1992
DOI: 10.1016/s0021-9258(18)42827-x
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P59, an hsp 90-binding protein. Cloning and sequencing of its cDNA and preparation of a peptide-directed polyclonal antibody.

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Cited by 170 publications
(20 citation statements)
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“…Recently, the same protein was isolated and characterized as an immunophilin following FK506 affinity chromatography (Yem et al, 1992); specific peptide sequences within this protein were shown to have strong homology to FKBP-12 and FKBP-13. The cloning of hsp56 from rabbit liver cDNA was subsequently reported, and the derived amino acid sequence of hsp56 confirmed our original inference that hsp56 contained an FK506-binding domain (Lebeau et al, 1992). Additionally, a human form of hsp56 has now been cloned and expressed in Escherichia coli (Peattie et al, 1992).…”
mentioning
confidence: 55%
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“…Recently, the same protein was isolated and characterized as an immunophilin following FK506 affinity chromatography (Yem et al, 1992); specific peptide sequences within this protein were shown to have strong homology to FKBP-12 and FKBP-13. The cloning of hsp56 from rabbit liver cDNA was subsequently reported, and the derived amino acid sequence of hsp56 confirmed our original inference that hsp56 contained an FK506-binding domain (Lebeau et al, 1992). Additionally, a human form of hsp56 has now been cloned and expressed in Escherichia coli (Peattie et al, 1992).…”
mentioning
confidence: 55%
“…rabbit (Lebeau et al, 1992) and human (Peattie et al, 1992) hsp56, as shown in Figure 4. In fact, the high level of similarity of these peptides from chicken hsp56 to corresponding peptides from the mammalian proteins made the alignment simple and unambiguous.…”
Section: Resultsmentioning
confidence: 99%
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“…Like most FKBPs, the protein had a migration rate on SDS−PAGE gel indicative of a higher molecular weight (56−59 kDa) than actually calculated from its sequence (51.8 kDa); hence the confusion in nomenclature. It was subsequently found that FKBP52 was identical to a previously described heat-shock protein (hsp 56) found as a component of several unliganded steroid receptor complexes. ,, FKBP52 contains two FKBP domains with detectable rotamase activity and a third domain which contains three tetratricopeptide repeat motifs . Following these three domains is a calmodulin-binding consensus sequence.…”
Section: The Peptidylprolyl Isomerasesmentioning
confidence: 79%
“…It was subsequently found that FKBP52 was identical to a previously described heat-shock protein (hsp 56) found as a component of several unliganded steroid receptor complexes. 22,23,67 FKBP52 contains two FKBP domains with detectable rotamase activity and a third domain which contains three tetratricopeptide repeat motifs. 68 Following these three domains is a calmodulin-binding consensus sequence.…”
Section: Introductionmentioning
confidence: 99%