1989
DOI: 10.1016/s0021-9258(18)63803-7
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Nucleotide Sequence and Regulation of a Human 90-kDa Heat Shock Protein Gene

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Cited by 72 publications
(5 citation statements)
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“…Although the similarity of the constituent amino acids is high, at the nucleotide level there are still some differences between HSP90α and the other three proteins, and this difference allows HSP90α to have more biological functions. 18 , 19 In vitro and in vivo experiments have found that HSP90α, which can promote wound healing, regulate inflammatory responses in normal tissues, and promote cell proliferation, invasion, epithelial–mesenchymal transition, and secondary drug resistance in tumor tissues, is a key target in tumor progression. 20–24 …”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Although the similarity of the constituent amino acids is high, at the nucleotide level there are still some differences between HSP90α and the other three proteins, and this difference allows HSP90α to have more biological functions. 18 , 19 In vitro and in vivo experiments have found that HSP90α, which can promote wound healing, regulate inflammatory responses in normal tissues, and promote cell proliferation, invasion, epithelial–mesenchymal transition, and secondary drug resistance in tumor tissues, is a key target in tumor progression. 20–24 …”
Section: Discussionmentioning
confidence: 99%
“…Although the similarity of the constituent amino acids is high, at the nucleotide level there are still some differences between HSP90α and the other three proteins, and this difference allows HSP90α to have more biological functions. 18,19 In vitro and in vivo experiments have found that HSP90α, which can promote wound healing, regulate inflammatory responses in normal tissues, and promote cell proliferation, invasion, epithelial-mesenchymal transition, and secondary drug resistance in tumor tissues, is a key target in tumor progression. [20][21][22][23][24] Trepel et al 25 analyzed the patient information from The Cancer Genome Atlas and found that HSP90AA1, encoding HSP90α, is highly expressed in bladder cancer and other malignant tumor tissues and is negatively correlated with the prognosis of patients, suggesting that HSP90α may be a potential tumor marker.…”
Section: Discussionmentioning
confidence: 99%
“…An 843-bp insert was digested out with ClaI and HindIII and subcloned into the vector pSP72. Hsp90␣ and hsp90␤ cDNA plasmids, which were obtained from Dr. L. Weber (Hickey et al, 1989;Rebbe et al, 1989), contained a 1.4-kb partial insert and a 2.1-kb full-length insert of hsp90␣ and hsp90␤ coding sequences, respectively. For hsp90␣, a 700-bp insert from the 3Ј-coding region was digested out of the cDNA plasmid with BclI and HindIII and subcloned into a pSP72 vector.…”
Section: Plasmidsmentioning
confidence: 99%
“…Και οι δύο υποοικογένειες περιλαµβάνουν αρκετά ψευδογονίδια (Durkin et al, 1993;Vamvakopoulos et al, 1993). Το hsp90-β αποτελείται από 12 εξώνια (Rebbe et al, 1989), ενώ το hsp90-α αποτελείται από 11 εξώνια και 10 εσώνια.…”
Section: A52 ∆οµή και ρύθµιση του γονιδίου Hsp90unclassified
“…Φυλογενετικές µελέτες Συζήτηση έχουν δείξει ότι οι ισοµορφές αυτές (HSP90-α και HSP90-β) προέρχονται από το διπλασιασµό ενός αρχικού γονιδίου, που συνέβη κατά την εποχή της εµφάνισης των τελεόστεων, πριν από περίπου 500 εκατοµµύρια χρόνια. Εποµένως, όλοι οι οργανισµοί που ανήκουν στα Σπονδυλωτά αναµένεται να έχουν και τις δύο ισοµορφές και αυτό ισχύει σε όσους οργανισµούς έχουν µελετηθεί µέχρι σήµερα (Binart et al, 1989;Hickey et al, 1989;Meng et al, 1993;Moore et al, 1987;Moore et al, 1989;Rebbe et al, 1989). Στα έντοµα που έχουν µελετηθεί, δεν έχει βρεθεί δεύτερη κυτταροπλασµατική ισοµορφή (Benedict et al, 1996;Blackman and Meselson, 1986;Konstantopoulou and Scouras, 1998;Landais et al, 2001;.…”
Section: ∆2 θερµοεπαγόµενη και συστατική έκφραση του γονιδίου Cchsp83unclassified