Global identification of peptidase specificity by multiplex substrate profiling. - Wikidata - wikimedia - TriplyDB

Global identification of peptidase specificity by multiplex substrate profiling.

Global identification of peptidase specificity by multiplex substrate profiling.

http://www.wikidata.org/entity/Q34424750

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The Dipeptidyl Peptidase Family, Prolyl Oligopeptidase, and Prolyl Carboxypeptidase in the Immune System and Inflammatory Disease, Including Atherosclerosis Cysteine and Aspartyl Proteases Contribute to Protein Digestion in the Gut of Freshwater Planaria Global substrate profiling of proteases in human neutrophil extracellular traps reveals consensus motif predominantly contributed by elastase Substrate-driven mapping of the degradome by comparison of sequence logos Characterizing Protease Specificity: How Many Substrates Do We Need?Proteome-derived peptide libraries to study the substrate specificity profiles of carboxypeptidases.Determinants of Macromolecular Specificity from Proteomics-Derived Peptide Substrate Data.Identification of Protease Specificity Using Biotin-Labeled Substrates.The Rational Design of Therapeutic Peptides for Aminopeptidase N using a Substrate-Based Approach.Carboxypeptidases in disease: insights from peptidomic studies.Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis.Dissecting the active site of the collagenolytic cathepsin L3 protease of the invasive stage of Fasciola hepatica.Imaging active urokinase plasminogen activator in prostate cancer.Destructin-1 is a collagen-degrading endopeptidase secreted by Pseudogymnoascus destructans, the causative agent of white-nose syndrome.Protease substrate profiling using bacterial display of self-blocking affinity proteins and flow-cytometric sorting.Integrated Activity and Genetic Profiling of Secreted Peptidases in Cryptococcus neoformans Reveals an Aspartyl Peptidase Required for Low pH Survival and Virulence.Multiplex Substrate Profiling by Mass Spectrometry for Kinases as a Method for Revealing Quantitative Substrate Motifs.Evolutionary Selection on Barrier Activity: Bar1 Is an Aspartyl Protease with Novel Substrate Specificity.Excretion/secretion products from Schistosoma mansoni adults, eggs and schistosomula have unique peptidase specificity profiles.Structure- and function-based design of Plasmodium-selective proteasome inhibitors Quantitative MS-based enzymology of caspases reveals distinct protein substrate specificities, hierarchies, and cellular roles.Global Identification of Biofilm-Specific Proteolysis in Candida albicans.Design of Selective Substrates and Activity-Based Probes for Hydrolase Important for Pathogenesis 1 (HIP1) from Mycobacterium tuberculosis.Proteomic identification of protease cleavage sites: cell-biological and biomedical applications.Proteases and proteomics: cutting to the core of human skin pathologies.Substrate Profiling and High Resolution Co-complex Crystal Structure of a Secreted C11 Protease Conserved across Commensal Bacteria.Pathophysiological roles of proteases in gastrointestinal disease.Procathepsin E is highly abundant but minimally active in pancreatic ductal adenocarcinoma tumors.Emerging challenges in the design of selective substrates, inhibitors and activity-based probes for indistinguishable proteases.Targeting proteasomes in infectious organisms to combat disease.Caspases and their substrates.Specificity determinants for autoproteolysis of LexA, a key regulator of bacterial SOS mutagenesis.Full genome analysis of enterovirus D-68 strains circulating in Alberta, Canada.Monitoring proteolytic processing events by quantitative mass spectrometry.A novel outbreak enterovirus D68 strain associated with acute flaccid myelitis cases in the USA (2012-14): a retrospective cohort study.Block-based characterization of protease specificity from substrate sequence profile.Specificity of a protein-protein interface: local dynamics direct substrate recognition of effector caspases.Immunoproteasome functions explained by divergence in cleavage specificity and regulation.Complementary Proteomic and Biochemical Analysis of Peptidases in Lobster Gastric Juice Uncovers the Functional Role of Individual Enzymes in Food Digestion.Global substrate specificity profiling of post-translational modifying enzymes.

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P2860

Global identification of peptidase specificity by multiplex substrate profiling.

http://www.wikidata.org/entity/Q34424750

description

2012 nî lūn-bûn

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2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Global identification of peptidase specificity by multiplex substrate profiling.

@ast

Global identification of peptidase specificity by multiplex substrate profiling.

@en

Global identification of peptidase specificity by multiplex substrate profiling.

@nl

type

label

Global identification of peptidase specificity by multiplex substrate profiling.

@ast

Global identification of peptidase specificity by multiplex substrate profiling.

@en

Global identification of peptidase specificity by multiplex substrate profiling.

@nl

prefLabel

Global identification of peptidase specificity by multiplex substrate profiling.

@ast

Global identification of peptidase specificity by multiplex substrate profiling.

@en

Global identification of peptidase specificity by multiplex substrate profiling.

@nl

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Global identification of peptidase specificity by multiplex substrate profiling.

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A Alegra Eroy-Reveles

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Alexander L Greninger

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Alma L Burlingame

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Anthony J O'Donoghue

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Charles S Craik

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Daniel R Hostetter

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David A Maltby

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Gang Qu

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Jacob B Statnekov

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Jessica Ingram

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P2860

MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini

Characterization of structural determinants of granzyme B reveals potent mediators of extended substrate specificity

Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry

A model for random sampling and estimation of relative protein abundance in shotgun proteomics

Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics

Determination of protease cleavage site motifs using mixture-based oriented peptide libraries.

Cercarial elastase is encoded by a functionally conserved gene family across multiple species of schistosomes.

Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries

Significance analysis of spectral count data in label-free shotgun proteomics

P2888

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1095-1100

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10.1038/NMETH.2182

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11

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9

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Giselle M. Knudsen

James H McKerrow

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2012-09-30T00:00:00Z

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231613267

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1045616754

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23023596

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3707110

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