Mechanism-based probe for the analysis of cathepsin cysteine proteases in living cells.
about
Bioorthogonal chemistry: fishing for selectivity in a sea of functionalityNeisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasomeApplications of small molecule probes in dissecting mechanisms of bacterial virulence and host responsesLive imaging of cysteine-cathepsin activity reveals dynamics of focal inflammation, angiogenesis, and polyp growthOn the Mechanism of Dimethylarginine Dimethylaminohydrolase Inactivation by 4-HalopyridinesUsing small molecules to dissect mechanisms of microbial pathogenesis.Organelle-specific activity-based protein profiling in living cells.Comparative methods for analysis of protein covalent modification by electrophilic quinoids formed from xenobiotics.Cysteine-mediated redox signaling: chemistry, biology, and tools for discoveryDirect measurement of cathepsin B activity in the cytosol of apoptotic cells by an activity-based probe.Development of activity-based probes for cathepsin X.The Salmonella-containing vacuole: moving with the times.Bifunctional Probes of Cathepsin Protease Activity and pH Reveal Alterations in Endolysosomal pH during Bacterial Infection.Cysteine protease inhibition by nitrile-based inhibitors: a computational study.Natural products and their biological targets: proteomic and metabolomic labeling strategies.Staudinger ligation as a method for bioconjugation.Activity-based probes for the study of proteases: recent advances and developments.A cross-disciplinary perspective on the innate immune responses to bacterial lipopolysaccharideActivity-based protein profiling: recent advances in probe development and applications.Chemical approaches to discovery and study of sources and targets of hydrogen peroxide redox signaling through NADPH oxidase proteins.Comparative analysis of click chemistry mediated activity-based protein profiling in cell lysates.Howard Hang: posttranslational pathogenesis. Interview by Nicole LeBrasseur.A chemical approach for detecting sulfenic acid-modified proteins in living cells.A simple and effective cleavable linker for chemical proteomics applicationsAzido-BODIPY acid reveals quantitative Staudinger-Bertozzi ligation in two-step activity-based proteasome profilingSalmonella inhibits retrograde trafficking of mannose-6-phosphate receptors and lysosome function.Cleavable trifunctional biotin reagents for protein labelling, capture and release.Site-selective chemical modification of chymotrypsin using peptidyl derivatives bearing optically active diphenyl 1-amino-2-phenylethylphosphonate: Stereochemical effect of the diphenyl phosphonate moiety.Target identification reveals protein arginine methyltransferase 1 is a potential target of phenyl vinyl sulfone and its derivatives.
P2860
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P2860
Mechanism-based probe for the analysis of cathepsin cysteine proteases in living cells.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Mechanism-based probe for the analysis of cathepsin cysteine proteases in living cells.
@en
type
label
Mechanism-based probe for the analysis of cathepsin cysteine proteases in living cells.
@en
prefLabel
Mechanism-based probe for the analysis of cathepsin cysteine proteases in living cells.
@en
P2093
P356
P1433
P1476
Mechanism-based probe for the analysis of cathepsin cysteine proteases in living cells.
@en
P2093
Adrianus W M van der Velden
Annette M Pollington
Eric Spooner
Hidde L Ploegh
Howard C Hang
Joana Loureiro
Michael N Starnbach
Rene Maehr
You-Me Kim
P304
P356
10.1021/CB600431A
P577
2006-12-01T00:00:00Z