HSP90AB1

HSP90AB1

Heat shock protein 90kDa alpha (cytosolic), class B member 1, also known as HSP90AB1, is a human gene. [cite web | title = Entrez Gene: HSP90AB1 Heat shock protein 90kDa alpha (cytosolic), class B member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3326| accessdate = ]

PBB_Summary
section_title =
summary_text =

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Hoffmann T, Hovemann B |title=Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens. |journal=Gene |volume=74 |issue= 2 |pages= 491–501 |year= 1989 |pmid= 2469626 |doi=
*cite journal | author=Lees-Miller SP, Anderson CW |title=Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. |journal=J. Biol. Chem. |volume=264 |issue= 5 |pages= 2431–7 |year= 1989 |pmid= 2492519 |doi=
*cite journal | author=Rebbe NF, Hickman WS, Ley TJ, "et al." |title=Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene. |journal=J. Biol. Chem. |volume=264 |issue= 25 |pages= 15006–11 |year= 1989 |pmid= 2768249 |doi=
*cite journal | author=Rebbe NF, Ware J, Bertina RM, "et al." |title=Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family. |journal=Gene |volume=53 |issue= 2-3 |pages= 235–45 |year= 1987 |pmid= 3301534 |doi=
*cite journal | author=Tang PZ, Gannon MJ, Andrew A, Miller D |title=Evidence for oestrogenic regulation of heat shock protein expression in human endometrium and steroid-responsive cell lines. |journal=Eur. J. Endocrinol. |volume=133 |issue= 5 |pages= 598–605 |year= 1995 |pmid= 7581991 |doi=
*cite journal | author=Nemoto T, Ohara-Nemoto Y, Ota M, "et al." |title=Mechanism of dimer formation of the 90-kDa heat-shock protein. |journal=Eur. J. Biochem. |volume=233 |issue= 1 |pages= 1–8 |year= 1995 |pmid= 7588731 |doi=
*cite journal | author=Takahashi I, Tanuma R, Hirata M, Hashimoto K |title=A cosmid clone at the D6S182 locus on human chromosome 6p12 contains the 90-kDa heat shock protein beta gene (HSP90 beta). |journal=Mamm. Genome |volume=5 |issue= 2 |pages= 121–2 |year= 1994 |pmid= 8180474 |doi=
*cite journal | author=Ji H, Reid GE, Moritz RL, "et al." |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605–13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344
*cite journal | author=Yano M, Naito Z, Yokoyama M, "et al." |title=Expression of hsp90 and cyclin D1 in human breast cancer. |journal=Cancer Lett. |volume=137 |issue= 1 |pages= 45–51 |year= 1999 |pmid= 10376793 |doi=
*cite journal | author=Sato S, Fujita N, Tsuruo T |title=Modulation of Akt kinase activity by binding to Hsp90. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 20 |pages= 10832–7 |year= 2000 |pmid= 10995457 |doi= 10.1073/pnas.170276797
*cite journal | author=Gisler SM, Stagljar I, Traebert M, "et al." |title=Interaction of the type IIa Na/Pi cotransporter with PDZ proteins. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9206–13 |year= 2001 |pmid= 11099500 |doi= 10.1074/jbc.M008745200
*cite journal | author=Wiemann S, Weil B, Wellenreuther R, "et al." |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701
*cite journal | author=King FW, Wawrzynow A, Höhfeld J, Zylicz M |title=Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53. |journal=EMBO J. |volume=20 |issue= 22 |pages= 6297–305 |year= 2002 |pmid= 11707401 |doi= 10.1093/emboj/20.22.6297
*cite journal | author=Bouhouche-Chatelier L, Chadli A, Catelli MG |title=The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor. |journal=Cell Stress Chaperones |volume=6 |issue= 4 |pages= 297–305 |year= 2002 |pmid= 11795466 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Sato N, Yamamoto T, Sekine Y, "et al." |title=Involvement of heat-shock protein 90 in the interleukin-6-mediated signaling pathway through STAT3. |journal=Biochem. Biophys. Res. Commun. |volume=300 |issue= 4 |pages= 847–52 |year= 2003 |pmid= 12559950 |doi=
*cite journal | author=Wu JM, Xiao L, Cheng XK, "et al." |title=PKC epsilon is a unique regulator for hsp90 beta gene in heat shock response. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51143–9 |year= 2004 |pmid= 14532285 |doi= 10.1074/jbc.M305537200
*cite journal | author=Mungall AJ, Palmer SA, Sims SK, "et al." |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055
*cite journal | author=Nagaraja GM, Kandpal RP |title=Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins. |journal=Biochem. Biophys. Res. Commun. |volume=313 |issue= 3 |pages= 654–65 |year= 2004 |pmid= 14697242 |doi=
*cite journal | author=Bouwmeester T, Bauch A, Ruffner H, "et al." |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать курсовую

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”