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Yasumasa Ishida
Researcher at Nara Institute of Science and Technology
Publications - 33
Citations - 7407
Yasumasa Ishida is an academic researcher from Nara Institute of Science and Technology. The author has contributed to research in topics: Gene & Programmed cell death. The author has an hindex of 19, co-authored 32 publications receiving 6735 citations. Previous affiliations of Yasumasa Ishida include Howard Hughes Medical Institute & Kyoto University.
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Induced expression of PD-1, a novel member of the immunoglobulin gene superfamily, upon programmed cell death.
TL;DR: The results suggest that activation of the PD‐1 gene may be involved in the classical type of programmed cell death.
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Stimulation of CD25 + CD4 + regulatory T cells through GITR breaks immunological self-tolerance
TL;DR: GITR plays a key role in dominant immunological self-tolerance maintained by CD25+CD4+ regulatory T cells and could be a suitable molecular target for preventing or treating autoimmune disease.
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Expression of the PD-1 antigen on the surface of stimulated mouse T and B lymphocytes
Yasutoshi Agata,Akemi Kawasaki,Hiroyuki Nishimura,Yasumasa Ishida,Takeshi Tsubata,Hideo Yagita,Tasuku Honjo +6 more
TL;DR: The results suggest that the expression of thePD-1 antigen is tightly regulated and induced by signal transduction through the antigen receptor and do not exclude the possibility that the PD- 1 antigen may play a role in clonal selection of lymphocytes although PD-1 expression is not required for the common pathway of apoptosis.
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Inhibition of Carnitine Palmitoyltransferase I Augments Sphingolipid Synthesis and Palmitate-induced Apoptosis
TL;DR: Results indicate that apoptosis induced by palmitate or stearate is correlated with de novo synthesis of ceramide and inhibition of CPT I by etomoxir enhanced palmitates-induced cell death and led to a further increase in ceramide synthesis.
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Structure and chromosomal localization of the human PD-1 gene (PDCD1)
TL;DR: The deduced amino acid sequence of human PD-1 was 60% identical to the mouse counterpart, and a putative tyrosine kinase-association motif was well conserved.