Cited by 1,886Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingProtease and Inhibitor Mechanisms

The DOI matches its Crossref record; 77 of the 77 references it cites were found in a registry or an index.

Protein Tyrosine Phosphatases in the Human Genome

Open access

Alonso, Andres, Sasin, Joanna, Bottini, Nunzio, Friedberg, Ilan, Friedberg, Iddo, Osterman, Andrei, Godzik, Adam, Hunter, Tony, Dixon, Jack, Mustelin, Tomas·2004·Cell

DOI 10.1016/j.cell.2004.05.018

Open this paper in CoChat — free account Open PDF

Abstract

Tyrosine phosphorylation is catalyzed by protein tyrosine kinases, which are represented by 90 genes in the human genome. Here, we present the set of 107 genes in the human genome that encode members of the four protein tyrosine phosphatase (PTP) families. The four families of PTPases, their substrates, structure, function, regulation, and the role of these enzymes in human disease will be discussed.

Integrity signals

Registry

Crossref · 10.1016/j.cell.2004.05.018

Cites

77 of 77 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Self-citation
Increased Insulin Sensitivity and Obesity Resistance in Mice Lacking the Protein Tyrosine Phosphatase-1B Gene
Elchebly, M., Payette, P., Michaliszyn, E., Cromlish, W., Collins, S., Loy, A. L., Normandin, D., Cheng, A., Himms-Hagen, J., Chan, C.-C., et al. (1999) · Science · doi:10.1126/science.283.5407.1544 · Cited by 2,210
Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome
Liaw, D., Marsh, D. J., Li, J., Dahia, P. L. M., Wang, S. I., Zheng, Z., Bose, S., Call, K. M., Tsou, H. C., Peacoke, M., et al. (1997) · Nature Genetics · doi:10.1038/ng0597-64 · Cited by 2,067
Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome
Tartaglia, M., Mehler, E. L., Goldberg, R. B., Zampino, G., Brunner, H. G., Kremer, H., van der Burgt, I., Crosby, A. H., Ion, A., Jeffery, S., et al. (2001) · Nature Genetics · doi:10.1038/ng772 · Cited by 1,736
A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes
Bottini, N., Musumeci, L., Alonso, A., Rahmouni, S., Nika, K., Rostamkhani, M., MacMurray, J. P., Meloni, T., Lucarelli, P., Pellecchia, M., et al. (2004) · Nature Genetics · doi:10.1038/ng1323 · Cited by 1,419
Self-citation
A thousand and one protein kinases
Hunter, T. R. (1987) · Cell · doi:10.1016/0092-8674(87)90509-5 · Cited by 1,057
Self-citation
Crystal Structure of the Tyrosine Phosphatase SHP-2
Hof, P., Pluskey, S., Dhe‐Paganon, S., Eck, M. J., & Shoelson, S. E. (1998) · Cell · doi:10.1016/s0092-8674(00)80938-1 · Cited by 997
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951
Protein Tyrosine Phosphatases: A Diverse Family of Intracellular and Transmembrane Enzymes
Fischer, E. H., Charbonneau, H., & Tonks, N. K. (1991) · Science · doi:10.1126/science.1650499 · Cited by 950
CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B
Barford, D., Flint, A. J., & Tonks, N. K. (1994) · Science · doi:10.1126/science.8128219 · Cited by 761

Flagged first, then by citations

Show all 75 references

Research works printed but not linked: 3

Alonso, 2004, VHY, a novel, myristylated, testis-restricted, dual-specific protein phosphatase related to VHX, J. Biol. Chem., in press
Bottini, 2002, LMPTP and human disease, Arch. Immol. Ther. Exp., 50, 95
Bult, 1997, Step, Eur. J. Cell Biol., 72, 337

Sorted by citations

Items 501–600 of 1,000

In Vitro Characterization of theBacillus subtilisProtein Tyrosine Phosphatase YwqE
Mijakovic̀, I., Musumeci, L., Tautz, L., Petranović, D., Edwards, R. A., Jensen, P. R., Mustelin, T., Deutscher, J., & Bottini, N. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.10.3384-3390.2005 · Cited by 49
Self-citation
Glycogen Phosphomonoester Distribution in Mouse Models of the Progressive Myoclonic Epilepsy, Lafora Disease
DePaoli-Roach, A. A., Contreras, C., Segvich, D. M., Heiß, C., Ishihara, M., Azadi, P., & Roach, P. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.607796 · Cited by 48
Shp2 protein tyrosine phosphatase inhibitor activity of estramustine phosphate and its triterpenoid analogs
Scott, L. M., Chen, L., Daniel, K. G., Brooks, W. H., Guida, W. C., Lawrence, H. R., Sebti, S. M., Lawrence, N. J., & Wu, J. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.11.117 · Cited by 48
Cell cycle-dependent Cdc25C phosphatase determines cell survival by regulating apoptosis signal-regulating kinase 1
Cho, Y.-C., Park, J. E., Park, B. C., Kim, J.-H., Jeong, D. G., Park, S., & Cho, S. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.2 · Cited by 48
Strategies for developing protein tyrosine phosphatase inhibitors
Tautz, L., & Mustelin, T. (2007) · Methods · doi:10.1016/j.ymeth.2007.02.014 · Cited by 48
Self-citation
Current Chemical Biology Tools for Studying Protein Phosphorylation and Dephosphorylation
Lu, C. H. S., Liu, K., Tan, L. P., & Yao, S. Q. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201103206 · Cited by 48
Estrogen-Mediated Suppression of the Gene Encoding Protein Tyrosine Phosphatase PTPRO in Human Breast Cancer: Mechanism and Role in Tamoxifen Sensitivity
Ramaswamy, B., Majumder, S., Roy, S., Ghoshal, K., Kutay, H., Datta, J., Younes, M., Shapiro, C. L., Motiwala, T., & Jacob, S. T. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0211 · Cited by 48
Low molecular weight protein tyrosine phosphatase: Multifaceted functions of an evolutionarily conserved enzyme
Caselli, A., Paoli, P., Santi, A., Mugnaioni, C., Toti, A., Camici, G., & Cirri, P. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.07.001 · Cited by 48
Suppression of PTPN6 exacerbates aluminum oxide nanoparticle-induced COPD-like lesions in mice through activation of STAT pathway
Li, X., Yang, H., Wu, S., Meng, Q., Sun, H., Lu, R., Cui, J., Zheng, Y., Chen, W., Zhang, R., et al. (2017) · Particle and Fibre Toxicology · doi:10.1186/s12989-017-0234-0 · Cited by 48
The roles of protein tyrosine phosphatases in bone-resorbing osteoclasts
Shalev, M., & Elson, A. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.07.005 · Cited by 47
Significance of protein tyrosine kinase/protein tyrosine phosphatase balance in the regulation of NF-κB signaling in the inflammatory process and aging
Jung, K. J., Lee, E. K., Yu, B. P., & Chung, H. Y. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.009 · Cited by 48
Dual-Selective Catalysis in Dephosphorylation Tuned by Hf6‑Containing Metal–Organic Frameworks Mimicking Phosphatase
Dong, J., An, H., Yue, Z.-K., Hou, S., Chen, Y., Zhang, Z., Cheng, P., Peng, Q., & Zhao, B. (2021) · ACS Central Science · doi:10.1021/acscentsci.0c01581 · Cited by 47
Status of research on natural protein tyrosine phosphatase 1B inhibitors as potential antidiabetic agents: Update
Liu, Z., Gao, H., Zhao, Z., Huang, M., Wang, S., & Zhan, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113990 · Cited by 49
Methods to monitor classical protein‐tyrosine phosphatase oxidation
Karisch, R., & Neel, B. G. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08626.x · Cited by 46
Global Analysis of Serine/Threonine and Tyrosine Protein Phosphatase Catalytic Subunit Genes inNeurospora crassaReveals Interplay Between Phosphatases and the p38 Mitogen-Activated Protein Kinase
Ghosh, A., Servin, J. A., Park, G., & Borkovich, K. A. (2013) · G3 Genes Genomes Genetics · doi:10.1534/g3.113.008813 · Cited by 48
Optimization of a Cyclic Peptide Inhibitor of Ser/Thr Phosphatase PPM1D (Wip1)
Hayashi, R., Tanoue, K., Durell, S. R., Chatterjee, D. K., Jenkins, L. M. M., Appella, D. H., & Appella, E. (2011) · Biochemistry · doi:10.1021/bi101949t · Cited by 47
Redox regulation of protein tyrosine phosphatase activity by hydroxyl radical
Meng, F.-G., & Zhang, Z. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.06.018 · Cited by 48
Inputs and outputs of insulin receptor
Du, Y., & Wei, T. (2014) · Protein & Cell · doi:10.1007/s13238-014-0030-7 · Cited by 48
Multisite Phosphorylation of S6K1 Directs a Kinase Phospho-code that Determines Substrate Selection
Arif, A., Jia, J., Willard, B. B., Li, X., & Fox, P. L. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.11.017 · Cited by 50
A malachite green-based assay to assess glucan phosphatase activity
Sherwood, A., Paasch, B. C., Worby, C. A., & Gentry, M. S. (2012) · Analytical Biochemistry · doi:10.1016/j.ab.2012.10.044 · Cited by 50
Modulation of gold(III) porphyrin 1a-induced apoptosis by mitogen-activated protein kinase signaling pathways
Wang, Y., He, Q., Che, C., Tsao, S. W., Sun, R. W., & Chiu, J. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.11.024 · Cited by 47
Mutational analysis of gene families in human cancer
Bardelli, A., & Velculescu, V. E. (2004) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.12.009 · Cited by 48
C1858T Functional Variant of PTPN22 Gene Is Not Associated With Celiac Disease Genetic Predisposition
Rueda‐Medina, B., Núñez, C., Orozco, G., López‐Nevot, M. Á., de la Concha, E. G., Martin, J. J., & Urcelay, E. (2005) · Human Immunology · doi:10.1016/j.humimm.2005.04.008 · Cited by 47
MAPK-specific tyrosine phosphatases: new targets for drug discovery?
Barr, A., & Knapp, S. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.08.005 · Cited by 46
Novel excitation-contraction coupling related genes reveal aspects of muscle weakness beyond atrophy—new hopes for treatment of musculoskeletal diseases
Manring, H. R., de Abreu, E. L., Brotto, L. S., Weisleder, N. L., & Brotto, M. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00037 · Cited by 45
Protein tyrosine phosphatase receptor-like genes are frequently hypermethylated in sporadic colorectal cancer
Łaczmańska, I., Karpiński, P., Bębenek, M., Sedziak, T., Ramsey, D., Szmida, E., & Sasiadek, M. M. (2012) · Journal of Human Genetics · doi:10.1038/jhg.2012.119 · Cited by 46
Large-Scale Structural Biology of the Human Proteome
Edwards, A. M. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.070907.103305 · Cited by 46
Thioredoxin reductase 1 and NADPH directly protect protein tyrosine phosphatase 1B from inactivation during H2O2 exposure
Dagnell, M., Pace, P., Cheng, Q., Frijhoff, J., Östman, A., Arnér, E. S. J., Hampton, M. B., & Winterbourn, C. C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.793745 · Cited by 47
Proteomic Identification of Protein Tyrosine Phosphatase and Substrate Interactions in Living Mammalian Cells by Genetic Encoding of Irreversible Enzyme Inhibitors
Tang, H., Dai, Z., Qin, X., Cai, W., Hu, L., Huang, Y., Cao, W., Yang, F., Wang, C., & Liu, T. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b06922 · Cited by 46
Recent advances in the discovery of protein tyrosine phosphatase SHP2 inhibitors
Kong, J., & Long, Y. (2022) · RSC Medicinal Chemistry · doi:10.1039/d1md00386k · Cited by 45
Identification of novel PTP1B inhibitors by pharmacophore based virtual screening, scaffold hopping and docking
Balaramnavar, V. M., Srivastava, R., Rahuja, N., Gupta, S., Rawat, A., Varshney, S., Chandasana, H., Chhonker, Y. S., Doharey, P. K., Kumar, S., et al. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.09.097 · Cited by 45
Protein tyrosine phosphatases encoded in Cotesia plutellae bracovirus: Sequence analysis, expression profile, and a possible biological role in host immunosuppression
Ibrahim, A. M. A., Choi, J. Y., Je, Y. H., & Kim, Y. (2006) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2006.11.005 · Cited by 45
Thiol redox biochemistry: insights from computer simulations
Zeida, A., Guardia, C. M. A., Lichtig, P., Perissinotti, L. L., Defelipe, L. A., Turjanski, A. G., Radí, R., Trujillo, M., & Estrin, D. A. (2014) · Biophysical Reviews · doi:10.1007/s12551-013-0127-x · Cited by 45
Expression, localization, and biological function of the R3 subtype of receptor-type protein tyrosine phosphatases in mammals
Matozaki, T., Murata, Y., Mori, M., Kotani, T., Okazawa, H., & Ohnishi, H. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.07.001 · Cited by 45
Rational Design of Selective Organoruthenium Inhibitors of Protein Tyrosine Phosphatase 1B
Ong, J. X., Yap, C. W., & Ang, W. H. (2012) · Inorganic Chemistry · doi:10.1021/ic301884j · Cited by 45
An epigenetic modifier induces production of (10′S)-verruculide B, an inhibitor of protein tyrosine phosphatases by Phoma sp. nov. LG0217, a fungal endophyte of Parkinsonia microphylla
Gubiani, J. R., Wijeratne, E. M. K., Shi, T., Araújo, Â. R., Arnold, A. E., Chapman, E., & Gunatilaka, A. A. L. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.01.048 · Cited by 45
The Roles of Protein Tyrosine Phosphatases in Hepatocellular Carcinoma
Huang, Y., Zhang, Y., Ge, L., Lin, Y., & Kwok, H. F. (2018) · Cancers · doi:10.3390/cancers10030082 · Cited by 47
Crystal Structure of the Catalytic Domain of Human MAP Kinase Phosphatase 5: Structural Insight into Constitutively Active Phosphatase
Jeong, D. G., Yoon, T., Kim, J., Shim, M. Y., Jung, S., Son, J. H., Ryu, S. E., & Kim, S. J. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.059 · Cited by 45
Quantitative proteomic approaches for studying phosphotyrosine signaling
Ding, S., Qian, W., & Smith, R. D. (2007) · Expert Review of Proteomics · doi:10.1586/14789450.4.1.13 · Cited by 45
Regulation of TRP channel TRPM2 by the tyrosine phosphatase PTPL1
Zhang, W., Tong, Q., Conrad, K., Wozney, J. L., Cheung, J. Y., & Miller, B. A. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00569.2006 · Cited by 45
Modulation of TCR Signaling by Tyrosine Phosphatases: From Autoimmunity to Immunotherapy
Castro-Sanchez, P., Teagle, A. R., Prade, S., & Zamoyska, R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.608747 · Cited by 44
The mitochondrial reactive oxygen species regulator p66Shc controls PDGF-induced signaling and migration through protein tyrosine phosphatase oxidation
Frijhoff, J., Dagnell, M., Augsten, M., Beltrami, E., Giorgio, M., & Östman, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.022 · Cited by 43
Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells
Omerović, J., Clague, M. J., & Prior, I. A. (2009) · Biochemical Journal · doi:10.1042/bj20091413 · Cited by 44
Dynamic changes in the expression of DEP‐1 and other PDGF receptor‐antagonizing PTPs during onset and termination of neointima formation
Kappert, K., Paulsson, J., Sparwel, J., Leppänen, O., Hellberg, C. B., Östman, A., & Micke, P. (2006) · The FASEB Journal · doi:10.1096/fj.06-6219com · Cited by 44
Redox-mediated substrate recognition by Sdp1 defines a new group of tyrosine phosphatases
Fox, G. C., Shafiq, M., Briggs, D. C., Knowles, P. P., Collister, M., Didmon, M. P., Makrantoni, V., Dickinson, R. J., Hanrahan, S. J., Totty, N. F., et al. (2007) · Nature · doi:10.1038/nature05804 · Cited by 45
Functional Genomics meets neurodegenerative disorders
Hoerndli, F. J., David, D. C., & Götz, J. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.07.002 · Cited by 44
Extensive protein pyrophosphorylation revealed in human cell lines
Morgan, J. A. M., Singh, A., Kurz, L., Nadler-Holly, M., Ruwolt, M., Ganguli, S., Sharma, S., Penkert, M., Krause, E., Liu, F., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01613-5 · Cited by 49
Protein Tyrosine Phosphatase Assays
Lorenz, U. M. (2011) · Current Protocols in Immunology · doi:10.1002/0471142735.im1107s93 · Cited by 43
Attempted Replication of 50 Reported Asthma Risk Genes Identifies a SNP in RAD50 as Associated with Childhood Atopic Asthma
Murk, W. K., Walsh, K. M., Hsu, L., Zhao, L., Bracken, M. B., & DeWan, A. T. (2011) · Human Heredity · doi:10.1159/000319536 · Cited by 43
Protein Topology Determines Cysteine Oxidation Fate: The Case of Sulfenyl Amide Formation among Protein Families
Defelipe, L. A., Lanzarotti, E., Gauto, D. F., Marti, M. A., & Turjanski, A. G. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004051 · Cited by 46
VHR / DUSP 3 phosphatase: structure, function and regulation
Pavic, K., Duan, G., & Köhn, M. (2015) · FEBS Journal · doi:10.1111/febs.13263 · Cited by 46
Understanding the biology of reactive oxygen species and their link to cancer: NADPH oxidases as novel pharmacological targets
Harrison, I. P., & Selemidis, S. (2014) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.12238 · Cited by 44
Downregulation of p53 by phosphatase of regenerating liver 3 is mediated by MDM2 and PIRH2
Min, S., Kim, D., Heo, Y.-S., Kim, H. M., Kim, I., & Yoo, O.-J. (2009) · Life Sciences · doi:10.1016/j.lfs.2009.11.010 · Cited by 42
DUSP3 Genetic Deletion Confers M2-like Macrophage–Dependent Tolerance to Septic Shock
Singh, P., Dejager, L., Amand, M., Théâtre, E., Vandereyken, M., Zurashvili, T., Singh, M., Mack, M., Timmermans, S., Musumeci, L., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402431 · Cited by 43
Self-citation
Lack of Mitogen-Activated Protein Kinase Phosphatase-1 Protects ApoE-Null Mice Against Atherosclerosis
Shen, J., Chandrasekharan, U. M., Ashraf, M. Z., Long, E., Morton, R. E., Liu, Y., Smith, J. D., & DiCorleto, P. E. (2010) · Circulation Research · doi:10.1161/circresaha.109.198069 · Cited by 43
Cell Regulation by Phosphotyrosine-Targeted Ubiquitin Ligases
Cooper, J. A., Kaneko, T., & Li, S. S. ‐. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00098-15 · Cited by 45
Discovery of 4-[(5-arylidene-4-oxothiazolidin-3-yl)methyl]benzoic acid derivatives active as novel potent allosteric inhibitors of protein tyrosine phosphatase 1B: In silico studies and in vitro evaluation as insulinomimetic and anti-inflammatory agents
Ottanà, R., Paoli, P., Naß, A., Lori, G., Cardile, V., Adornato, I., Rotondo, A., Graziano, A. C. E., Wolber, G., & Maccari, R. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.10.063 · Cited by 43
The function and mechanism of preactivated thiomers in triggering epithelial tight junctions opening
Zhang, Y., Zhou, S., Deng, F., Chen, X., Wang, X., Wang, Y., Zhang, H., Dai, W., He, B., Zhang, Q., et al. (2018) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2018.10.014 · Cited by 43
Regulation of peripheral and central immunity: Understanding the role of Src homology 2 domain-containing tyrosine phosphatases, SHP-1 & SHP-2
Garg, M., Wahid, M., & Khan, F. (2019) · Immunobiology · doi:10.1016/j.imbio.2019.09.006 · Cited by 43
FGF Signalling in Vertebrate Development
Pownall, M. E., & Isaacs, H. V. (2010) · Colloquium Series on Developmental Biology · doi:10.4199/c00011ed1v01y201004deb002 · Cited by 45
14-3-3 Protein Signaling in Development and Growth Factor Responses
Thomas, D., Guthridge, M. A., Woodcock, J. M., & Lopez, A. F. (2005) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(05)67009-3 · Cited by 43
Defining SH2 domain and PTP specificity by screening combinatorial peptide libraries
Wavreille, A., Garaud, M., Zhang, Y., & Pei, D. (2007) · Methods · doi:10.1016/j.ymeth.2007.02.010 · Cited by 47
Crystal Structure of the PTPL1/FAP-1 Human Tyrosine Phosphatase Mutated in Colorectal Cancer
Villa, F., Deák, M., Bloomberg, G. B., Alessi, D. R., & van Aalten, D. M. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412211200 · Cited by 43
PTPσ binds and dephosphorylates neurotrophin receptors and can suppress NGF-dependent neurite outgrowth from sensory neurons
Faux, C. H., Hawadle, M., Nixon, J., Wallace, A. S., Lee, S. M., Murray, S. S., & Stoker, A. W. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.06.008 · Cited by 43
Inhibition of receptor tyrosine kinase signalling by small molecule agonist of T-cell protein tyrosine phosphatase
Mattila, E., Marttila, H., Sahlberg, N., Kohonen, P. J., Tähtinen, S., Halonen, P., Perälä, M., & Ivaska, J. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-7 · Cited by 45
Low Molecular Weight Phosphotyrosine Protein Phosphatases as Emerging Targets for the Design of Novel Therapeutic Agents
Maccari, R., & Ottanà, R. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200607g · Cited by 43
Vascular signaling through cholesterol-rich domains: implications in hypertension
Callera, G. E., Montezano, A. C. I., Yogi, Á., Tostes, R. C., & Touyz, R. M. (2007) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e328040bfbd · Cited by 44
PTPN2 in the Immunity and Tumor Immunotherapy: A Concise Review
Song, J., Lan, J., Tang, J., & Luo, N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710025 · Cited by 42
Supramolecular Photonic Hydrogel for High‐Sensitivity Alkaline Phosphatase Detection via Synergistic Driving Force
Lu, D., Qin, M., Zhao, Y., Li, H., Luo, L., Ding, C., Cheng, P., Su, M., Li, H., Song, Y., et al. (2023) · Small · doi:10.1002/smll.202206461 · Cited by 42
Tyrosine phosphatases as a superfamily of tumor suppressors in colorectal cancer.
Łaczmańska, I., & Sasiadek, M. M. (2011) · Acta Biochimica Polonica · doi:10.18388/abp.2011_2212 · Cited by 42
Inhibition of Lymphoid Tyrosine Phosphatase by Benzofuran Salicylic Acids
Vang, T., Xie, Y., Liu, W. H., Vidović, D., Liu, Y., Wu, S., Smith, D. H., Rinderspacher, A., Chung, C., Gong, G., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm101004d · Cited by 42
Self-citation
Integrating phosphoproteomics in systems biology
Liu, Y., & Chance, M. R. (2014) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2014.07.003 · Cited by 41
Diverse Levels of Sequence Selectivity and Catalytic Efficiency of Protein-Tyrosine Phosphatases
Selner, N. G., Luechapanichkul, R., Chen, X., Neel, B. G., Zhang, Z., Knapp, S., Bell, C. E., & Pei, D. (2013) · Biochemistry · doi:10.1021/bi401223r · Cited by 42
Protein Tyrosine Phosphatase Inhibition by Metals and Metal Complexes
Lu, L., & Zhu, M. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5720 · Cited by 42
Hyaluronan Synthases Posttranslational Regulation in Cancer
Vigetti, D., & Passi, A. G. (2014) · Advances in cancer research · doi:10.1016/b978-0-12-800092-2.00004-6 · Cited by 42
Lafora Disease: A Ubiquitination-Related Pathology
García-Gimeno, M. A., Knecht, E., & Sanz, P. (2018) · Cells · doi:10.3390/cells7080087 · Cited by 41
Inhibitors of Protein Tyrosine Phosphatase PTP1B With Anticancer Potential
Kostrzewa, T., Styszko, J., Górska‐Ponikowska, M., Śledziński, T., & Kuban‐Jankowska, A. (2019) · Anticancer Research · doi:10.21873/anticanres.13481 · Cited by 42
Expression of ERK signaling inhibitors Dusp6, Dusp7, and Dusp9 during mouse ear development
Urness, L. D., Li, Z., Wang, X., & Mansour, S. L. (2007) · Developmental Dynamics · doi:10.1002/dvdy.21380 · Cited by 44
DNA methylation of membrane-bound tyrosine phosphatase genes in acute lymphoblastic leukaemia
Stevenson, W. S., Best, G., Przybylla, A., Chen, Q., Singh, N., Koleth, M., Pierce, S. A., Kennedy, T., Tong, W.-G., Kuang, S.-Q., et al. (2013) · Leukemia · doi:10.1038/leu.2013.270 · Cited by 42
Lipidyl Pseudopteranes A−F: Isolation, Biomimetic Synthesis, and PTP1B Inhibitory Activity of a New Class of Pseudopteranoids from the Gorgonian Pseudopterogorgia acerosa
Kate, A. S., Aubry, I., Tremblay, M. L., & Kerr, R. G. (2008) · Journal of Natural Products · doi:10.1021/np800544b · Cited by 42
Src-homology 2 domain-containing tyrosine phosphatase 2 promotes oral cancer invasion and metastasis
Wang, H., Chiang, W., Huang, H.-H., Shen, Y., & Chiang, H. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-442 · Cited by 42
Modulation of α-catenin Tyr phosphorylation by SHP2 positively effects cell transformation induced by the constitutively active FGFR3
Burks, J., & Agazie, Y. M. (2006) · Oncogene · doi:10.1038/sj.onc.1209728 · Cited by 46
Emerging Pharmacotherapeutic Strategies to Overcome Undruggable Proteins in Cancer
Lu, Y., Yang, Y., Zhu, G., Zeng, H., Fan, Y., Guo, F., Xu, D., Wang, B., Chen, D., & Ge, G. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.83026 · Cited by 42
Palmitoylated transmembrane adaptor proteins in leukocyte signaling
Štěpánek, O., Dráber, P., & Hořejšı́, V. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.01.007 · Cited by 41
Identification and characterization of DUSP27, a novel dual‐specific protein phosphatase
Friedberg, I., Nika, K., Tautz, L., Saito, K., Cerignoli, F., Friedberg, I., Godzik, A., & Mustelin, T. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.059 · Cited by 41
Self-citation
Anharmonic simulations of the vibrational spectrum of sulfated compounds: application to the glycosaminoglycan fragment glucosamine 6-sulfate
Barnes, L., Schindler, B., Allouche, A.-R., Simon, D., Chambert, S., Oomens, J., & Compagnon, I. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp02079d · Cited by 41
Next generation of network medicine: interdisciplinary signaling approaches
Korcsmáros, T., Schneider, M. V., & Superti‐Furga, G. (2017) · Integrative Biology · doi:10.1039/c6ib00215c · Cited by 42
Recent advances in the development of allosteric protein tyrosine phosphatase inhibitors for drug discovery
Elhassan, R. M., Hou, X., & Fang, H. (2021) · Medicinal Research Reviews · doi:10.1002/med.21871 · Cited by 40
Identification of 3-(piperazinylmethyl)benzofuran derivatives as novel type II CDK2 inhibitors: design, synthesis, biological evaluation, and in silico insights
Eldehna, W. M., Maklad, R. M., Almahli, H., Al-Warhi, T. I., Elkaeed, E. B., Abourehab, M. A. S., Abdel‐Aziz, H. A., & Kerdawy, A. M. E. (2022) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2022.2062337 · Cited by 40
Preferential redox regulation of cysteine‐based protein tyrosine phosphatases: structural and biochemical diversity
Netto, L. E. S., & Machado, L. E. S. F. (2022) · FEBS Journal · doi:10.1111/febs.16466 · Cited by 39
Anoikis effector Bit1 negatively regulates Erk activity
Kairouz-Wahbe, R., Biliran, H., Luo, X., Khor, I., Wankell, M., Besch-Williford, C. L., Pascual, J., Oshima, R. G., & Ruoslahti, E. I. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711357105 · Cited by 41
Inhibition of MAPK by Prolactin Signaling through the Short Form of Its Receptor in the Ovary and Decidua
Devi, Y. S., Seibold, A. M., Shehu, A., Maizels, E. T., Halperín, J., Le, J., Binart, N., Bao, L., & Gibori, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166603 · Cited by 43
Dimerization of Protein Tyrosine Phosphatase σ Governs both Ligand Binding and Isoform Specificity
Lee, S. M., Faux, C. H., Nixon, J., Alete, D. E., Chilton, J. K., Hawadle, M., & Stoker, A. W. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00535-06 · Cited by 41
Suppression of protein tyrosine phosphatase N23 predisposes to breast tumorigenesis via activation of FYN kinasePreprint
Zhang, S., Fan, G., Yuan, H., Hammell, M., Wilkinson, J. E., & Tonks, N. K. (2017) · Genes & Development · doi:10.1101/gad.304261.117 · Cited by 42
Structure of the Hematopoietic Tyrosine Phosphatase (HePTP) Catalytic Domain: Structure of a KIM Phosphatase with Phosphate Bound at the Active Site
Mustelin, T., Tautz, L., & Page, R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.09.049 · Cited by 40
Self-citation
Phosphatase of regenerating liver‐3 promotes migration and invasion by upregulating matrix metalloproteinases‐7 in human colorectal cancer cells
Lee, S., Han, Y., Yun, J., Lee, C. W., Shin, D., Ha, Y., Kim, J., Koh, J. S., Hong, S., Han, D. C., et al. (2011) · International Journal of Cancer · doi:10.1002/ijc.27381 · Cited by 40
Novel PTP1B inhibitors identified by DNA display of fragment pairs
Barluenga, S., Zambaldo, C., Ioannidou, H. A., Ciobanu, M., Morieux, P., Daguer, J., & Winssinger, N. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.11.102 · Cited by 40
PTPRJ Inhibits Leptin Signaling, and Induction of PTPRJ in the Hypothalamus Is a Cause of the Development of Leptin Resistance
Shintani, T., Higashi, S., Suzuki, R., Takeuchi, Y., Ikaga, R., Yamazaki, T., Kobayashi, K., & Noda, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-12070-7 · Cited by 40
HoxA10 Facilitates SHP-1-Catalyzed Dephosphorylation of p38 MAPK/STAT3 To Repress Hepatitis B Virus Replication by a Feedback Regulatory Mechanism
Yang, Q., Qi, Z., Zhang, X., You, L., Wang, W., Liu, W., Han, Y., Ma, C., Xu, W. Q., Chen, J., et al. (2019) · Journal of Virology · doi:10.1128/jvi.01607-18 · Cited by 40
Important roles of protein tyrosine phosphatase PTPN12 in tumor progression
Lee, C., & Rhee, I. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.04.011 · Cited by 40

Authors: Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
Salk Institute for Biological Studies (US)
University of California San Diego (US)
Corresponding author: Mustelin, Tomas
ORCID: Bottini, Nunzio
Friedberg, Iddo
Osterman, Andrei
Godzik, Adam
Hunter, Tony
Dixon, Jack
Mustelin, Tomas
Venue: Cell
Publisher: Elsevier BV
Published: 2004-06
Volume: 117
Issue: 6
Pages: 699-711
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2004.05.018
OpenAlex: W2043617798
Cited by: 1,886
References: 75
Citations by year: 2026: 34 · 2025: 30 · 2024: 63 · 2023: 62 · 2022: 56 · 2021: 78 · 2020: 67 · 2019: 77 · 2018: 69 · 2017: 95 · 2016: 67 · 2015: 97 · 2014: 110 · 2013: 133 · 2012: 118
FWCI: 7.71
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3333 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords: protein tyrosine phosphatase, human genome, tyrosine phosphorylation, tyrosine kinase, enzyme structure-function, enzyme regulation, human disease
MeSH terms: Amino Acid Sequence, Humans, Phosphorylation, Phylogeny, Tyrosine, Signal Transduction, Genome, Human, Gene Expression Regulation, Enzymologic, Protein Tyrosine Phosphatases, Protein Structure, Tertiary

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Protein Tyrosine Phosphatases in the Human Genome

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks