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Volumn 132, Issue 10, 2010, Pages 3264-3265

Activity-based probes that target functional subclasses of phospholipases in proteomes

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY-BASED; ACTIVITY-BASED PROBE; CATALYTIC PROPERTIES; CHEMICAL PROBES; ENDOCANNABINOID; HYDROLASES; IN-CELL; MOLECULAR CHARACTERIZATION; PHOSPHOLIPASES; PROTEIN PROFILING; PROTEOMES; SIGNALING PATHWAYS; SUBSTRATE SPECIFICITY; SYNTHESIS AND CHARACTERIZATION;

EID: 77950511344     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja1000505     Document Type: Article
Times cited : (54)

References (15)
  • 12
    • 77950484954 scopus 로고    scopus 로고
    • We attempted to characterize the activity of DDHD2 with PC substrates containing sn-l ester/sn-2 ether or sn-1 ether/sn-2 ester linkages (Supporting Figure 6), but unlike DDHD1, DDHD2 did not accept substrates having ether linkages at the sn- 1/sn-2 positions
    • We attempted to characterize the activity of DDHD2 with PC substrates containing sn-l ester/sn-2 ether or sn-1 ether/sn-2 ester linkages (Supporting Figure 6), but unlike DDHD1, DDHD2 did not accept substrates having ether linkages at the sn- 1/sn-2 positions.
  • 15
    • 77950476128 scopus 로고    scopus 로고
    • Phospholipases can also show head-group selectivity, and we therefore envision that variants of probes 1 and 2 in which the choline group is replaced with serine, ethanolamine, or inositol may also prove useful for characterizing additional types of phospholipases
    • Phospholipases can also show head-group selectivity, and we therefore envision that variants of probes 1 and 2 in which the choline group is replaced with serine, ethanolamine, or inositol may also prove useful for characterizing additional types of phospholipases.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.