ComSin

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ComSin

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

metasource: bio.tools
version: extracted_at: 2022-11-04T11:33:56.409468

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comsin

metasource: bio.tools
version: extracted_at: 2022-11-04T11:33:56.409468

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Other names: comsin

Protein structures in bound and unbound states

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Publications

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ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder
PMID: 19906708

metasource: bio.tools
version: extracted_at: 2022-11-04T11:33:56.409468

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http://nar.oxfordjournals.org/content/38/suppl_1/D283

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

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• ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder PubMed citations: 19.

  19 articles citing: ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder

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  D3PM: a comprehensive database for protein motions ranging from residue to domain. PMID:35164668

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  The challenge of ORF1p phosphorylation: Effects on L1 activity and its host. PMID:27066302

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  CCProf: exploring conformational change profile of proteins. PMID:27016699

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  Amino Acids in Nine Ligand-Prefer Ramachandran Regions. PMID:26491686

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  Protein flexibility in the light of structural alphabets. PMID:26075209

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  Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. PMID:25988147

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  Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling. PMID:25510932

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  Structural interface parameters are discriminatory in recognising near-native poses of protein-protein interactions. PMID:24498255

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  IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners. PMID:24178034

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  Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes. PMID:23364837

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  An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites. PMID:23075227

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  Structure fluctuations and conformational changes in protein binding. PMID:22809338

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  Comparison of tertiary structures of proteins in protein-protein complexes with unbound forms suggests prevalence of allostery in signalling proteins. PMID:22554255

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  AH-DB: collecting protein structure pairs before and after binding. PMID:22084200

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  Disordered patterns in clustered Protein Data Bank and in eukaryotic and bacterial proteomes. PMID:22073276

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  Intrinsic protein disorder in human pathways. PMID:22012032

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  Expanding the proteome: disordered and alternatively folded proteins. PMID:21729349

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  CSpritz: accurate prediction of protein disorder segments with annotation for homology, secondary structure and linear motifs. PMID:21646342

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  Intrinsic disorder and protein multibinding in domain, terminal, and linker regions. PMID:20544079
• http://nar.oxfordjournals.org/content/38/suppl_1/D283

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structure databases

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

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protein structure

metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657

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proteins

metasource: bio.tools
version: extracted_at: 2022-11-04T11:33:56.409468

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protein structure analysis

metasource: bio.tools
version: extracted_at: 2022-11-04T11:33:56.409468

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protein disordered structure

metasource: bio.tools
version: extracted_at: 2022-11-04T11:33:56.409468

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protein folds and structural domains

metasource: bio.tools
version: extracted_at: 2022-11-04T11:33:56.409468

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sequence composition, complexity and repeats

metasource: bio.tools
version: extracted_at: 2022-11-04T11:33:56.409468

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structure protein structure proteins protein structure analysis protein disordered structure protein folds and structural domains sequence composition, complexity and repeats