Computational Identification of MoRFs in Protein Sequences Using Hierarchical Application of Bayes Rule

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Computational Identification of MoRFs in Protein Sequences Using Hierarchical Application of Bayes Rule is …
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scholarly articleQ13442814

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P819ADS bibcode2015PLoSO..1041603M
P356DOI10.1371/JOURNAL.PONE.0141603
P932PMC publication ID4627796
P698PubMed publication ID26517836
P5875ResearchGate publication ID283345876

P50authorNawar MalhisQ86630992
P2093author name stringJörg Gsponer
Eric T C Wong
Roy Nassar
P2860cites workPrediction of protein binding regions in disordered proteinsQ21145360
Classification of intrinsically disordered regions and proteinsQ22061736
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Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stressQ27937702
Overcome support vector machine diagnosis overfittingQ28082900
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The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins.Q52974739
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DISOPRED3: precise disordered region predictions with annotated protein-binding activityQ30633989
On the importance of polar interactions for complexes containing intrinsically disordered proteinsQ31129225
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Computational identification of MoRFs in protein sequencesQ34460669
The DISOPRED server for the prediction of protein disorderQ34546645
Getting the most from PSI-BLAST.Q34563343
Mining alpha-helix-forming molecular recognition features with cross species sequence alignmentsQ34708119
MFSPSSMpred: identifying short disorder-to-order binding regions in disordered proteins based on contextual local evolutionary conservationQ35008000
Intrinsically disordered proteins in cellular signalling and regulation.Q35510300
Characterization of molecular recognition features, MoRFs, and their binding partnersQ36944291
Intrinsically disordered proteins: regulation and diseaseQ37868137
Linear motifs: lost in (pre)translationQ38019262
Promiscuity as a functional trait: intrinsically disordered regions as central players of interactomesQ38132466
Intrinsically disordered proteins and intrinsically disordered protein regionsQ38194194
Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networksQ41884066
ESpritz: accurate and fast prediction of protein disorderQ44385437
Structure and intrinsic disorder in protein autoinhibition.Q45251643
Coupled folding and binding with alpha-helix-forming molecular recognition elementsQ48122045
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue10
P407language of work or nameEnglishQ1860
P921main subjectcomputational biologyQ177005
P304page(s)e0141603
P577publication date2015-10-30
P1433published inPLOS OneQ564954
P1476titleComputational Identification of MoRFs in Protein Sequences Using Hierarchical Application of Bayes Rule
P478volume10

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cites work (P2860)
Q55518742IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding.
Q63044066Improved measures for evolutionary conservation that exploit taxonomy distances
Q34526381MoRFchibi SYSTEM: software tools for the identification of MoRFs in protein sequences
Q92946510Portrait of the Intrinsically Disordered Side of the HTLV-1 Proteome
Q36268811Predicting MoRFs in protein sequences using HMM profiles.
Q97878176Understanding COVID-19 via comparative analysis of dark proteomes of SARS-CoV-2, human SARS and bat SARS-like coronaviruses

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