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

Signaling Through Scaffold, Anchoring, and Adaptor Proteins

Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256

[11] Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates

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[3] Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations

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A human peptidyl–prolyl isomerase essential for regulation of mitosis

Lu, K. P., Hanes, S. D., & Hunter, T. (1996) · Nature · doi:10.1038/380544a0 · Cited by 908

Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism

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

Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721

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

Ranganathan, R., Lu, K. P., Hunter, T. R., & Noel, J. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80273-1 · Cited by 703

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

Verdecia, M. A., Bowman, M. E., Lu, K. P., Hunter, T. R., & Noel, J. P. (2000) · Nature Structural Biology · doi:10.1038/77929 · Cited by 696

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 688

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

Zhou, X. Z., Kops, O., Werner, A., Lu, P., Shen, M., Stoller, G., Küllertz, G., Stark, M. J. R., Fischer, G. S., & Lu, K. P. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00083-3 · Cited by 543

CRABP1-complexes in exosome secretion

Nhieu, J., Wei, C.-W., Ludwig, M., Drake, J. M., & Wei, L. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01749-w · Cited by 5

Trypanosomatid P in1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation

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Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain

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Role of PIN1 in human pathology: Cellular regulation, pathogenesis and therapeutic implications (Review)

Maggio, J., Armando, R. G., Balcone, L., Vilarullo, R., Casco, M. D. P., Gómez, D. L. M., & Gomez, D. E. (2023) · World Academy of Sciences Journal · doi:10.3892/wasj.2023.220 · Cited by 3

Binding of an RNA pol II Ligand to the WW Domain of Pin1 Using Molecular Dynamics Docking Simulations

Ng, C., Oehme, D. P., Kato, Y. S., Tanokura, M., & Brownlee, R. T. C. (2009) · Journal of Chemical Theory and Computation · doi:10.1021/ct900190n · Cited by 4

Achieving Peptide Binding Specificity and Promiscuity by Loops: Case of the Forkhead-Associated Domain

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Hepatic Pin1 Expression, Particularly in Nuclei, Is Increased in NASH Patients in Accordance with Evidence of the Role of Pin1 in Lipid Accumulation Shown in Hepatoma Cell Lines

Kanna, M., Nakatsu, Y., Yamamotoya, T., Kushiyama, A., Fujishiro, M., Sakoda, H., Ono, H., Arihiro, K., & Asano, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108847 · Cited by 4

Competitive Binding of Proline-Rich Sequences by SH3, WW, and Other Functionally Related Protein Domains

Sudol, M., & Bedford, M. T. (2005) · Springer eBooks · doi:10.1007/0-387-24532-4_9 · Cited by 4

Dissecting the functional behavior of the differentially phosphorylated prolyl isomerase, Pin1

Kay, D. F., Ozleyen, A., Heras, C. M. D. L., Doveston, R. G., & Leney, A. C. (2024) · Protein Science · doi:10.1002/pro.5138 · Cited by 3

Expression of Pin1, a Peptidyl-Prolyl Isomerase, in the Ovaries of eCG/hCG-Treated Immature Female Mice

Shimizu, T., Akiyama, H., Abe, Y., Sasada, H., Sato, E., Miyamoto, A., & Uchida, T. (2006) · Journal of Reproduction and Development · doi:10.1262/jrd.17057 · Cited by 3

Pin1 Protects Against Alzheimer's Disease: One Goal, Multiple Mechanisms

Pastorino, L., Kondo, A., Zhen, X., & Lu, K. P. (2013) · InTech eBooks · doi:10.5772/55085 · Cited by 2

Pin1 in cancer: Signaling mechanisms, structural basis and advances in inhibitor development

Wu, W., Mo, J., Su, J., Zhu, G., Zhang, Y., Wang, Y., & Zhang, J. (2026) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2026.119171 · Cited by 1

Molecular Mechanisms of Parathyroid Hormone Synthesis

Naveh‐Many, T., & Nechama, M. (2012) · Springer eBooks · doi:10.1007/978-1-4419-5550-0_1 · Cited by 1

The molecular mechanisms of peptidyl-prolyl cis/trans isomerase Pin1 and its relevance to kidney disease

Wu, S., Zou, Y., Tan, X., Yang, S., Chen, T., Zhang, J., Xu, X., Wang, F., & Li, W. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1373446 · Cited by 1

Atomistic Modelling of Phosphopeptide Recognition for Modular Domains

Chang, C. A., & Huang, Y. M. (2013) · Annual reports in computational chemistry · doi:10.1016/b978-0-444-62672-1.00003-0 · Cited by 1

Regulation und Koordination der Proteinkinase A im cAMP-vermittelten Signalweg

Zenn, H.-M. (2011) · Kobra (Universitätsbibliothek Kassel) · Cited by 1

Neuronal Cytoskeleton Regulation and Neurodegeneration

Zheng, Y., Amin, N. D., Rudrabhatla, P., Kesavapany, S., & Pant, H. C. (2009) · Springer eBooks · doi:10.1007/978-0-387-87995-6_6 · Cited by 1

Targets and Small Molecules Against Tauopathies. Part 1: From Genes to Soluble, Aggregation-Prone Tau Proteins

Seneci, P. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50015-5

Structural biology of transcriptional regulation in the c-Myc network

Helander, S. (2014) · Linköping University Electronic Press eBooks · doi:10.3384/diss.diva-106185

Human notch1 and pin1 unveil a molecular circuitry involved in tumorigenesis

Tiberi, L. (2008) · OpenstarTs (Univeristy of Trieste https://www.units.it/)

Expression von Peptidyl-prolyl cis/trans isomerase NIMA-interacting 1 (PIN1) in Blasten von Patienten mit akuter myeloischer Leukämie

Hangen, H. (2011) · doi:10.53846/goediss-1021

DEVELOPMENT OF A LIVE-CELL ASSAY PLATFORM TO STUDY PROTEIN-PROTEIN INTERACTIONS OF MICROTUBULE-ASSOCIATED PROTEIN TAU

Nykänen, N.-P. (2012) · UEF eRepo (University of Eastern Finland)

Post-transcriptional Regulation of Parathyroid Hormone Gene Expression in Health and Disease

Naveh‐Many, T. (2015) · Springer eBooks · doi:10.1007/978-3-319-25124-0_11

Regulation of RUNX3 in gastric and breast cancer

Tsang, Y. N. (2012) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)

A Correction to the Perspective Titled: "PINing for Things Past" by Todd Charlton Sacktor

(2010) · Science Signaling · doi:10.1126/scisignal.3114er1

Investigation of PIN1 as a Genetic Modifier in Li-Fraumeni Syndrome

Villani, A. (2015) · TSpace (University of Toronto)

Pin1 Catalytic and WW Domain Ligands

Chen, X. R. (2011) · VTechWorks (Virginia Tech)

Function and Regulation of Septins During Mammalian Cell Division

Estey, M. P. (2012) · TSpace (University of Toronto)

Pin1: WW domain ligands, catalytic inhibitors, and the mechanism

Mercedes-Camacho, A. Y. (2011) · VTechWorks (Virginia Tech)

Regulation of Early Events in Cell Cycle Progression by Hedgehog Signaling in CNS Development and Tumorigenesis

Kenney, A. M., & Rowitch, D. H. (2007) · Springer eBooks · doi:10.1007/0-387-33777-6_15

Non-POU Domain-Containing Octamer-Binding (NONO) Protein Stability Regulated by PIN1 is Crucial for Breast Cancer Tumorigenicity Via the MAPK/β-Catenin PathwayPreprint

Lone, B. A., Siraj, F., Sharma, I., Ahmad, F., Nagar, P., & Pokharel, Y. R. (2022) · Research Square · doi:10.21203/rs.3.rs-1392189/v1

Pin1

Lee, T. H., Zhou, X. Z., & Lu, K. P. (2010) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a002516.01

Data from 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. (2023) · doi:10.1158/0008-5472.c.6499086.v1

PTH-dependent stabilization of RANKL mRNA is associated with increased phosphorylation of the KH-type splicing regulatory protein

Yao, G., Zhu, M., & Insogna, K. L. (2024) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2024.112412

Structural and functional characterization of Pin1BP1: A novel Pin1-interacting protein regulating apoptosis

Lin, W., Lee, Y., Cheng, H.-C., Lo, H.-H., Mehmood, A., Yang, C., & Lu, P. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.145587

Additional file 2 of CRABP1-complexes in exosome secretion

Nhieu, J., Wei, C.-W., Ludwig, M., Drake, J. M., & Wei, L.-N. (2024) · Figshare · doi:10.6084/m9.figshare.26754898

Additional file 2 of Long-term normalization of calcineurin activity in model mice rescues Pin1 and attenuates Alzheimer’s phenotypes without blocking peripheral T cell IL-2 response

Stallings, N. R., O’Neal, M. A., Hu, J., Shen, Z.-J., & Malter, J. S. (2024) · Figshare · doi:10.6084/m9.figshare.26628040

Additional file 1 of Long-term normalization of calcineurin activity in model mice rescues Pin1 and attenuates Alzheimer’s phenotypes without blocking peripheral T cell IL-2 response

Stallings, N. R., O’Neal, M. A., Hu, J., Shen, Z.-J., & Malter, J. S. (2024) · Figshare · doi:10.6084/m9.figshare.26628037

Additional file 3 of CRABP1-complexes in exosome secretion

Nhieu, J., Wei, C.-W., Ludwig, M., Drake, J. M., & Wei, L.-N. (2024) · Figshare · doi:10.6084/m9.figshare.26754901

Additional file 1 of CRABP1-complexes in exosome secretion

Nhieu, J., Wei, C.-W., Ludwig, M., Drake, J. M., & Wei, L.-N. (2024) · Figshare · doi:10.6084/m9.figshare.26754895

Additional file 4 of CRABP1-complexes in exosome secretion

Nhieu, J., Wei, C.-W., Ludwig, M., Drake, J. M., & Wei, L.-N. (2024) · Figshare · doi:10.6084/m9.figshare.26754904

Additional file 4 of Long-term normalization of calcineurin activity in model mice rescues Pin1 and attenuates Alzheimer’s phenotypes without blocking peripheral T cell IL-2 response

Stallings, N. R., O’Neal, M. A., Hu, J., Shen, Z.-J., & Malter, J. S. (2024) · Figshare · doi:10.6084/m9.figshare.26628046

Additional file 3 of Long-term normalization of calcineurin activity in model mice rescues Pin1 and attenuates Alzheimer’s phenotypes without blocking peripheral T cell IL-2 response

Stallings, N. R., O’Neal, M. A., Hu, J., Shen, Z.-J., & Malter, J. S. (2024) · Figshare · doi:10.6084/m9.figshare.26628043

Role of the prolyl isomerase Pin1 in the pathogenesis of Parkinson's disease and neuroprotection by novel targeted compounds in pre-clinical animal models of the disease

Ghosh, A. (2012) · Iowa State University Digital Repository (Iowa State University) · doi:10.31274/etd-180810-1769

Effet des agonistes des TRL sur la production des FRO par la NADPH oxydase des polynucléaires neutrophiles humains

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BindingDB Entry 50043232: Pin1 inhibitors: Pitfalls, progress and cellular pharmacology.

BindingDB (2014) · UC San Diego · doi:10.7270/q2dv1m9t

BindingDB Entry 50039280: Synthesis and antiproliferative evaluation of certain indeno[1,2-c]quinoline derivatives. Part 2.

BindingDB (2013) · UC San Diego · doi:10.7270/q2bz6710

Covalent Protein Modification as a Mechanism for Dynamic Recruitment of Specific Interactors

Bertos, N., Sangwan, V., Yang, X., & Park, M. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_11

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 688

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

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

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