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Volumn 341, Issue 6145, 2013, Pages 549-553

Functional lysine modification by an intrinsically reactive primary glycolytic metabolite

Author keywords

[No Author keywords available]

Indexed keywords

1,3 DIPHOSPHOGLYCERIC ACID; GLUCOSE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCERIC ACID; GLYCOLYTIC ENZYME; LYSINE; UNCLASSIFIED DRUG;

EID: 84881077601     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1238327     Document Type: Article
Times cited : (165)

References (27)
  • 12
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    • E. L. Huttlin et al., Cell 143, 1174-1189 (2010).
    • (2010) Cell , vol.143 , pp. 1174-1189
    • Huttlin, E.L.1
  • 13
    • 84881044920 scopus 로고    scopus 로고
    • note
    • Primary data (.RAW files) from mouse tissue phosphoproteomes (enriched by strong cation exchange chromatography and IMAC) as reported in (12), were downloaded from the Proteome Commons public database. MS2 files were generated with RAW Xtractor and searched for pgK modified peptides by using a mouse EBI-IPI forward-reverse proteomic database as discussed in Materials and Methods. False-positive rates were between 0.0 and 0.5%.
  • 21
    • 84881079755 scopus 로고    scopus 로고
    • note
    • A review of literature on glycolytic enzyme modification revealed evidence for phosphate-modified forms of GAPDH and ENO1 in bacteria, which were interpreted to potentially correspond to enzymes modified by adenosine diphosphate ribosylation and substrate (2-phosphoglycerate), respectively (22). Our data offer an additional interpretation of these findings as evidence that 1,3-BPG may also modify glycolytic enzymes in bacteria.
  • 22
    • 10744223320 scopus 로고    scopus 로고
    • G. Boël et al.
    • G. Boël et al., J. Mol. Biol. 337, 485-496 (2004).
    • (2004) J. Mol. Biol. , vol.337 , pp. 485-496
  • 26
    • 84865300414 scopus 로고    scopus 로고
    • W. Yi et al., Science 337, 975-980 (2012).
    • (2012) Science , vol.337 , pp. 975-980
    • Yi, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.