Prediction of protein deamidation rates from primary and three-dimensional structure.
about
Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligasesSolution structure and stability of the full-length excisionase from bacteriophage HK022Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditionsEmerging Roles of Protein Deamidation in Innate Immune SignalingInsight of brain degenerative protein modifications in the pathology of neurodegeneration and dementia by proteomic profilingControl of cellular Bcl-xL levels by deamidation-regulated degradationStructure-based prediction of asparagine and aspartate degradation sites in antibody variable regionsStructural effects of protein aging: terminal marking by deamidation in human triosephosphate isomerase.Structural features determining thermal adaptation of esterases.Deamidations in recombinant human phenylalanine hydroxylase. Identification of labile asparagine residues and functional characterization of Asn --> Asp mutant forms.Folding of a designed simple ankyrin repeat protein.Effects of spontaneous deamidation on the cytotoxic activity of the Bacillus anthracis protective antigen.Evidence of the involvement of asparagine deamidation in the formation of cyclodextrin glycosyltransferase isoforms in Paenibacillus sp. RB01.Widespread Occurrence of Non-Enzymatic Deamidations of Asparagine Residues in Yersinia pestis Proteins Resulting from Alkaline pH Membrane Extraction Conditions.Deamidation of human proteins.Protein deamidationAge estimation of museum wool textiles from Ovis aries using deamidation rates utilizing matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.Top-down study of β2-microglobulin deamidationBiochemical, molecular characterization, and glycoproteomic analyses of alpha(1)-proteinase inhibitor products used for replacement therapy.An alternative view of the proposed alternative activities of hemopexin.Electron transfer dissociation with supplemental activation to differentiate aspartic and isoaspartic residues in doubly charged peptide cations.Albinism-causing mutations in recombinant human tyrosinase alter intrinsic enzymatic activity.Prediction of Spontaneous Protein Deamidation from Sequence-Derived Secondary Structure and Intrinsic Disorder.Mildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease Glu-C at pH 4.5.Asparagine deamidation reduces DNA-binding affinity of the Drosophila melanogaster Scr homeodomain.Deamidation: Differentiation of aspartyl from isoaspartyl products in peptides by electron capture dissociation.Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometryEffect of N-1 and N-2 residues on peptide deamidation rate in solution and solid state.High-resolution MS for structural characterization of protein therapeutics: advances and future directions.Differentiating N-terminal aspartic and isoaspartic acid residues in peptides.Quantification of biopharmaceuticals and biomarkers in complex biological matrices: a comparison of liquid chromatography coupled to tandem mass spectrometry and ligand binding assays.Protein asparagine deamidation prediction based on structures with machine learning methodsBiopharmaceutical Informatics: supporting biologic drug development via molecular modelling and informatics.From chemical metabolism to life: the origin of the genetic coding process.Glutamine deamidation: an indicator of antiquity, or preservational quality?Deamidation of Human γS-Crystallin Increases Attractive Protein Interactions: Implications for Cataract.Deamidation accelerates amyloid formation and alters amylin fiber structureAntifragility and Tinkering in Biology (and in Business) Flexibility Provides an Efficient Epigenetic Way to Manage Risk.Increasing the productivity of glycopeptides analysis by using higher-energy collision dissociation-accurate mass-product-dependent electron transfer dissociation.Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
P2860
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P2860
Prediction of protein deamidation rates from primary and three-dimensional structure.
description
2001 nî lūn-bûn
@nan
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Prediction of protein deamidation rates from primary and three-dimensional structure.
@ast
Prediction of protein deamidation rates from primary and three-dimensional structure.
@en
type
label
Prediction of protein deamidation rates from primary and three-dimensional structure.
@ast
Prediction of protein deamidation rates from primary and three-dimensional structure.
@en
prefLabel
Prediction of protein deamidation rates from primary and three-dimensional structure.
@ast
Prediction of protein deamidation rates from primary and three-dimensional structure.
@en
P2860
P356
P1476
Prediction of protein deamidation rates from primary and three-dimensional structure.
@en
P2093
Robinson AB
Robinson NE
P2860
P304
P356
10.1073/PNAS.071066498
P407
P577
2001-04-01T00:00:00Z