HSP90B1

Heat shock protein 90kDa beta (Grp94), member 1 is a human chaperone protein. HSP90B1 is the human gene encoding it.

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Further reading

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*cite journal | author=Li Z, Dai J, Zheng H, "et al." |title=An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response. |journal=Front. Biosci. |volume=7 |issue= |pages= d731–51 |year= 2002 |pmid= 11861214 |doi=
*cite journal | author=Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R |title=Mortalin: present and prospective. |journal=Exp. Gerontol. |volume=37 |issue= 10-11 |pages= 1157–64 |year= 2003 |pmid= 12470827 |doi=
*cite journal | author=Schaiff WT, Hruska KA, McCourt DW, "et al." |title=HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. |journal=J. Exp. Med. |volume=176 |issue= 3 |pages= 657–66 |year= 1992 |pmid= 1512535 |doi=
*cite journal | author=Zolnierowicz S, Work C, Hutchison K, Fox IH |title=Partial separation of platelet and placental adenosine receptors from adenosine A2-like binding protein. |journal=Mol. Pharmacol. |volume=37 |issue= 4 |pages= 554–9 |year= 1990 |pmid= 2325637 |doi=
*cite journal | author=Maki RG, Old LJ, Srivastava PK |title=Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 15 |pages= 5658–62 |year= 1990 |pmid= 2377606 |doi=
*cite journal | author=Hutchison KA, Nevins B, Perini F, Fox IH |title=Soluble and membrane-associated human low-affinity adenosine binding protein (adenotin): properties and homology with mammalian and avian stress proteins. |journal=Biochemistry |volume=29 |issue= 21 |pages= 5138–44 |year= 1990 |pmid= 2378869 |doi=
*cite journal | author=Chang SC, Erwin AE, Lee AS |title=Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors. |journal=Mol. Cell. Biol. |volume=9 |issue= 5 |pages= 2153–62 |year= 1989 |pmid= 2546060 |doi=
*cite journal | author=Anderson SL, Shen T, Lou J, "et al." |title=The endoplasmic reticular heat shock protein gp96 is transcriptionally upregulated in interferon-treated cells. |journal=J. Exp. Med. |volume=180 |issue= 4 |pages= 1565–9 |year= 1994 |pmid= 7523574 |doi=
*cite journal | author=Bruneau N, Lombardo D |title=Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13524–33 |year= 1995 |pmid= 7768954 |doi=
*cite journal | author=Chavany C, Mimnaugh E, Miller P, "et al." |title=p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2. |journal=J. Biol. Chem. |volume=271 |issue= 9 |pages= 4974–7 |year= 1996 |pmid= 8617772 |doi=
*cite journal | author=Kuznetsov G, Chen LB, Nigam SK |title=Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 3057–63 |year= 1997 |pmid= 9006956 |doi=
*cite journal | author=Hoshino T, Wang J, Devetten MP, "et al." |title=Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression. |journal=Blood |volume=91 |issue= 11 |pages= 4379–86 |year= 1998 |pmid= 9596688 |doi=
*cite journal | author=Linnik KM, Herscovitz H |title=Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state. |journal=J. Biol. Chem. |volume=273 |issue= 33 |pages= 21368–73 |year= 1998 |pmid= 9694898 |doi=
*cite journal | author=Delom F, Lejeune PJ, Vinet L, "et al." |title=Involvement of oxidative reactions and extracellular protein chaperones in the rescue of misassembled thyroglobulin in the follicular lumen. |journal=Biochem. Biophys. Res. Commun. |volume=255 |issue= 2 |pages= 438–43 |year= 1999 |pmid= 10049727 |doi= 10.1006/bbrc.1999.0229
*cite journal | author=Reddy RK, Lu J, Lee AS |title=The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis. |journal=J. Biol. Chem. |volume=274 |issue= 40 |pages= 28476–83 |year= 1999 |pmid= 10497210 |doi=
*cite journal | author=Roher N, Sarno S, Miró F, "et al." |title=The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme. |journal=FEBS Lett. |volume=505 |issue= 1 |pages= 42–6 |year= 2001 |pmid= 11557039 |doi=
*cite journal | author=Randow F, Seed B |title=Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. |journal=Nat. Cell Biol. |volume=3 |issue= 10 |pages= 891–6 |year= 2001 |pmid= 11584270 |doi= 10.1038/ncb1001-891
*cite journal | author=Vabulas RM, Braedel S, Hilf N, "et al." |title=The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20847–53 |year= 2002 |pmid= 11912201 |doi= 10.1074/jbc.M200425200
*cite journal | author=Shin HJ, Kim SS, Cho YH, "et al." |title=Host cell proteins binding to the encapsidation signal epsilon in hepatitis B virus RNA. |journal=Arch. Virol. |volume=147 |issue= 3 |pages= 471–91 |year= 2002 |pmid= 11958450 |doi=

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