome | Q46337513 | ||
Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers | Q47609385 | ||
More than just tails: intrinsic disorder in histone proteins | Q48050089 | ||
P433 | issue | 19 Pt A | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 2561-2569 | |
P577 | publication date | 2015-08-19 | |
P1433 | published in | FEBS Letters | Q1388051 |
P1476 | title | In various protein complexes, disordered protomers have large per-residue surface areas and area of protein-, DNA- and RNA-binding interfaces. | |
P478 | volume | 589 |
Q99604815 | Comprehensive Survey and Comparative Assessment of RNA-Binding Residue Predictions with Analysis by RNA Type |
Q63740433 | Computational Prediction of MoRFs, Short Disorder-to-order Transitioning Protein Binding Regions |
Q46607962 | Deciphering the cause of evolutionary variance within intrinsically disordered regions in human proteins |
Q47351608 | Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions. |
Q45046029 | Prediction of Disordered RNA, DNA, and Protein Binding Regions Using DisoRDPbind |
Q90064926 | SCRIBER: accurate and partner type-specific prediction of protein-binding residues from proteins sequences |
Q91708289 | Sequence-Derived Markers of Drug Targets and Potentially Druggable Human Proteins |
Q61486100 | The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity |
Q97878176 | Understanding COVID-19 via comparative analysis of dark proteomes of SARS-CoV-2, human SARS and bat SARS-like coronaviruses |
Search more.