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0028261389
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Cellular requirements for tumor-specific immunity elicited by heat shock proteins: Tumor rejection antigen gp96 primes CD8+ T cells in vivo
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Udono H, Levy DL, Srivastava PK. Cellular requirements for tumor-specific immunity elicited by heat shock proteins: tumor rejection antigen gp96 primes CD8+ T cells in vivo. Proc Natl Acad Sci USA. 91:1994;3077-3081.
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Udono, H.1
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2
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Cross-priming of minor histocompatability antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96
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Arnold D, Faath S, Rammensee HG, Schild H. Cross-priming of minor histocompatability antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96. J Exp Med. 182:1995;885-889.
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Arnold, D.1
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A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
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Suto R, Srivastava PK. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science. 269:1995;1585-1588.
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Heat shock proteins transfer peptides during antigen processing and CTL priming
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Srivastava PK, Udono H, Blachere NE, Li Z. Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics. 39:1994;93-98.
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Srivastava, P.K.1
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5
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0030820099
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Immunotherapy of cancers with autologous cancer-derived heat shock protein preparations
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+ response against the parent tumor, as well as metastatic lesions. Tumor-derived heat shock protein - peptide complexes are shown to be effective immunother-apeutic agents against spontaneous, chemically induced and UV light-induced cancers. This consistutes the first demonstration that heat shock proteins vaccines are effective in models of pre-existing cancer
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+ response against the parent tumor, as well as metastatic lesions. Tumor-derived heat shock protein - peptide complexes are shown to be effective immunother-apeutic agents against spontaneous, chemically induced and UV light-induced cancers. This consistutes the first demonstration that heat shock proteins vaccines are effective in models of pre-existing cancer.
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Tamura, Y.1
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6
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0030775140
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Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide - Specific cytotoxic T lymphocyte response and tumor immunity
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+ responses. Data are presented demonstrating prophylactic immunization against a lymphoma variant expressing the nucleocapsid protein of vesicular stomatitis virus (VSV), following vaccination with GRP94 reconstituted in vitro with the dominant immunogenic epitope of VSV
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+ responses. Data are presented demonstrating prophylactic immunization against a lymphoma variant expressing the nucleocapsid protein of vesicular stomatitis virus (VSV), following vaccination with GRP94 reconstituted in vitro with the dominant immunogenic epitope of VSV.
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Blachere, N.E.1
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Basu, S.6
Udono, H.7
Srivsatava, P.K.8
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7
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0030905479
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The endoplasmic reticulum-resident stress protein gp96 binds peptides translocated by TAP
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of special interest. Using paired cell systems differing in the transporter associated with antigen presentation(TAP) expression, the authors demonstrate the endoplasmic reticulum (ER)-localized GRP94/gp96 binds peptides trafficked to the ER in a TAP-dependent manner. This report clearly demonstrates that GRP94/gp96 participates in peptide trafficking in the ER and raises interesting questions concerning the fate of peptides that are transported by TAP, yet escape assembly onto class I molecules
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Lammert E, Arnold D, Nijenhuis M, Momburg F, Häamerling GJ, Brunner J, Stevanovic S, Rammensee HG, Schild H. The endoplasmic reticulum-resident stress protein gp96 binds peptides translocated by TAP. of special interest Eur J Immunol. 27:1997;923-927 Using paired cell systems differing in the transporter associated with antigen presentation(TAP) expression, the authors demonstrate the endoplasmic reticulum (ER)-localized GRP94/gp96 binds peptides trafficked to the ER in a TAP-dependent manner. This report clearly demonstrates that GRP94/gp96 participates in peptide trafficking in the ER and raises interesting questions concerning the fate of peptides that are transported by TAP, yet escape assembly onto class I molecules.
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Eur J Immunol
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Lammert, E.1
Arnold, D.2
Nijenhuis, M.3
Momburg, F.4
Häamerling, G.J.5
Brunner, J.6
Stevanovic, S.7
Rammensee, H.G.8
Schild, H.9
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8
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0030800342
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Influences of transporter associated with antigen processing (TAP) on the repertoire of peptides associated with the endoplasmic reticulum-resident stress protein gp96
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of outstanding interest. In investigating the transporter associated with antigen presentation (TAP) dependence for peptide loading onto GRP94/gp96, the authors have discovered that GRP94/gp96 can associate with a diverse array of peptides, regardless of whether the peptides are transported in a TAP-dependent or TAP-independent manner. These data demonstrate that the GRP94/gp96-bound peptide fraction is wholly independent of the MHC haplotype and suggest that this fraction is broadly representative of the endoplasmic reticulum-associated peptide pool
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Arnold D, Wahl C, Faath S, Rammensee HG, Schild H. Influences of transporter associated with antigen processing (TAP) on the repertoire of peptides associated with the endoplasmic reticulum-resident stress protein gp96. of outstanding interest J Exp Med. 186:1997;461-466 In investigating the transporter associated with antigen presentation (TAP) dependence for peptide loading onto GRP94/gp96, the authors have discovered that GRP94/gp96 can associate with a diverse array of peptides, regardless of whether the peptides are transported in a TAP-dependent or TAP-independent manner. These data demonstrate that the GRP94/gp96-bound peptide fraction is wholly independent of the MHC haplotype and suggest that this fraction is broadly representative of the endoplasmic reticulum-associated peptide pool.
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J Exp Med
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Arnold, D.1
Wahl, C.2
Faath, S.3
Rammensee, H.G.4
Schild, H.5
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9
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0030901877
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A molecular clamp in the crystal structure of the N-terminal domain of the yeast hsp90-chaperone
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of special interest. The crystal structure of recombinant amino-terminal domain of yeast hsp90 reveals a domain-swapped dimer that includes a potential 'molecular clamp' region lying within the intrasubunit groove. These results suggest both a potential site of hsp90 - substrate interaction and a structural mechanism for regulating substrate binding and release
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Prodromou C, Roe SM, Piper PW, Pearl LH. A molecular clamp in the crystal structure of the N-terminal domain of the yeast hsp90-chaperone. of special interest Nat Struct Biol. 4:1997;477-482 The crystal structure of recombinant amino-terminal domain of yeast hsp90 reveals a domain-swapped dimer that includes a potential 'molecular clamp' region lying within the intrasubunit groove. These results suggest both a potential site of hsp90 - substrate interaction and a structural mechanism for regulating substrate binding and release.
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Prodromou, C.1
Roe, S.M.2
Piper, P.W.3
Pearl, L.H.4
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10
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0031444238
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Identification and structural characterization of the ATP/ADP-binding site in the hsp90 molecular chaperone
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of outstanding interest. When co-crystallized with ATP or ADP, a highly conserved region of the amino-terminal region was found to contain a binding site for adenine nucleotides. The analysis of binding affinities indicates a preference for ADP over ATP. For both nucleotides, the measured affinities are quite low, perhaps suggesting a structural, rather than enzymatic, contribution to hsp90 function
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Prodromou C, Roe SM, Obrien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the hsp90 molecular chaperone. of outstanding interest Cell. 90:1997;65-75 When co-crystallized with ATP or ADP, a highly conserved region of the amino-terminal region was found to contain a binding site for adenine nucleotides. The analysis of binding affinities indicates a preference for ADP over ATP. For both nucleotides, the measured affinities are quite low, perhaps suggesting a structural, rather than enzymatic, contribution to hsp90 function.
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Prodromou, C.1
Roe, S.M.2
Obrien, R.3
Ladbury, J.E.4
Piper, P.W.5
Pearl, L.H.6
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11
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0031005361
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Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an anti-tumor agent
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of outstanding interest. The co-crystal structure of the anti-tumor agent geldanamycin and the amino-terminal domain of hsp90 reveals a monomeric quaternary structure and a hydrophobic binding pocket within a highly conserved region of the hsp90 family of proteins. The geldanamycin binding site is suggested to mimic a binding site for a pentameric peptide domain and may therefore describe the peptide binding site of the native protein
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Stebbins CE, Russo AA, Rosen N, Hartl FU, Pavletich NP. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an anti-tumor agent. of outstanding interest Cell. 89:1997;239-250 The co-crystal structure of the anti-tumor agent geldanamycin and the amino-terminal domain of hsp90 reveals a monomeric quaternary structure and a hydrophobic binding pocket within a highly conserved region of the hsp90 family of proteins. The geldanamycin binding site is suggested to mimic a binding site for a pentameric peptide domain and may therefore describe the peptide binding site of the native protein.
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Cell
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Stebbins, C.E.1
Russo, A.A.2
Rosen, N.3
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Pavletich, N.P.5
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Phylogenetic analysis of the 90kD heat shock family of protein sequences and an examination of the relationship between animals, plants, and fungal species
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Gupta, R.S.1
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GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II
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ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)
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Mazzarella RA, Green M. ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). J Biol Chem. 262:1987;8875-8883.
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Maki RG, Old LI, Srivastava PK. Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins. Proc Natl Acad Sci USA. 87:1990;5658-5662.
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Wearsch, P.A.1
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Altmeyer A, Maki RG, Feldweg AM, Heike M, Protopopov VP, Masur SK, Srivastava PK. Tumor-specific cell surface expression of the -KDEL containing endoplasmic reticulum heat shock protein gp96. Int J Cancer. 69:1996;340-349.
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Regulation of the glucose-regulated protein genes by beta-mercaptoethanol requires de novo protein synthesis and correlates with inhibition of protein glycosylation
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Kim YK, Kim KS, Lee AS. Regulation of the glucose-regulated protein genes by beta-mercaptoethanol requires de novo protein synthesis and correlates with inhibition of protein glycosylation. J Cell Physiol. 133:1986;533-559.
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The endoplasmic reticulum protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains
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Melnick J, Aviel S, Argon Y. The endoplasmic reticulum protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J Biol Chem. 267:1992;21303-21306.
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24
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HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
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Schaiff WT, Hruska KA, McCourt DW, Green M, Schwartz BD. HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J Exp Med. 176:1992;657-666.
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Kuznetsov G, Chen LB, Nigam SK. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J Biol Chem. 272:1997;3057-3063.
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Association of Hsp47, Grp78 and Grp94 with procollagen supports the successive or coupled action of molecular chaperones
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Ferreira LR, Norris K, Smith T, Hebert C, Sauk JJ. Association of Hsp47, Grp78 and Grp94 with procollagen supports the successive or coupled action of molecular chaperones. J Cell Biochem. 56:1994;518-526.
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Melnick J, Dul J, Argon Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin light chains in the endoplasmic reticulum. Nature. 370:1994;373-375.
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TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin
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of outstanding interest. Photoaffinity peptide analogs were used to identify gp96, protein disulfide isomerase and calreticulin as peptide-binding proteins of the endoplasmic reticulum lumen. Of particular note, screening of a peptide library containing degenerate residues at the 2 and 9 positions indicated a distinct bias by gp96 for peptides containing uncharged amino acids at these positions. These data are the first description of a peptide binding specificity for gp96
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Spee P, Neefjes J. TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin. of outstanding interest Eur J Immunol. 27:1997;2441-2449 Photoaffinity peptide analogs were used to identify gp96, protein disulfide isomerase and calreticulin as peptide-binding proteins of the endoplasmic reticulum lumen. Of particular note, screening of a peptide library containing degenerate residues at the 2 and 9 positions indicated a distinct bias by gp96 for peptides containing uncharged amino acids at these positions. These data are the first description of a peptide binding specificity for gp96.
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Van Bleek, G.M.1
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Milano: Universita Degli Studi Di Milano
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Fourth International Symposium on Dendritic Cells in Fundamental and Clinical Immunology: Oct 1996; Venice, Italy
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Bernhard, H.1
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Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent
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of special interest. The analysis of the interaction of native glucose regulated protein (GRP)-94 with ATP indicates that GRP94 does not display high affinity ATP binding or hydrolysis. The binding of VSV8, a known peptide substrate for GRP94, is shown to be identical when assayed in the presence or absence of ATP, or when ATP is present subsequent to peptide binding. These results indicate that the interaction of GRP94 with peptide substrates is regulated independently of ATP
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Wearsch PA, Nicchitta CV. Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent. of special interest J Biol Chem. 272:1997;5152-5156 The analysis of the interaction of native glucose regulated protein (GRP)-94 with ATP indicates that GRP94 does not display high affinity ATP binding or hydrolysis. The binding of VSV8, a known peptide substrate for GRP94, is shown to be identical when assayed in the presence or absence of ATP, or when ATP is present subsequent to peptide binding. These results indicate that the interaction of GRP94 with peptide substrates is regulated independently of ATP.
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Wearsch, P.A.1
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Protein disulfide isomerase is the dominant acceptor for peptides translocated into the endoplasmic reticulum
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of outstanding interest. Investigations into the fate of peptides transported by the transporter associated with antigen presentation (TAP) reveal that protein disulfide isomerase was the predominant peptide acceptor. The authors raise some very interesting issues regarding the fate of peptides transported into the endoplasmic reticulum (ER) and propose a number of provocative models for the role of ER chaperones in peptide transport into, and out of, the ER
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Lammert E, Stevanovic S, Rammensee HG, Schild H. Protein disulfide isomerase is the dominant acceptor for peptides translocated into the endoplasmic reticulum. of outstanding interest Eur J Immunol. 27:1997;1685-1690 Investigations into the fate of peptides transported by the transporter associated with antigen presentation (TAP) reveal that protein disulfide isomerase was the predominant peptide acceptor. The authors raise some very interesting issues regarding the fate of peptides transported into the endoplasmic reticulum (ER) and propose a number of provocative models for the role of ER chaperones in peptide transport into, and out of, the ER.
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Eur J Immunol
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Lammert, E.1
Stevanovic, S.2
Rammensee, H.G.3
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Translocation of ATP into the lumen of rough endoplasmic reticlum-derived vesicles and its binding to lumenal proteins including BiP (GRP78) and GRP94
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Clairmont CA, De Maio A, Hirschberg CB. Translocation of ATP into the lumen of rough endoplasmic reticlum-derived vesicles and its binding to lumenal proteins including BiP (GRP78) and GRP94. J Biol Chem. 267:1992;3983-3990.
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Clairmont, C.A.1
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42
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0030752373
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ATP-binding properties of human hsp90
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of special interest. In addressing the somewhat controversial data regarding the interaction of adenine nucleotides with mammalian hsp90, an unusual, very low affinity (half maximal binding=400 μM) interaction between spin-labeled ATP analogs and human hsp90 is reported. The finding that bovine serum albumin exhibits identical interactions suggests that ATP binding does not directly contribute to the regulatin of hsp90-substrate interactions
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Scheibel T, Neuhofen S, Weik T, Mayr C, Reinstein J, Vogel PD, Buchner J. ATP-binding properties of human hsp90. of special interest J Biol Chem. 272:1997;18608-18613 In addressing the somewhat controversial data regarding the interaction of adenine nucleotides with mammalian hsp90, an unusual, very low affinity (half maximal binding=400 μM) interaction between spin-labeled ATP analogs and human hsp90 is reported. The finding that bovine serum albumin exhibits identical interactions suggests that ATP binding does not directly contribute to the regulatin of hsp90-substrate interactions.
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J Biol Chem
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Scheibel, T.1
Neuhofen, S.2
Weik, T.3
Mayr, C.4
Reinstein, J.5
Vogel, P.D.6
Buchner, J.7
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43
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Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain
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Wearsch PA, Nicchitta CV. Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain. Biochemistry. 35:1996;16760-16769.
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Wearsch, P.A.1
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0025058815
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Class I restricted processing and presentation and exogenous cell-associated antigens in vivo
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Carbone FR, Bevan MJ. Class I restricted processing and presentation and exogenous cell-associated antigens in vivo. J Exp Med. 171:1990;377-387.
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Carbone, F.R.1
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Efficient major histocompatability complex class I presentation of exogenous antigen upon phagocytosis by macrophages
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Kovacsovics-Bankowski M, Clark K, Benacerraf B, Rock KL. Efficient major histocompatability complex class I presentation of exogenous antigen upon phagocytosis by macrophages. Proc Natl Acad Sci USA. 90:1993;4942-4946.
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Kovacsovics-Bankowski, M.1
Clark, K.2
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Rock, K.L.4
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46
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Injection of detergent-denatured ovalbumin primes murine class I restricted T cells in vivo
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Schirmbeck R, Böhm W, Reimann J. Injection of detergent-denatured ovalbumin primes murine class I restricted T cells in vivo. Eur J Immunol. 24:1994;2068-2072.
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Schirmbeck, R.1
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Reimann, J.3
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47
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0030873428
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Direct delivery of exogenous MHC class I molecule-binding oligopeptides to the endoplasmic reticulum of viable cells
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of outstanding interest. An interesting study demonstrating a novel intracellular trafficking pathway for the transport of peptides from the extracellular medium to the lumen of the endoplasmic reticulum (ER). This pathway can contribute to peptide loading onto MHC class I molecules and may represent a novel pathway for modulating the chemical composition of the ER, or, perhaps more likely, in the regulation of signal transduction events in the ER membrane
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Day PM, Yewdell JW, Porgador A, Germain RN, Bennink JR. Direct delivery of exogenous MHC class I molecule-binding oligopeptides to the endoplasmic reticulum of viable cells. of outstanding interest Proc Natl Acad Sci USA. 94:1997;8064-8069 An interesting study demonstrating a novel intracellular trafficking pathway for the transport of peptides from the extracellular medium to the lumen of the endoplasmic reticulum (ER). This pathway can contribute to peptide loading onto MHC class I molecules and may represent a novel pathway for modulating the chemical composition of the ER, or, perhaps more likely, in the regulation of signal transduction events in the ER membrane.
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Proc Natl Acad Sci USA
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Day, P.M.1
Yewdell, J.W.2
Porgador, A.3
Germain, R.N.4
Bennink, J.R.5
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48
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0031030792
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Constitutive macropinocytosis allows TAP-dependent major histocompatability complex class I presentation of exogenous soluble antigen by bone marrow-derived dendritic cells
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of outstanding interest. This report describes a novel trafficking pathway, operating in bone marrow-derived dendritic cells (BMDC), that delivers soluble proteins from the extracellular space to the cytosol, thereby allowing transporter for antigen presentation (TAP)-dependent presentation of extracellular antigens on class I molecules. This pathway is likely to be unique to professional antigen-presenting cells and may be critical in determining the capacity of BMDC to traffic antigens into the class I pathway
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Norbury CC, Chambers BJ, Prescott AR, Ljunggren H-G, Watt C. Constitutive macropinocytosis allows TAP-dependent major histocompatability complex class I presentation of exogenous soluble antigen by bone marrow-derived dendritic cells. of outstanding interest Eur J Immunol. 27:1997;280-288 This report describes a novel trafficking pathway, operating in bone marrow-derived dendritic cells (BMDC), that delivers soluble proteins from the extracellular space to the cytosol, thereby allowing transporter for antigen presentation (TAP)-dependent presentation of extracellular antigens on class I molecules. This pathway is likely to be unique to professional antigen-presenting cells and may be critical in determining the capacity of BMDC to traffic antigens into the class I pathway.
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Eur J Immunol
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Norbury, C.C.1
Chambers, B.J.2
Prescott, A.R.3
Ljunggren H-G4
Watt, C.5
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49
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0029550235
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Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages
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Norbury CC, Hewlett LJ, Prescott AR, Shastri N, Watts C. Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages. Immunity. 3:1995;783-791.
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Norbury, C.C.1
Hewlett, L.J.2
Prescott, A.R.3
Shastri, N.4
Watts, C.5
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50
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0028920154
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The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack
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Miesenböck G, Rothman JE. The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack. J Cell Biol. 129:1995;309-319.
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Miesenböck, G.1
Rothman, J.E.2
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51
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0031046750
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Novel peptide-binding proteins and peptide transport in normal and TAP-deficient microsomes
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of special interest. Using photo-labeled peptide analogs, a number of endoplasmic reticulum (ER)-specific peptide binding proteins are identified including glucose regulated protein (GRP0-94, p60, and a complex of lower molecular weight proteins specific for N-linked sugar bearing peptides (p36 complex). This is an important study that will contribute to the elucidation of the regulation of peptide transport into, and out of, the ER lumen. In addition, data are presented demonstrating sequence-specific peptide transport in the presence of transporter associated with antigen processing (TAP)-1 alone
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Marusina K, Reid G, Gabathuier R, Jefferies W, Monaco JJ. Novel peptide-binding proteins and peptide transport in normal and TAP-deficient microsomes. of special interest Biochemistry. 36:1997;856-863 Using photo-labeled peptide analogs, a number of endoplasmic reticulum (ER)-specific peptide binding proteins are identified including glucose regulated protein (GRP0-94, p60, and a complex of lower molecular weight proteins specific for N-linked sugar bearing peptides (p36 complex). This is an important study that will contribute to the elucidation of the regulation of peptide transport into, and out of, the ER lumen. In addition, data are presented demonstrating sequence-specific peptide transport in the presence of transporter associated with antigen processing (TAP)-1 alone.
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(1997)
Biochemistry
, vol.36
, pp. 856-863
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Marusina, K.1
Reid, G.2
Gabathuier, R.3
Jefferies, W.4
Monaco, J.J.5
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