about
Neighbor-dependent Ramachandran probability distributions of amino acids developed from a hierarchical Dirichlet process modelMolecular cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivoD-strand perturbation and amyloid propensity in beta-2 microglobulinA novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomesMolecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASPThe structure and function of proline-rich regions in proteinsMutations of the KISS1 gene in disorders of pubertyCrystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolutionDiscovery of active proteins directly from combinatorial randomized protein libraries without display, purification or sequencing: identification of novel zinc finger proteinsStatistically significant dependence of the Xaa-Pro peptide bond conformation on secondary structure and amino acid sequenceThe Ramachandran plots of glycine and pre-prolineRole of proline in cell wall synthesis and plant development and its implications in plant ontogenyThe solution structure of the anti-HIV chemokine vMIP-IIThe NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micellesVisualization of a water-selective pore by electron crystallography in vitreous iceModel peptide studies of sequence regions in the elastomeric biomineralization protein, Lustrin A. I. The C-domain consensus-PG-, -NVNCT-motifStructural consequences of replacement of an alpha-helical Pro residue in Escherichia coli thioredoxinCrystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolutionCrystal structure of a defective folding proteinThe conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroniStructure of putative CutA1 fromHomo sapiensdetermined at 2.05 Å resolutionThe mechanism of domain alternation in the acyl-adenylate forming ligase superfamily member 4-chlorobenzoate: coenzyme A ligaseNMR Structure of the Human Prion Protein with the Pathological Q212P Mutation Reveals Unique Structural FeaturesStructural characterization of human S100A16, a low-affinity calcium binderNMR studies of the solution conformation of the sex peptide from Drosophila melanogasterLong-range Electrostatic Complementarity Governs Substrate Recognition by Human Chymotrypsin C, a Key Regulator of Digestive Enzyme ActivationThe paradox of conformational constraint in the design of Cbl(TKB)-binding peptidesCrystal structure of a putative isochorismatase hydrolase from Oleispira antarctica.Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline IsomerizationEngineered thermostable fungal Cel6A and Cel7A cellobiohydrolases hydrolyze cellulose efficiently at elevated temperaturesConformational diversity in contryphans from Conus venom: cis-trans isomerisation and aromatic/proline interactions in the 23-membered ring of a 7-residue peptide disulfide loopStructure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27Solution structure of the epsilon-aminohexanoic acid complex of human plasminogen kringle 1Determination of the structure of the N-terminal splice region of the cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and identification of the membrane association domain using chimeric constructsCrystal structure of a recombinant form of the maltodextrin-binding protein carrying an inserted sequence of a B-cell epitope from the preS2 region of hepatitis B virusALK mutations conferring differential resistance to structurally diverse ALK inhibitors.C terminus of Nce102 determines the structure and function of microdomains in the Saccharomyces cerevisiae plasma membraneCo- and Post-Translational Protein Folding in the ERThe emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's diseasePost-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo
P2860
Q21145340-435E6E10-57C2-487E-8754-FB5BCDCD3428Q24291116-EF24B217-B10E-4CC9-8D25-87A3860CBA97Q24302181-04346D07-E3B1-4118-8111-4F24450E37A5Q24304237-C19DBB69-CED4-4A2E-A11C-C5A9060C1572Q24310239-DCF37EA5-DD4C-4DEB-9AAE-104FBD9BBB3BQ24528663-FF36EC4D-E990-4851-8CCD-2F3F4A424B2EQ24618754-701A4E12-5966-499F-9316-4B93A8914272Q24683205-243B2E45-BECE-4581-BB71-706E58F49281Q24792033-5A3CC1EA-531D-4DE7-AA41-8669342FBF50Q24794977-335AED73-2E80-43EC-AAF9-211EC939F832Q24812279-B9DFD190-213F-4C77-A099-9278AF87209CQ26800108-DAE7127C-03F9-4EEA-B32A-E33381DCD0EBQ27620649-76C58CB9-F7BD-4571-B093-A9E473877F97Q27621702-9AF7CE4A-807A-4C09-81C7-744990FF8F13Q27629440-34C4C53E-BA11-4DB4-9521-97B17554BFDDQ27638630-91F4D9C7-536B-431D-ACD4-B03F886FB093Q27639736-625A0AD2-9ACE-462A-AB5F-7C413D3B9DD6Q27640295-E49E533F-BEF4-4E39-904A-2BF61208CA03Q27640520-3A3BB9B5-89E5-4841-91EB-3B0C4DA1A42DQ27641652-A9CA816E-EA36-46EE-91CA-657753B2824CQ27650517-F2688038-B1F1-49AB-89C9-026215B3D2BDQ27654352-29AB3D2A-78AB-466F-9BCE-296C64ED8FA7Q27663617-FF787093-F346-4587-968E-6730A26A279DQ27665571-E16EDE8E-BCA4-4BCE-90DD-F30AD3CDFD4DQ27667110-297CBEC2-39AE-452C-9B40-40AADCB6B9E7Q27676497-AA0C9CEF-B183-472D-B5D3-8B9A4ECF9991Q27677282-9DF4ACC1-203A-485C-B73F-FEE1FABA1B43Q27677386-AF3E6502-AAD9-40FB-89B7-8E21FB53C86BQ27679204-C2416E04-635E-40E2-92F4-7285662BC10CQ27683987-FD591B11-71AB-473A-B3A7-8CB3821A32C6Q27687104-FFFAB142-C704-4D63-BB7D-906B78DC8A1BQ27696314-7B74E3B9-FD70-4B97-9E26-B9FA63FED592Q27731320-6487607B-03EB-4D18-A450-9F34C0A5CCCFQ27732838-872FA10C-DD13-4D40-98FE-024F06C34CB2Q27734823-B3621975-BB4D-4B9F-B414-FC8252F0540FQ27851672-5FFCB7E7-D7CA-4AC3-80C5-1BFD9C94C661Q27933760-124328A8-E6FF-4505-B2D3-FF93CC480A32Q28078736-6759363E-E609-4214-93F3-2E1891248951Q28085108-9973C83F-D46A-4310-B6B8-64B3C26D6859Q28141258-20A9B8DF-2ADE-462C-BD42-A1CC205A171E
P2860
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh-hant
name
Influence of proline residues on protein conformation.
@en
Influence of proline residues on protein conformation.
@nl
type
label
Influence of proline residues on protein conformation.
@en
Influence of proline residues on protein conformation.
@nl
prefLabel
Influence of proline residues on protein conformation.
@en
Influence of proline residues on protein conformation.
@nl
P1476
Influence of proline residues on protein conformation.
@en
P2093
MacArthur MW
P304
P356
10.1016/0022-2836(91)90721-H
P407
P577
1991-03-01T00:00:00Z