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z-VAD-fmk inhibits peptide:N-glycanase and may result in ER stress

descriptionPublicationkeyboard_double_arrow_right Article 08 Jul 2005 United Kingdom Publisher:Springer Science and Business Media LLCJournal:Cell Death & Differentiation, volume 13, pages 163-165 (issn: 1350-9047, eissn: 1476-5403,

Authors: Gregory A. Korbel; Eric Spooner; Benedikt M. Kessler; Benedikt M. Kessler; Shahram Misaghi; Hidde L. Ploegh;

doi: 10.1038/sj.cdd.4401716

pmid: 16003388

z-VAD-fmk inhibits peptide:N-glycanase and may result in ER stress

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Country

United Kingdom

Related Organizations

Harvard University
United States
University of Oxford
United Kingdom
University of Oxford
United Kingdom

Keywords

Binding Sites, Sequence Homology, Amino Acid, Molecular Sequence Data, Saccharomyces cerevisiae, Endoplasmic Reticulum, Caspase Inhibitors, Peptide Mapping, Amino Acid Chloromethyl Ketones, Mice, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Animals, Humans, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Amino Acid Sequence, Enzyme Inhibitors

1 Research products, page 1 of 1

Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
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	citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	39
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	influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	Top 10%
	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Top 10%