Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity and Pin1 Function

Signaling Through Scaffold, Anchoring, and Adaptor Proteins

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The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

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Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent

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Structural basis for phosphoserine-proline recognition by group IV WW domains.

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Function of WW Domains as Phosphoserine- or Phosphothreonine-Binding Modules

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Pin1-Dependent Prolyl Isomerization Regulates Dephosphorylation of Cdc25C and Tau Proteins

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Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c‐Jun towards cyclin D1

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The FHA Domain Is a Modular Phosphopeptide Recognition Motif

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Molecular Chaperone Machines: Chaperone Activities of the Cyclophilin Cyp-40 and the Steroid Aporeceptor-Associated Protein p23

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NeW Wrinkles for an Old Domain

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The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteinsPreprint

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The mitotic peptidyl‐prolyl isomerase, Pin1, interacts with Cdc25 and Plx1

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Requirement of the Prolyl Isomerase Pin1 for the Replication Checkpoint

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The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery

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Phospho-Carboxyl-Terminal Domain Binding and the Role of a Prolyl Isomerase in Pre-mRNA 3′-End Formation

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Requirement for cAMP-PKA Pathway Activation by M Phase-Promoting Factor in the Transition from Mitosis to Interphase

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Phosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism

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Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis.

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Binding of [3H]forskolin to rat brain membranes.

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Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain

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Inhibition of cAMP‐dependent protein kinase plays a key role in the induction of mitosis and nuclear envelope breakdown in mammalian cells.

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The Xenopus Suc1/Cks Protein Promotes the Phosphorylation of G2/M Regulators

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Grabbing phosphoproteins

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A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1

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The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease

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Prolyl cis-trans isomerization as a molecular timer

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Regulation of Raf-1 by direct feedback phosphorylation.

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The Life Cycle of C-Myc: From Synthesis to Degradation

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Prevalent Overexpression of Prolyl Isomerase Pin1 in Human Cancers

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Pinning down proline-directed phosphorylation signaling

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Pin1, a new player in the fate of HIF-1α degradation: an hypothetical mechanism inside vascular damage as Alzheimer’s disease risk factor

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A genetically encoded fluorescent sensor of ERK activity

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Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins

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The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target

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Active Pin1 is a key target of all-trans retinoic acid in acute promyelocytic leukemia and breast cancer

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PIN1 Is an E2F Target Gene Essential for Neu/Ras-Induced Transformation of Mammary Epithelial Cells

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Pinning down cell signaling, cancer and Alzheimer's disease

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Phosphorylation-specific prolyl isomerization: is there an underlying theme?

Wulf, G. M., Finn, G., Suizu, F., & Lu, K. P. (2005) · Nature Cell Biology · doi:10.1038/ncb0505-435 · Cited by 238 · see citing works

The prolyl isomerase Pin1 is a novel prognostic marker in human prostate cancer.

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Prolyl isomerase Pin1 in cancer

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Death-Associated Protein Kinase 1 Phosphorylates Pin1 and Inhibits Its Prolyl Isomerase Activity and Cellular Function

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Prolyl isomerase Pin1: a catalyst for oncogenesis and a potential therapeutic target in cancer

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Pin1 modulates the structure and function of human RNA polymerase IIPreprint

Xu, Y., Hirose, Y., Zhou, X. Z., Lu, K. P., & Manley, J. L. (2003) · Genes & Development · doi:10.1101/gad.1135503 · Cited by 163 · see citing works

Peptidyl‐prolyl isomerases: a new twist to transcription

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Prolyl isomerase Pin1: a promoter of cancer and a target for therapy

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Identification of a Novel Proline-Arginine Motif Involved in CIN85-dependent Clustering of Cbl and Down-regulation of Epidermal Growth Factor Receptors

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The peptidyl-prolyl isomerase Pin1 regulates the stability of granulocyte-macrophage colony-stimulating factor mRNA in activated eosinophils

Shen, Z.-J., Esnault, S. J., & Malter, J. S. (2005) · Nature Immunology · doi:10.1038/ni1266 · Cited by 127 · see citing works

Prolyl isomerase Pin1 as a molecular target for cancer diagnostics and therapeutics

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Epigallocatechin-gallate Suppresses Tumorigenesis by Directly Targeting Pin1

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Structural Analysis of the Mitotic Regulator hPin1 in Solution

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Pin1 and WWP2 regulate GluR2 Q/R site RNA editing by ADAR2 with opposing effects

Marcucci, R., Brindle, J., Paro, S., Casadio, A., Hempel, S., Morrice, N. A., Bisso, A., Keegan, L. P., Sal, G. D., & O’Connell, M. A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.303 · Cited by 121 · see citing works

Induction of cells with cancer stem cell properties from nontumorigenic human mammary epithelial cells by defined reprogramming factors

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Pin1 Regulates Centrosome Duplication, and Its Overexpression Induces Centrosome Amplification, Chromosome Instability, and Oncogenesis

Suizu, F., Ryo, A., Wulf, G. M., Lim, J., & Lu, K. P. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1463-1479.2006 · Cited by 117 · see citing works

Synthesis and antiproliferative evaluation of certain indeno[1,2-c]quinoline derivatives

Tseng, C.-H., Chen, Y., Lu, P., Yang, C.-N., & TZENG, C. ‐. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.12.028 · Cited by 116 · see citing works

Polo-like Kinase 1-mediated Phosphorylation Stabilizes Pin1 by Inhibiting Its Ubiquitination in Human Cells

Eckerdt, F., Yuan, J., Saxena, K., Martin, B. T., Kappel, S., Lindenau, C., Krämer, A., Naumann, S. C., Daum, S., Fischer, G. S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504548200 · Cited by 110 · see citing works

Pin1 inhibitors: Pitfalls, progress and cellular pharmacology

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PIN1 promoter polymorphisms are associated with Alzheimer's disease

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MicroRNA-296-5p (miR-296-5p) functions as a tumor suppressor in prostate cancer by directly targeting Pin1

Lee, K., Lin, F., Hsu, T., Lin, J., Guo, J.-H., Tsai, C.-H., Lee, Y., Lee, Y., Chen, C., Hsiao, M., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.06.001 · Cited by 99 · see citing works

Effective Disruption of Phosphoprotein−Protein Surface Interaction Using Zn(II) Dipicolylamine-Based Artificial Receptors via Two-Point Interaction

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Serine threonine protein kinases of mycobacterial genus: phylogeny to function.

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The Peptidylprolyl cis/trans-Isomerase Pin1 Modulates Stress-induced Dephosphorylation of Tau in Neurons

Galas, M.-C., Dourlen, P., Bégard, S., Ando, K., Blum, D., Hamdane, M., & Buée, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601849200 · Cited by 97 · see citing works

The peptidyl-prolyl isomerase Pin1 determines parathyroid hormone mRNA levels and stability in rat models of secondary hyperparathyroidism

Nechama, M., Uchida, T., Levi, I. M.-Y., Silver, J., & Naveh‐Many, T. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39522 · Cited by 96 · see citing works

A Dynamic View of Domain-Motif Interactions

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The cell cycle as a therapeutic target for Alzheimer's disease

Neve, R. L., & McPhie, D. L. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.09.005 · Cited by 92 · see citing works

Pin1 in Alzheimer's disease: Multiple substrates, one regulatory mechanism?

Balaštík, M., Lim, J., Pastorino, L., & Lu, K. P. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.01.006 · Cited by 90 · see citing works

Proline‐directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's Disease

Lu, K. P., Liou, Y., & Vincent, I. J. (2003) · BioEssays · doi:10.1002/bies.10223 · Cited by 90 · see citing works

Prolyl isomerase, Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer’s disease

Takahashi, K., Uchida, C., Shin, R.-W., Shimazaki, K., & Uchida, T. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7270-0 · Cited by 105 · see citing works

Molecular Crowding Drives Active Pin1 into Nonspecific Complexes with Endogenous Proteins Prior to Substrate Recognition

Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja405244v · Cited by 88 · see citing works

Inositol pyrophosphates: structure, enzymology and function

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Pin1 modulates RNA polymerase II activity during the transcription cyclePreprint

Xu, Y., & Manley, J. L. (2007) · Genes & Development · doi:10.1101/gad.1592807 · Cited by 85 · see citing works

Pin1 and PKMζ Sequentially Control Dendritic Protein Synthesis

Westmark, P. R., Westmark, C. J., Wang, S., Levenson, J. M., O’Riordan, K. J., Bürger, C., & Malter, J. S. (2010) · Science Signaling · doi:10.1126/scisignal.2000451 · Cited by 84 · see citing works

Pin1 allows for differential Tau dephosphorylation in neuronal cells

Hamdane, M., Dourlen, P., Bretteville, A., Sambo, A., Ferreira, S., Ando, K., Kerdraon, O., Bégard, S., Geay, L., Lippens, G. M., et al. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.03.006 · Cited by 82 · see citing works

Synthesis and Antiproliferative Evaluation of Certain Indeno[1,2-c]quinoline Derivatives. Part 2

Tseng, C.-H., TZENG, C. ‐., Yang, C., Lu, P., Chen, H., Li, H., Chuang, Y.-C., Yang, C.-N., & Chen, Y. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm1005447 · Cited by 80 · see citing works

Two pathways mediate interdomain allosteric regulation in pin1

Guo, J., Pang, X., & Zhou, H.-X. (2015) · Structure · doi:10.1016/j.str.2014.11.009 · Cited by 78 · see citing works

The prolyl isomerase Pin1 in breast development and cancer

Wulf, G. M., Ryo, A., Liou, Y., & Lu, K. P. (2003) · Breast Cancer Research · doi:10.1186/bcr572 · Cited by 77 · see citing works

Design of a Hybrid Biosensor for Enhanced Phosphopeptide Recognition Based on a Phosphoprotein Binding Domain Coupled with a Fluorescent Chemosensor

Anai, T., Nakata, E., Koshi, Y., Ojida, A., & Hamachi, I. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0693284 · Cited by 76 · see citing works

Prolyl isomerase Pin1 is highly expressed in Her2-positive breast cancer and regulates erbB2 protein stability

Lam, P. B., Burga, L. N., Wu, B. P., Hofstatter, E. W., Lu, K. P., & Wulf, G. M. (2008) · Molecular Cancer · doi:10.1186/1476-4598-7-91 · Cited by 73 · see citing works

Pin1 Mediates Neural-Specific Activation of the Mitochondrial Apoptotic Machinery

Becker, E. B. E., & Bonni, A. (2006) · Neuron · doi:10.1016/j.neuron.2006.01.034 · Cited by 75 · see citing works

Binding of the Proline-Rich Segment of Myelin Basic Protein to SH3 Domains: Spectroscopic, Microarray, and Modeling Studies of Ligand Conformation and Effects of Posttranslational Modifications

Polverini, E., Rangaraj, G., Libich, D. S., Boggs, J. M., & Harauz, G. (2007) · Biochemistry · doi:10.1021/bi701336n · Cited by 74 · see citing works

Peripheral Blood Mononuclear Cells as a Laboratory to Study Dementia in the Elderly

Arosio, B., D’Addario, C., Gussago, C., Casati, M., Tedone, E., Ferri, E., Nicolini, P., Rossi, P. D., Maccarrone, M., & Mari, D. (2014) · BioMed Research International · doi:10.1155/2014/169203 · Cited by 73 · see citing works

The Peptidyl-Prolyl Isomerase Pin1 Regulates Granulocyte-Macrophage Colony-Stimulating Factor mRNA Stability in T Lymphocytes

Esnault, S. J., Shen, Z.-J., Whitesel, E., & Malter, J. S. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.10.6999 · Cited by 72 · see citing works

Mixed-lineage kinase 3 phosphorylates prolyl-isomerase Pin1 to regulate its nuclear translocation and cellular function

Rangasamy, V., Mishra, R., Sondarva, G. V., Das, S., Lee, T. H., Bakowska, J. C., Tzivion, G., Malter, J. S., Rana, B., Lu, K. P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200804109 · Cited by 72 · see citing works

Peptidyl‐prolyl cis/trans isomerases and transcription: is there a twist in the tail?

Shaw, P. E. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400873 · Cited by 69 · see citing works

Molecular mechanisms of the phospho‐dependent prolyl cis/trans isomerase Pin1

Lippens, G. M., Landrieu, I., & Smet‐Nocca, C. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06057.x · Cited by 68 · see citing works

Pinning down phosphorylated tau and tauopathies

Lim, J., & Lu, K. P. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.003 · Cited by 67 · see citing works

Peptidyl-Prolyl Isomerase Pin1 Is a Cellular Factor Required for Hepatitis C Virus Propagation

Lim, Y.-S., Tran, H. T. L., Park, S.-J., Yim, S.-A., & Hwang, S. B. (2011) · Journal of Virology · doi:10.1128/jvi.02533-10 · Cited by 64 · see citing works

P in1 promotes neuronal death in stroke by stabilizing N otch intracellular domain

Baik, S., Fane, M. E., Park, J. H., Cheng, Y., Fann, D. Y., Yun, U. J., Choi, Y., Park, J., Chai, B. H., Park, J. S., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24347 · Cited by 63 · see citing works

Peptide Bond cis/trans Isomerases: A Biocatalysis Perspective of Conformational Dynamics in Proteins

Schiene‐Fischer, C., Aumüller, T., & Fischer, G. S. (2011) · Topics in current chemistry · doi:10.1007/128_2011_151 · Cited by 63 · see citing works

Pin1 affects Tau phosphorylation in response to Aβ oligomers

Bulbarelli, A., Lonati, E., Cazzaniga, E., Gregori, M., & Masserini, M. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.06.001 · Cited by 58 · see citing works

A Distinct Role for Pin1 in the Induction and Maintenance of Pluripotency

Nishi, M., Akutsu, H., Masui, S., Kondo, A., Nagashima, Y., Kimura, H., Perrem, K., Shigeri, Y., Toyoda, M., Okayama, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.187989 · Cited by 57 · see citing works

Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity

Helander, S., Montecchio, M., Pilstål, R., Su, Y., Kuruvilla, J., Elvén, M., Ziauddin, J. M. E., Anandapadamanaban, M., Cristóbal, S., Lundström, P., et al. (2015) · Structure · doi:10.1016/j.str.2015.10.010 · Cited by 57 · see citing works

Landscape of Pin1 in the cell cycle

Lin, C., Li, H., Lee, Y., Calkins, M. J., Lee, K., Yang, C.-N., & Lu, P. (2015) · Experimental Biology and Medicine · doi:10.1177/1535370215570829 · Cited by 56 · see citing works

Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis

Greenwood, A. I., Rogals, M. J., De, S., Lu, K. P., Kovrigin, E. L., & Nicholson, L. K. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9538-9 · Cited by 56 · see citing works

Inhibition of Pin1 Reduces Glutamate-induced Perikaryal Accumulation of Phosphorylated Neurofilament-H in Neurons

Kesavapany, S., Patel, V., Zheng, Y., Pareek, T. K., Bjelogrlic, M., Albers, W., Amin, N. D., Jaffe, H., Gutkind, J. S., Strong, M. J., et al. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-03-0237 · Cited by 56 · see citing works

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

Yu, J. H., Im, C. Y., & Min, S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00120 · Cited by 56 · see citing works

Pin1 Prolyl Isomerase Regulates Endothelial Nitric Oxide Synthase

Ruan, L., Torres, C. M., Qian, J., Chen, F., MINTZ, J. D., Stepp, D. W., Fulton, D. J., & Venema, R. C. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.213181 · Cited by 55 · see citing works

Phosphorylation of Serine 147 of tis21/BTG2/pc3 by p-Erk1/2 Induces Pin-1 Binding in Cytoplasm and Cell Death

Hong, J. W., Ryu, M. S., & Lim, I. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500318200 · Cited by 54 · see citing works

Combining SPOT Synthesis and Native Peptide Ligation to Create Large Arrays of WW Protein Domains

Toepert, F., Knaute, T., Guffler, S., Pires, J. R., Matzdorf, T., Oschkinat, H., & Schneider‐Mergener, J. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200390298 · Cited by 54 · see citing works

C-terminal domain small phosphatase 1 and MAP kinase reciprocally control REST stability and neuronal differentiation

Nesti, E., Corson, G. M., McCleskey, M., Oyer, J. A., & Mandel, G. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414770111 · Cited by 52 · see citing works

Pin1 Catalyzes Conformational Changes of Thr-187 in p27Kip1 and Mediates Its Stability through a Polyubiquitination Process

Zhou, W., Yang, Q., Low, C. B., Chandrababu, K. B., Wang, Y., Ryo, A., Yao, S. Q., Yang, D., & Liou, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022814 · Cited by 52 · see citing works

Targeting carcinogenesis: A role for the prolyl isomerase Pin1?

Lu, K. P., Suizu, F., Zhou, X. Z., Finn, G., Lam, P. B., & Wulf, G. M. (2006) · Molecular Carcinogenesis · doi:10.1002/mc.20216 · Cited by 52 · see citing works

Relative Resistance of Cdk5-phosphorylated CRMP2 to Dephosphorylation

Cole, A. R., Soutar, M. P. M., Rembutsu, M., van Aalten, L., Hastie, C. J., McLauchlan, H., Peggie, M. W., Balaštík, M., Lu, K. P., & Sutherland, C. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801645200 · Cited by 50 · see citing works

PIN1 in breast development and cancer: a clinical perspective

Rustighi, A., Zannini, A., Campaner, E., Ciani, Y., Piazza, S., & Sal, G. D. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.122 · Cited by 50 · see citing works

Physiological and Pathogenic Roles of Prolyl Isomerase Pin1 in Metabolic Regulations via Multiple Signal Transduction Pathway Modulations

Nakatsu, Y., Matsunaga, Y., Yamamotoya, T., Ueda, K., Inoue, Y., Mori, K., Sakoda, H., Fujishiro, M., Ono, H., Kushiyama, A., et al. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091495 · Cited by 49 · see citing works

Structure and function of the human parvulins Pin1 and Par14/17

Matena, A., Rehic, E., Hönig, D., Kamba, B. E., & Bayer, P. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0137 · Cited by 47 · see citing works

Neurofibrillary degeneration of the Alzheimer-type: an alternate pathway to neuronal apoptosis?

Hamdane, M., Delobel, P., Sambo, A., Smet‐Nocca, C., Bégard, S., Violleau, A., Landrieu, I., Delacourte, A., Lippens, G. M., Flament, S., et al. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(03)00533-1 · Cited by 47 · see citing works

Prolyl Isomerase Pin1 Regulates Axon Guidance by Stabilizing CRMP2A Selectively in Distal Axons

Balaštík, M., Zhou, X. Z., Alberich-Jordà, M., Weissová, R., Žiak, J., Pazyra‐Murphy, M. F., Cosker, K., Machoňová, O., Kozmiková, I., Chen, C.-H., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.026 · Cited by 45 · see citing works

Human Immunodeficiency Virus Type 1 Replication and Regulation of APOBEC3G by Peptidyl Prolyl Isomerase Pin1

Watashi, K., Khan, M. H., Yedavalli, V. R. K., Yeung, M. L., Strebel, K., & Jeang, K. (2008) · Journal of Virology · doi:10.1128/jvi.01017-08 · Cited by 44 · see citing works

Pin1 : A Therapeutic Target in Alzheimer Neurodegeneration

Hamdane, M., Smet‐Nocca, C., Sambo, A., Leroy, A., Wieruszeski, J., Delobel, P., Maurage, C., Ghestem, A., Wintjens, R. T., Bégard, S., et al. (2002) · Journal of Molecular Neuroscience · doi:10.1385/jmn:19:3:275 · Cited by 43 · see citing works

Semidominant Mutations in Reduced Epidermal Fluorescence 4 Reduce Phenylpropanoid Content in Arabidopsis

Stout, J. M., Romero-Severson, E. O., Ruegger, M. O., & Chapple, C. C. S. (2008) · Genetics · doi:10.1534/genetics.107.083881 · Cited by 41 · see citing works

The role of Pin1 in the development and treatment of cancer

Min, S., Zhou, X. Z., & Lu, K. P. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0821-x · Cited by 41 · see citing works

Deficiency of microRNA-628-5p promotes the progression of gastric cancer by upregulating PIN1

Chen, Y., Wu, Y., Yu, S., Yang, H., Wang, X., Zhang, Y., Zhu, S., Jie, M., Liu, C., Li, X., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02766-6 · Cited by 40 · see citing works

Prolyl isomerase Pin1 downregulates tumor suppressor RUNX3 in breast cancer

Tsang, Y.-H. N., Wu, X.-W., Lim, J.-S., Ong, C. W., Salto‐Tellez, M., Ito, K., Ito, Y., & Chen, L.-F. (2012) · Oncogene · doi:10.1038/onc.2012.178 · Cited by 40 · see citing works

Prolyl isomerase Pin1 negatively regulates the stability of SUV39H1 to promote tumorigenesis in breast cancer

Khanal, P., Kim, G., Lim, S., Yun, H., Lee, K. Y., Choi, H., & Choi, H. S. (2013) · The FASEB Journal · doi:10.1096/fj.13-236851 · Cited by 38 · see citing works

Pin1 acts as a negative regulator of the G2/M transition through an interplay with the Aurora A/hBora complex

Lee, Y., Que, J., Chen, Y., Lin, J., Liou, Y.-C., Liao, P.-C., Liu, Y., Lee, K., Lin, L.-C., Hsiao, M., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.121368 · Cited by 37 · see citing works

Peptidyl-Prolyl Isomerase Pin1 Markedly Enhances the Oncogenic Activity of the Rel Proteins in the Nuclear Factor-κB Family

Fan, G., Fan, Y., Gupta, N., Matsuura, I., Liu, F., Zhou, X. Z., Lu, K. P., & Gélinas, C. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4117 · Cited by 37 · see citing works

Regulation of mitochondrial apoptosis by Pin1 in cancer and neurodegeneration

Sorrentino, G., Comel, A., Mantovani, F., & Sal, G. D. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.08.003 · Cited by 36 · see citing works

p66Shc in Cardiovascular Pathology

Haslem, L., Hays, J. M., & Hays, F. A. (2022) · Cells · doi:10.3390/cells11111855 · Cited by 37 · see citing works

Gonadotrophin‐Releasing Hormone Signalling Downstream of Calmodulin

Melamed, P., Savulescu, D. M., Lim, S. X., Wijeweera, A., Luo, Z., Luo, M., & Pnueli, L. (2012) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2012.02359.x · Cited by 36 · see citing works

Synthetic Receptors for the Differentiation of Phosphorylated Peptides with Nanomolar Affinities

Grauer, A., Riechers, A., Ritter, S., & König, B. (2008) · Chemistry - A European Journal · doi:10.1002/chem.200800432 · Cited by 36 · see citing works

Pin1 Facilitates the Phosphorylation-Dependent Ubiquitination of SF-1 To Regulate Gonadotropin β-Subunit Gene Transcription

Luo, Z., Wijeweera, A., Oh, Y., Liou, Y., & Melamed, P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00807-09 · Cited by 36 · see citing works

Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1

Wang, X., Mahoney, B. J., Zhang, M., Zintsmaster, J. S., & Peng, J. W. (2015) · Structure · doi:10.1016/j.str.2015.08.019 · Cited by 35 · see citing works

Oncogenic Hijacking of the PIN1 Signaling Network

Zannini, A., Rustighi, A., Campaner, E., & Sal, G. D. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00094 · Cited by 35 · see citing works

Phosphorylation-Specific Peptidyl-Prolyl Isomerization of Neuronal Cytoskeletal Proteins by Pin1: Implications for Therapeutics in Neurodegeneration

Rudrabhatla, P., & Pant, H. C. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1243 · Cited by 34 · see citing works

Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity

Function, P., Liou, Y.-C., Noel, J. P., & Lu, K. P. (2001)

Function of WW Domains as Phosphoserine- or Phosphothreonine-Binding Modules

Lu, P., Zhou, X. Z., Shen, M., & Lu, K. P. (1999) · Science · doi:10.1126/science.283.5406.1325 · Cited by 683 · see citing works

Regulation of Pin1 peptidyl‐prolyl cis/trans isomerase activity by its WW binding module on a multi‐phosphorylated peptide of Tau protein

Smet‐Nocca, C., Wieruszeski, J., Buée, L., Landrieu, I., & Lippens, G. M. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.06.048 · Cited by 61 · see citing works

Non-catalytic participation of the Pin1 peptidyl-prolyl isomerase domain in target binding

Innes, B. T., Bailey, M. L., Brandl, C. J., Shilton, B. H., & Litchfield, D. W. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00018 · Cited by 41 · see citing works

Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1

Lee, Y. M., & Liou, Y. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00469 · Cited by 40 · see citing works