FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1602103265> ?p ?o ?g. }

• W1602103265 endingPage "451" @default.
• W1602103265 startingPage "436" @default.
• W1602103265 abstract "The prenylation of proteins, including several in the visual transduction pathway, is one of the most recently discovered modifications of eukaryotic cell proteins.1–4 Some prenylated proteins, including rhodopsin kinase, the γ subunit of transducin, the α subunit of retinal cGMP phosphodiesterase, Ras, and lamin B, are initially produced with a C-terminal sequence motif CaaX (C is cysteine, a is usually but not necessarily an aliphatic residue, and X is typically M, S, or Q). Prenylation occurs by enzyme-catalyzed attachment of a 15-carbon farnesyl group to cysteine via a thioether linkage. After prenylation, aaX is released by a membrane-bound endoprotease,5–8 and the newly exposed S-farnesylcysteine is methylated on its α-carboxyl group by a membrane-bound methyltransferase.9,10 Other prenylated proteins, including the γ subunits of many heterotrimeric G proteins, the β subunit of retinal cGMP phosphodiesterase, and a subset of small GTP-binding proteins, contain a CaaX motif (X = L, F) and are modified by the attachment of the 20-carbon geranylgeranyl group. Removal of aaX and C-terminal methylation occurs as for farnesylated proteins. Finally, the subset of GTP-binding proteins termed Rab contains two cysteines near or at the C terminus (CCXX, XXCC, CXC), and both cysteine sulfhydryls contain a thioether-linked geranylgeranyl group.11 The attachment of prenyl groups to these three classes of proteins is catalyzed by three distinct protein prenyltranferases.12,13Structures of protein prenyl groups have been rigorously established by releasing the protein-bound lipids with Raney nickel (to cleave reductively the bond between cysteine S and C-1 of the prenyl group) and analyzing the released hydrocarbons by combined gas chromatography–mass spectrometry versus authentic standards.14–17 Protein prenyl groups can also be released by treatment with methyl iodide to produce farnesol and geranylgeraniol along with isomerized prenols.16,18 This method has been used when relatively small amounts of prenylated protein are available, typically from tissue culture cells that have been grown in the presence of radiolabeled mevalonic acid (the precursor of prenyl groups) or its lactone in the presence of statins, which block the production of endogenous mevalonic acid. The radiolabeled prenol is analyzed versus standards by reversed phase high-performance liquid chromatography (HPLC).16 While this approach does not establish the chemical structure of the prenyl group, it provides strong circumstantial evidence for the presence of protein-bound farnesyl and geranylgeranyl groups. However, in our hands, we have experienced difficulties with methyl iodide cleavage, in that yields are highly variable and can be quite low in some cases (<10% cleavage). Work in our laboratory has shown that the Raney nickel cleavage method is superior to methyl iodide treatment, and the details of this procedure, combined with HPLC analysis of the released radiolabeled hydrocarbons, are described in this chapter. This method has been used to analyze protein prenyl groups from protein extracted from sodium dodecyl sulfate (SDS)–polyacrylamide gel slices. Also described here is the use of Raney nickel cleavage followed by combined gas chromatography–mass spectrometry to determine the structure of prenyl groups released from delipidated total cell protein.The rigorous structural analysis of aaX removal and C-terminal methylation has been carried out by fast atom bombardment mass spectrometry of C-terminal peptides from prenylated proteins.11,19 A less rigorous approach has been used to explore C-terminal methylation: HPLC analysis of the product of oxidative scission of the prenyl–cysteine linkage combined with amide bond hydrolysis to yield cysteic acid methyl ester.20 In the present chapter, a method for electrospray mass spectrometric analysis of protein C-terminal peptides is presented, which has been applied to the analysis of prenylated peptides in a complex mixture (a tryptic digest of partially purified bovine rhodopsin kinase). This method is facilitated by the availability of prenylated peptide standards, and a convenient synthesis of peptides and peptide methyl esters radiolabeled with high specific activity farnesyl and geranylgeranyl groups is described." @default.
• W1602103265 created "2016-06-24" @default.
• W1602103265 creator A5008335995 @default.
• W1602103265 creator A5019677607 @default.
• W1602103265 creator A5026524686 @default.
• W1602103265 creator A5037735643 @default.
• W1602103265 creator A5045657649 @default.
• W1602103265 creator A5054562365 @default.
• W1602103265 creator A5079803971 @default.
• W1602103265 creator A5083768832 @default.
• W1602103265 date "2000-01-01" @default.
• W1602103265 modified "2023-10-18" @default.
• W1602103265 title "[29] Structural analysis of protein prenyl groups and associated C-terminal modifications" @default.
• W1602103265 cites W1491433568 @default.
• W1602103265 cites W1546934509 @default.
• W1602103265 cites W1964489808 @default.
• W1602103265 cites W1989171805 @default.
• W1602103265 cites W1992972153 @default.
• W1602103265 cites W2013410321 @default.
• W1602103265 cites W2015763826 @default.
• W1602103265 cites W2017264694 @default.
• W1602103265 cites W2018596954 @default.
• W1602103265 cites W2023353768 @default.
• W1602103265 cites W2036405416 @default.
• W1602103265 cites W2036546637 @default.
• W1602103265 cites W2040286337 @default.
• W1602103265 cites W2040315421 @default.
• W1602103265 cites W2043921136 @default.
• W1602103265 cites W2057724275 @default.
• W1602103265 cites W2094365118 @default.
• W1602103265 cites W2094916229 @default.
• W1602103265 cites W2156398385 @default.
• W1602103265 cites W2158407439 @default.
• W1602103265 cites W2176744910 @default.
• W1602103265 cites W2178557511 @default.
• W1602103265 cites W4237555097 @default.
• W1602103265 cites W4237568731 @default.
• W1602103265 cites W4238563914 @default.
• W1602103265 cites W4247100506 @default.
• W1602103265 cites W945913723 @default.
• W1602103265 doi "https://doi.org/10.1016/s0076-6879(00)16741-2" @default.
• W1602103265 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1435690" @default.
• W1602103265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10800693" @default.
• W1602103265 hasPublicationYear "2000" @default.
• W1602103265 type Work @default.
• W1602103265 sameAs 1602103265 @default.
• W1602103265 citedByCount "7" @default.
• W1602103265 countsByYear W16021032652014 @default.
• W1602103265 crossrefType "book-chapter" @default.
• W1602103265 hasAuthorship W1602103265A5008335995 @default.
• W1602103265 hasAuthorship W1602103265A5019677607 @default.
• W1602103265 hasAuthorship W1602103265A5026524686 @default.
• W1602103265 hasAuthorship W1602103265A5037735643 @default.
• W1602103265 hasAuthorship W1602103265A5045657649 @default.
• W1602103265 hasAuthorship W1602103265A5054562365 @default.
• W1602103265 hasAuthorship W1602103265A5079803971 @default.
• W1602103265 hasAuthorship W1602103265A5083768832 @default.
• W1602103265 hasBestOaLocation W16021032652 @default.
• W1602103265 hasConcept C181199279 @default.
• W1602103265 hasConcept C185592680 @default.
• W1602103265 hasConcept C2779664074 @default.
• W1602103265 hasConcept C31258907 @default.
• W1602103265 hasConcept C41008148 @default.
• W1602103265 hasConcept C55493867 @default.
• W1602103265 hasConcept C57790582 @default.
• W1602103265 hasConceptScore W1602103265C181199279 @default.
• W1602103265 hasConceptScore W1602103265C185592680 @default.
• W1602103265 hasConceptScore W1602103265C2779664074 @default.
• W1602103265 hasConceptScore W1602103265C31258907 @default.
• W1602103265 hasConceptScore W1602103265C41008148 @default.
• W1602103265 hasConceptScore W1602103265C55493867 @default.
• W1602103265 hasConceptScore W1602103265C57790582 @default.
• W1602103265 hasLocation W16021032651 @default.
• W1602103265 hasLocation W16021032652 @default.
• W1602103265 hasLocation W16021032653 @default.
• W1602103265 hasLocation W16021032654 @default.
• W1602103265 hasOpenAccess W1602103265 @default.
• W1602103265 hasPrimaryLocation W16021032651 @default.
• W1602103265 hasRelatedWork W1531601525 @default.
• W1602103265 hasRelatedWork W2329535185 @default.
• W1602103265 hasRelatedWork W2607424097 @default.
• W1602103265 hasRelatedWork W2748952813 @default.
• W1602103265 hasRelatedWork W2782497155 @default.
• W1602103265 hasRelatedWork W2899084033 @default.
• W1602103265 hasRelatedWork W2948807893 @default.
• W1602103265 hasRelatedWork W2949937423 @default.
• W1602103265 hasRelatedWork W2952407896 @default.
• W1602103265 hasRelatedWork W2778153218 @default.
• W1602103265 isParatext "false" @default.
• W1602103265 isRetracted "false" @default.
• W1602103265 magId "1602103265" @default.
• W1602103265 workType "book-chapter" @default.