A conserved NAD+ binding pocket that regulates protein-protein interactions during aging

Science

Volumn 355, Issue 6331, 2017, Pages 1312-1317

  Li, Jun ^a   Bonkowski, Michael S ^a   Moniot, Sébastien ^b   Zhang, Dapeng ^c,g   Hubbard, Basil P ^a,h   Ling, Alvin J Y ^a   Rajman, Luis A ^a   Qin, Bo ^d   Lou, Zhenkun ^d   Gorbunova, Vera ^e   Aravind, L ^c   Steegborn, Clemens ^b   Sinclair, David A ^a,f  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF BAYREUTH   (Germany)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

^d MAYO CLINIC   (United States)

^e UNIVERSITY OF ROCHESTER   (United States)

^f UNIVERSITY OF NEW SOUTH WALES   (Australia)

^g SAINT LOUIS UNIVERSITY   (United States)

^h UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

DBC1 PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE NUCLEOTIDE; PEPTIDES AND PROTEINS; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SIRTUIN 1; UNCLASSIFIED DRUG; DBC1 PROTEIN, HUMAN; PARAQUAT; PARP1 PROTEIN, HUMAN; SMALL INTERFERING RNA; TUMOR SUPPRESSOR PROTEIN;

AGING; CANCER; CHEMICAL BINDING; DAMAGE; GENE; HOMOLOGY; PROTEIN; RODENT;

AGING; ARTICLE; BINDING SITE; COMPLEX FORMATION; DNA DAMAGE; DNA REPAIR; HEK293 CELL LINE; HUMAN; NONHUMAN; NUDIX HOMOLOGY DOMAIN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; ANIMAL; CHEMISTRY; CONSERVED SEQUENCE; DRUG EFFECTS; FIBROBLAST; GENETICS; METABOLISM; MOLECULAR MODEL; MOUSE; NEOPLASM; PROTEIN DOMAIN; RADIATION TOLERANCE; SEQUENCE HOMOLOGY;

MUS;

AGING; ANIMALS; CONSERVED SEQUENCE; DNA DAMAGE; DNA REPAIR; FIBROBLASTS; HEK293 CELLS; HUMANS; MICE; MODELS, MOLECULAR; NAD; NEOPLASMS; PARAQUAT; POLY (ADP-RIBOSE) POLYMERASE-1; PROTEIN INTERACTION DOMAINS AND MOTIFS; RADIATION TOLERANCE; RNA, SMALL INTERFERING; SEQUENCE HOMOLOGY, NUCLEIC ACID; TUMOR SUPPRESSOR PROTEINS;

EID: 85016317809     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aad8242     Document Type: Article

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