(Q40911426)

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Enhanced susceptibility to cytotoxic T lymphocytes without increase of MHC class I antigen expression after conditional overexpression of heat shock protein 70 in target cells

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Enhanced susceptibility to cytotoxic T lymphocytes without increase of MHC class I antigen expression after conditional overexpression of heat shock protein 70 in target cells (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

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Europe PubMed Central

PubMed publication ID

24 September 2017

author name string

Dressel R

1

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Europe PubMed Central

PubMed publication ID

24 September 2017

Lübbers M

2

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Europe PubMed Central

PubMed publication ID

24 September 2017

Herr W

4

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Europe PubMed Central

PubMed publication ID

24 September 2017

Günther E

5

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Europe PubMed Central

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24 September 2017

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publication date

1 December 1999

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Europe PubMed Central

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24 September 2017

European Journal of Immunology

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Europe PubMed Central

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24 September 2017

29

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Europe PubMed Central

PubMed publication ID

24 September 2017

12

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Europe PubMed Central

PubMed publication ID

24 September 2017

3925-3935

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Europe PubMed Central

PubMed publication ID

24 September 2017

Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world

1 reference

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Isolation of processed, H-2Kb-binding ovalbumin-derived peptides associated with the stress proteins HSP70 and gp96.

1 reference

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Mechanisms of MHC class I--restricted antigen processing

1 reference

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21 January 2018

Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96/GRP94.

1 reference

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21 January 2018

The endoplasmic reticulum-resident stress protein gp96 binds peptides translocated by TAP.

1 reference

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21 January 2018

Protein disulfide isomerase is the dominant acceptor for peptides translocated into the endoplasmic reticulum

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

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Stress protein (hsp73)-mediated, TAP-independent processing of endogenous, truncated SV40 large T antigen for Db-restricted peptide presentation

1 reference

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Hsp72-mediated augmentation of MHC class I surface expression and endogenous antigen presentation

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21 January 2018

Tumor immunogenicity is determined by the mechanism of cell death via induction of heat shock protein expression

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21 January 2018

Comparative analysis of the three major histocompatibility complex-linked heat shock protein 70 (Hsp70) genes of the rat.

1 reference

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21 January 2018

Genetic aspects of the hsp70 multigene family in vertebrates

1 reference

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Transcriptional activation by tetracyclines in mammalian cells

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Unusual expression and localization of heat-shock proteins in human tumor cells

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Analysis of antigens recognized on human melanoma cells by A2-restricted cytolytic T lymphocytes (CTL).

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Two tyrosinase nonapeptides recognized on HLA-A2 melanomas by autologous cytolytic T lymphocytes

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An HLA-A2-restricted tyrosinase antigen on melanoma cells results from posttranslational modification and suggests a novel pathway for processing of membrane proteins

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21 January 2018

Effect of heat shock on susceptibility of normal lymphoblasts and of a heat shock protein 70-defective tumour cell line to cytotoxic T lymphocytes in vitro

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Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts

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21 January 2018

Constitutive expression of heat-shock protein 70 in mammalian cells confers thermoresistance

1 reference

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Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene

1 reference

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Heat shock proteins increase resistance to apoptosis.

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Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases.

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Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

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21 January 2018

Identifiers

10.1002/(SICI)1521-4141(199912)29:12<3925::AID-IMMU3925>3.0.CO;2-S

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

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