Global kinetic analysis of proteolysis via quantitative targeted proteomics. - Wikidata - awgldk - TriplyDB

Global kinetic analysis of proteolysis via quantitative targeted proteomics.

Global kinetic analysis of proteolysis via quantitative targeted proteomics.

http://www.wikidata.org/entity/Q35751043

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Recent advances in quantitative neuroproteomics Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation Advances in targeted proteomics and applications to biomedical research STL-based analysis of TRAIL-induced apoptosis challenges the notion of type I/type II cell line classification Sequence and conformational specificity in substrate recognition: several human Kunitz protease inhibitor domains are specific substrates of mesotrypsin.An unbiased proteomic screen reveals caspase cleavage is positively and negatively regulated by substrate phosphorylation Circulating proteolytic signatures of chemotherapy-induced cell death in humans discovered by N-terminal labeling.Parallel reaction monitoring for high resolution and high mass accuracy quantitative, targeted proteomics.Basis for substrate recognition and distinction by matrix metalloproteinases Inverse metabolic engineering to improve Escherichia coli as an N-glycosylation host.Global analysis of cellular proteolysis by selective enzymatic labeling of protein N-termini.Downregulation of microRNA-9 in iPSC-derived neurons of FTD/ALS patients with TDP-43 mutations.Importance of extended protease substrate recognition motifs in steering BNIP-2 cleavage by human and mouse granzymes B.Engineered cellular gene-replacement platform for selective and inducible proteolytic profiling.The N-end rule pathway counteracts cell death by destroying proapoptotic protein fragments A transposable element in a NAC gene is associated with drought tolerance in maize seedlings Quantitative profiling of caspase-cleaved substrates reveals different drug-induced and cell-type patterns in apoptosis.A Small Molecule that Induces Intrinsic Pathway Apoptosis with Unparalleled Speed.Conservation of caspase substrates across metazoans suggests hierarchical importance of signaling pathways over specific targets and cleavage site motifs in apoptosis Augmented generation of protein fragments during wakefulness as the molecular cause of sleep: a hypothesis.Substrates of IAP ubiquitin ligases identified with a designed orthogonal E3 ligase, the NEDDylator The DegraBase: a database of proteolysis in healthy and apoptotic human cells Quantitative MS-based enzymology of caspases reveals distinct protein substrate specificities, hierarchies, and cellular roles.Chloroquine interference with hemoglobin endocytic trafficking suppresses adaptive heme and iron homeostasis in macrophages: the paradox of an antimalarial agent.Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition.Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.Global cellular response to chemotherapy-induced apoptosis.Proteolytic post-translational modification of proteins: proteomic tools and methodology.Time-resolved analysis of the matrix metalloproteinase 10 substrate degradome.Interactome disassembly during apoptosis occurs independent of caspase cleavage.Considerations on selected reaction monitoring experiments: implications for the selectivity and accuracy of measurements.Opportunities for protein interaction network-guided cellular engineering.Proteomic identification of protease cleavage sites: cell-biological and biomedical applications.Profiling proteoforms: promising follow-up of proteomics for biomarker discovery.Colorectal cancer biomarker discovery and validation using LC-MS/MS-based proteomics in blood: truth or dare?Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform.Substrate Profiling and High Resolution Co-complex Crystal Structure of a Secreted C11 Protease Conserved across Commensal Bacteria.Multiplexed Liquid Chromatography-Multiple Reaction Monitoring Mass Spectrometry Quantification of Cancer Signaling Proteins.Comparative Analysis of Mitochondrial N-Termini from Mouse, Human, and Yeast.A SILAC-based approach identifies substrates of caspase-dependent cleavage upon TRAIL-induced apoptosis.

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P2860

Global kinetic analysis of proteolysis via quantitative targeted proteomics.

http://www.wikidata.org/entity/Q35751043

description

2012 nî lūn-bûn

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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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2012年论文

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name

Global kinetic analysis of proteolysis via quantitative targeted proteomics.

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Global kinetic analysis of proteolysis via quantitative targeted proteomics.

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type

label

Global kinetic analysis of proteolysis via quantitative targeted proteomics.

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Global kinetic analysis of proteolysis via quantitative targeted proteomics.

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prefLabel

Global kinetic analysis of proteolysis via quantitative targeted proteomics.

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Global kinetic analysis of proteolysis via quantitative targeted proteomics.

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Proceedings of the National Academy of Sciences of the United States of America

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Global kinetic analysis of proteolysis via quantitative targeted proteomics.

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Aenoch Lynn

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James A Wells

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Jonathan C Trinidad

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P2860

Specific involvement of caspases in the differentiation of monocytes into macrophages

Global mapping of the topography and magnitude of proteolytic events in apoptosis

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

GoMiner: a resource for biological interpretation of genomic and proteomic data

Dimer formation drives the activation of the cell death protease caspase 9

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

A method to describe enzyme-catalyzed reactions by combining steady state and time course enzyme kinetic parameters

Modeling a snap-action, variable-delay switch controlling extrinsic cell death

Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents

A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis

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