TMPad

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TMPad

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

metasource: bio.tools
version: extracted_at: 2022-11-04T11:35:59.016197

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tmpad

metasource: bio.tools
version: extracted_at: 2022-11-04T11:35:59.016197

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Other names: tmpad

The TransMembrane Protein Helix-Packing Database (TMPad) is an integrated repository of experimentally determined structural folds derived from helix-helix interactions in alpha-helical membrane proteins. TMPad includes geometric descriptors of helix-helix interactions, topology, lipid accessibility, ligand and binding sites information. In addition, TMPad provides structural classification and visualization of the above structural features of TM helix-packing.

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TMPad: an integrated structural database for helix-packing folds in transmembrane proteins
PMID: 21177659

metasource: bio.tools
version: extracted_at: 2022-11-04T11:35:59.016197

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http://nar.oxfordjournals.org/content/39/suppl_1/D347

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

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• TMPad: an integrated structural database for helix-packing folds in transmembrane proteins PubMed citations: 11.

  11 articles citing: TMPad: an integrated structural database for helix-packing folds in transmembrane proteins

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  Current status of PTMs structural databases: applications, limitations and prospects. PMID:35020020

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  Joint-based description of protein structure: its application to the geometric characterization of membrane proteins. PMID:28432363

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  Phylogeny of the Vitamin K 2,3-Epoxide Reductase (VKOR) Family and Evolutionary Relationship to the Disulfide Bond Formation Protein B (DsbB) Family. PMID:26230708

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  The observation of evolutionary interaction pattern pairs in membrane proteins. PMID:25887048

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  The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions. PMID:25703378

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  Expediting topology data gathering for the TOPDB database. PMID:25392424

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  Probabilistic grammatical model for helix-helix contact site classification. PMID:24350601

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  topPTM: a new module of dbPTM for identifying functional post-translational modifications in transmembrane proteins. PMID:24302577

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  Functional investigation of transmembrane helix 3 in H⁺-translocating pyrophosphatase. PMID:24121627

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  Lipid exposure prediction enhances the inference of rotational angles of transmembrane helices. PMID:24112406

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  DbPTM 3.0: an informative resource for investigating substrate site specificity and functional association of protein post-translational modifications. PMID:23193290
• http://nar.oxfordjournals.org/content/39/suppl_1/D347

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protein sequence databases

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

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protein localization and targeting

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

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protein folds and structural domains

metasource: bio.tools
version: extracted_at: 2022-11-04T11:35:59.016197

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lipids

metasource: bio.tools
version: extracted_at: 2022-11-04T11:35:59.016197

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protein folding, stability and design

metasource: bio.tools
version: extracted_at: 2022-11-04T11:35:59.016197

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membrane and lipoproteins

metasource: bio.tools
version: extracted_at: 2022-11-04T11:35:59.016197

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protein structural motifs and surfaces

metasource: bio.tools
version: extracted_at: 2022-11-04T11:35:59.016197

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protein sequence protein localization and targeting protein folds and structural domains lipids protein folding, stability and design membrane and lipoproteins protein structural motifs and surfaces