Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics

Peptidyl-prolyl isomerase (PIN1) specifically binds and isomerizes the phosphorylated serine/threonine–proline (pSer/Thr–Pro) motif, which results in the alteration of protein structure, function, and stability. The altered structure and function of these phosphorylated proteins regulated by PIN1 ar...
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Autor*in:	Ji Hoon Yu [verfasserIn] Chun Young Im [verfasserIn] Sang-Hyun Min [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	cancer therapeutics PIN1 PIN1 inhibitor proline-directed phosphorylation prolyl isomerase tumorigenesis

Übergeordnetes Werk:	In: Frontiers in Cell and Developmental Biology - Frontiers Media S.A., 2014, 8(2020)
Übergeordnetes Werk:	volume:8 ; year:2020

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fcell.2020.00120

Katalog-ID:	DOAJ011637811

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spelling	10.3389/fcell.2020.00120 doi (DE-627)DOAJ011637811 (DE-599)DOAJ6d1f7d06b1934db5bf2662cbadf5eb19 DE-627 ger DE-627 rakwb eng QH301-705.5 Ji Hoon Yu verfasserin aut Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peptidyl-prolyl isomerase (PIN1) specifically binds and isomerizes the phosphorylated serine/threonine–proline (pSer/Thr–Pro) motif, which results in the alteration of protein structure, function, and stability. The altered structure and function of these phosphorylated proteins regulated by PIN1 are closely related to cancer development. PIN1 is highly expressed in human cancers and promotes cancer as well as cancer stem cells by breaking the balance of oncogenes and tumor suppressors. In this review, we discuss the roles of PIN1 in cancer and PIN1-targeted small-molecule compounds. cancer therapeutics PIN1 PIN1 inhibitor proline-directed phosphorylation prolyl isomerase tumorigenesis Biology (General) Chun Young Im verfasserin aut Sang-Hyun Min verfasserin aut In Frontiers in Cell and Developmental Biology Frontiers Media S.A., 2014 8(2020) (DE-627)770398138 (DE-600)2737824-X 2296634X nnns volume:8 year:2020 https://doi.org/10.3389/fcell.2020.00120 kostenfrei https://doaj.org/article/6d1f7d06b1934db5bf2662cbadf5eb19 kostenfrei https://www.frontiersin.org/article/10.3389/fcell.2020.00120/full kostenfrei https://doaj.org/toc/2296-634X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2020
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callnumber-first	Q - Science
author	Ji Hoon Yu
spellingShingle	Ji Hoon Yu misc QH301-705.5 misc cancer therapeutics misc PIN1 misc PIN1 inhibitor misc proline-directed phosphorylation misc prolyl isomerase misc tumorigenesis misc Biology (General) Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics
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topic_title	QH301-705.5 Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics cancer therapeutics PIN1 PIN1 inhibitor proline-directed phosphorylation prolyl isomerase tumorigenesis
topic	misc QH301-705.5 misc cancer therapeutics misc PIN1 misc PIN1 inhibitor misc proline-directed phosphorylation misc prolyl isomerase misc tumorigenesis misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc cancer therapeutics misc PIN1 misc PIN1 inhibitor misc proline-directed phosphorylation misc prolyl isomerase misc tumorigenesis misc Biology (General)
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title	Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics
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title_full	Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics
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title_sort	function of pin1 in cancer development and its inhibitors as cancer therapeutics
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title_auth	Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics
abstract	Peptidyl-prolyl isomerase (PIN1) specifically binds and isomerizes the phosphorylated serine/threonine–proline (pSer/Thr–Pro) motif, which results in the alteration of protein structure, function, and stability. The altered structure and function of these phosphorylated proteins regulated by PIN1 are closely related to cancer development. PIN1 is highly expressed in human cancers and promotes cancer as well as cancer stem cells by breaking the balance of oncogenes and tumor suppressors. In this review, we discuss the roles of PIN1 in cancer and PIN1-targeted small-molecule compounds.
abstractGer	Peptidyl-prolyl isomerase (PIN1) specifically binds and isomerizes the phosphorylated serine/threonine–proline (pSer/Thr–Pro) motif, which results in the alteration of protein structure, function, and stability. The altered structure and function of these phosphorylated proteins regulated by PIN1 are closely related to cancer development. PIN1 is highly expressed in human cancers and promotes cancer as well as cancer stem cells by breaking the balance of oncogenes and tumor suppressors. In this review, we discuss the roles of PIN1 in cancer and PIN1-targeted small-molecule compounds.
abstract_unstemmed	Peptidyl-prolyl isomerase (PIN1) specifically binds and isomerizes the phosphorylated serine/threonine–proline (pSer/Thr–Pro) motif, which results in the alteration of protein structure, function, and stability. The altered structure and function of these phosphorylated proteins regulated by PIN1 are closely related to cancer development. PIN1 is highly expressed in human cancers and promotes cancer as well as cancer stem cells by breaking the balance of oncogenes and tumor suppressors. In this review, we discuss the roles of PIN1 in cancer and PIN1-targeted small-molecule compounds.
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title_short	Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics
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