Mass spectrometry captures off-target drug binding and provides mechanistic insights into the human metalloprotease ZMPSTE24

Nature Chemistry

Volumn 8, Issue 12, 2016, Pages 1152-1158

  Mehmood, Shahid ^a   Marcoux, Julien ^a   Gault, Joseph ^a   Quigley, Andrew ^b   Michaelis, Susan ^c   Young, Stephen G ^d   Carpenter, Elisabeth P ^b   Robinson, Carol V ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DRUG; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; LAMIN A; LIPID; MEMBRANE PROTEIN; METALLOPROTEINASE; PRELAMIN A; PROTEIN BINDING; ZINC; ZMPSTE24 PROTEIN, HUMAN;

ANTAGONISTS AND INHIBITORS; CHEMISTRY; ENZYME SPECIFICITY; HUMAN; MASS SPECTROMETRY; METABOLISM; PROTEIN PRENYLATION;

HIV PROTEASE INHIBITORS; HUMANS; LAMIN TYPE A; LIPIDS; MASS SPECTROMETRY; MEMBRANE PROTEINS; METALLOENDOPEPTIDASES; PHARMACEUTICAL PREPARATIONS; PROTEIN BINDING; PROTEIN PRENYLATION; SUBSTRATE SPECIFICITY; ZINC;

EID: 84996931805     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.2591     Document Type: Article

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