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Volumn 10, Issue 1, 1998, Pages 103-109

Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GLUCOSE REGULATED PROTEIN; PEPTIDE; TUMOR ANTIGEN;

EID: 0032007324     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(98)80039-3     Document Type: Article
Times cited : (123)

References (51)
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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
    • 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.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8064-8069
    • Day, P.M.1    Yewdell, J.W.2    Porgador, A.3    Germain, R.N.4    Bennink, J.R.5
  • 48
    • 0031030792 scopus 로고    scopus 로고
    • Constitutive macropinocytosis allows TAP-dependent major histocompatability complex class I presentation of exogenous soluble antigen by bone marrow-derived dendritic cells
    • 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
    • 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.
    • (1997) Eur J Immunol , vol.27 , pp. 280-288
    • Norbury, C.C.1    Chambers, B.J.2    Prescott, A.R.3    Ljunggren H-G4    Watt, C.5
  • 49
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    • Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages
    • 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.
    • (1995) Immunity , vol.3 , pp. 783-791
    • Norbury, C.C.1    Hewlett, L.J.2    Prescott, A.R.3    Shastri, N.4    Watts, C.5
  • 50
    • 0028920154 scopus 로고
    • The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack
    • 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.
    • (1995) J Cell Biol , vol.129 , pp. 309-319
    • Miesenböck, G.1    Rothman, J.E.2
  • 51
    • 0031046750 scopus 로고    scopus 로고
    • Novel peptide-binding proteins and peptide transport in normal and TAP-deficient microsomes
    • 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
    • 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.
    • (1997) Biochemistry , vol.36 , pp. 856-863
    • Marusina, K.1    Reid, G.2    Gabathuier, R.3    Jefferies, W.4    Monaco, J.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.