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Prolyl isomerase, Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer's disease.脯氨酰异构酶Pin1：癌症、哮喘和阿尔茨海默病中翻译后修饰及生理底物的新发现
Cell Mol Life Sci. 2008 Feb;65(3):359-75. doi: 10.1007/s00018-007-7270-0.
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The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production.脯氨酰异构酶Pin1调节淀粉样前体蛋白的加工和β淀粉样蛋白的产生。
Nature. 2006 Mar 23;440(7083):528-34. doi: 10.1038/nature04543.
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Phosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism.磷酸化依赖性脯氨酰异构化：一种新型信号调节机制。
Cell Mol Life Sci. 1999 Nov 30;56(9-10):788-806. doi: 10.1007/s000180050026.
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Tau pathology modulates Pin1 post-translational modifications and may be relevant as biomarker.tau 病理学调节 Pin1 的翻译后修饰，可能作为生物标志物具有相关性。
Neurobiol Aging. 2013 Mar;34(3):757-69. doi: 10.1016/j.neurobiolaging.2012.08.004. Epub 2012 Aug 25.
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Cancer and Alzheimer's disease inverse relationship: an age-associated diverging derailment of shared pathways.癌症与老年痴呆症呈负相关：共享通路在年龄相关的分歧中脱轨。
Mol Psychiatry. 2021 Jan;26(1):280-295. doi: 10.1038/s41380-020-0760-2. Epub 2020 May 7.
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Pin1 in Alzheimer's disease.Pin1与阿尔茨海默病
J Neurochem. 2006 Sep;98(6):1697-706. doi: 10.1111/j.1471-4159.2006.03995.x.
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The Peptidyl-Prolyl isomerase, Pin1, associates with Protein Kinase C θ a critical Phospho-Thr-Pro motif in the V3 regulatory domain.肽基脯氨酰顺反异构酶 Pin1 与蛋白激酶 Cθ 结合，在 V3 调节域的关键磷酸化 Thr-Pro 基序中。
Front Immunol. 2023 Mar 8;14:1126464. doi: 10.3389/fimmu.2023.1126464. eCollection 2023.
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Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin1 substrate recognition.磷酸化在决定丝氨酸/苏氨酸-脯氨酸基序的主链动力学及Pin1底物识别中的作用。
Biochemistry. 1998 Apr 21;37(16):5566-75. doi: 10.1021/bi973060z.
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[Unexpected roles of the peptidyl-prolyl cis/trans isomerase Pin1].肽基脯氨酰顺反异构酶Pin1的意外作用
Med Sci (Paris). 2003 Dec;19(12):1251-8. doi: 10.1051/medsci/200319121251.
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Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins.Pin1 依赖性脯氨酰异构化调节 Cdc25C 和 tau 蛋白的去磷酸化。
Mol Cell. 2000 Oct;6(4):873-83. doi: 10.1016/s1097-2765(05)00083-3.
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MYC Oncogene: A Druggable Target for Treating Cancers with Natural Products.MYC 癌基因：天然产物治疗癌症的可用药靶。
Aging Dis. 2024 Apr 1;15(2):640-697. doi: 10.14336/AD.2023.0520.
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The role of peptidyl-prolyl isomerase Pin1 in neuronal signaling in epilepsy.肽基脯氨酰异构酶Pin1在癫痫神经元信号传导中的作用。
Front Mol Neurosci. 2022 Oct 11;15:1006419. doi: 10.3389/fnmol.2022.1006419. eCollection 2022.
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FKBP51 modulates hippocampal size and function in post-translational regulation of Parkin.FKBP51 在后 Parkin 的翻译后调控中调节海马体体积和功能。
Cell Mol Life Sci. 2022 Mar 4;79(3):175. doi: 10.1007/s00018-022-04167-8.
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The Suppression of Pin1-Alleviated Oxidative Stress through the p38 MAPK Pathway in Ischemia- and Reperfusion-Induced Acute Kidney Injury.缺血再灌注诱导的急性肾损伤中通过 p38 MAPK 通路抑制 Pin1 减轻氧化应激。
Oxid Med Cell Longev. 2021 Jul 30;2021:1313847. doi: 10.1155/2021/1313847. eCollection 2021.
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MYC: a multipurpose oncogene with prognostic and therapeutic implications in blood malignancies.MYC：一种具有预后和治疗意义的多效癌基因，在血液恶性肿瘤中。
J Hematol Oncol. 2021 Aug 9;14(1):121. doi: 10.1186/s13045-021-01111-4.
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Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.结构分析表明，Ess1 通过双价锚定机制使 RNA 聚合酶 II 的羧基末端结构域发生构象变化。
Commun Biol. 2021 Mar 25;4(1):398. doi: 10.1038/s42003-021-01906-8.
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LigGrep: a tool for filtering docked poses to improve virtual-screening hit rates.LigGrep：一种用于筛选对接构象以提高虚拟筛选命中率的工具。
J Cheminform. 2020 Nov 11;12(1):69. doi: 10.1186/s13321-020-00471-2.
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PIN1 Provides Dynamic Control of MYC in Response to Extrinsic Signals.PIN1 对外源信号作出响应，对 MYC 进行动态调控。
Front Cell Dev Biol. 2020 Apr 2;8:224. doi: 10.3389/fcell.2020.00224. eCollection 2020.
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Mixed lineage kinase 3 inhibition induces T cell activation and cytotoxicity.混合谱系激酶 3 抑制诱导 T 细胞活化和细胞毒性。
Proc Natl Acad Sci U S A. 2020 Apr 7;117(14):7961-7970. doi: 10.1073/pnas.1921325117. Epub 2020 Mar 24.
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Post-translational Modifications of the Peptidyl-Prolyl Isomerase Pin1.肽基脯氨酰异构酶Pin1的翻译后修饰
Front Cell Dev Biol. 2020 Mar 4;8:129. doi: 10.3389/fcell.2020.00129. eCollection 2020.
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