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Tumor Suppressor Par-4 = Structural Features, Molecular Mechanisms and Function /
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Tumor Suppressor Par-4/ edited by Vivek M. Rangnekar.
其他題名:
Structural Features, Molecular Mechanisms and Function /
其他作者:
Rangnekar, Vivek M.
面頁冊數:
X, 323 p. 84 illus., 81 illus. in color.online resource. :
Contained By:
Springer Nature eBook
標題:
Internal Medicine. -
電子資源:
https://doi.org/10.1007/978-3-030-73572-2
ISBN:
9783030735722
Tumor Suppressor Par-4 = Structural Features, Molecular Mechanisms and Function /
Tumor Suppressor Par-4
Structural Features, Molecular Mechanisms and Function /[electronic resource] :edited by Vivek M. Rangnekar. - 1st ed. 2022. - X, 323 p. 84 illus., 81 illus. in color.online resource.
Discovery and Overview of Par-4 -- Par-4 in cell cycle regulation -- Conformational studies of the Par-4 C-terminal Domain -- Structural analysis of Par-4 and crystallographic analysis of the regulatory domain -- Regulation of Par-4 by Ubiquitinases -- REGULATION OF PAR-4 FUNCTION BY PHOSPHORYLATION -- Role of Par-4 in GRP78 translocation -- PAR-4 in the regulation of stem cell death and embryo development -- RASSF2 and the PAR-4 connection -- Regulation of tumor suppressor Par-4 by ceramide -- PAWR as a direct SRC-1/HOXC11 suppression target -- Index.
Par-4 is a tumor suppressor protein first discovered and identified in 1993 by Dr. Vivek Rangnekar’s laboratory in prostate cancer cells undergoing apoptosis. Par-4 (later also known as PAWR) is a naturally occurring tumor suppressor. Studies have indicated that Par-4 selectively induces apoptosis in cancer cells while leaving normal, healthy, cells unaffected. Mechanisms contributing to the cancer-selective action of Par-4 have been associated with protein kinase A activation of intracellular Par-4 in cancer cells or GRP78 expression primarily on the surface of cancer cells. Par-4 is downregulated, inactivated or mutated in diverse cancers. This first of two volumes will be the first on the market on the topic of Par-4, and will provide the opportunity for researchers to discuss the future direction of studies, broaden the scope of research, and contribute a more complete understanding of the molecule’s structural features, key functional domains, regulation and relevant basic and clinical/translational facets.
ISBN: 9783030735722
Standard No.: 10.1007/978-3-030-73572-2doiSubjects--Topical Terms:
668583
Internal Medicine.
LC Class. No.: R850.A1-854
Dewey Class. No.: 610.72
Tumor Suppressor Par-4 = Structural Features, Molecular Mechanisms and Function /
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Discovery and Overview of Par-4 -- Par-4 in cell cycle regulation -- Conformational studies of the Par-4 C-terminal Domain -- Structural analysis of Par-4 and crystallographic analysis of the regulatory domain -- Regulation of Par-4 by Ubiquitinases -- REGULATION OF PAR-4 FUNCTION BY PHOSPHORYLATION -- Role of Par-4 in GRP78 translocation -- PAR-4 in the regulation of stem cell death and embryo development -- RASSF2 and the PAR-4 connection -- Regulation of tumor suppressor Par-4 by ceramide -- PAWR as a direct SRC-1/HOXC11 suppression target -- Index.
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Par-4 is a tumor suppressor protein first discovered and identified in 1993 by Dr. Vivek Rangnekar’s laboratory in prostate cancer cells undergoing apoptosis. Par-4 (later also known as PAWR) is a naturally occurring tumor suppressor. Studies have indicated that Par-4 selectively induces apoptosis in cancer cells while leaving normal, healthy, cells unaffected. Mechanisms contributing to the cancer-selective action of Par-4 have been associated with protein kinase A activation of intracellular Par-4 in cancer cells or GRP78 expression primarily on the surface of cancer cells. Par-4 is downregulated, inactivated or mutated in diverse cancers. This first of two volumes will be the first on the market on the topic of Par-4, and will provide the opportunity for researchers to discuss the future direction of studies, broaden the scope of research, and contribute a more complete understanding of the molecule’s structural features, key functional domains, regulation and relevant basic and clinical/translational facets.
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