Specific Inhibition of Stat3 Signal Transduction by PIAS3

Positional cloning of the mouse obese gene and its human homologue

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Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins

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Stat3: a STAT Family Member Activated by Tyrosine Phosphorylation in Response to Epidermal Growth Factor and Interleukin-6

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Maximal activation of transcription by statl and stat3 requires both tyrosine and serine phosphorylation

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TRANSCRIPTIONAL RESPONSES TO POLYPEPTIDE LIGANDS: The JAK-STAT Pathway

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Targeted disruption of the mouse Stat3 gene leads to early embryonic lethality

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Cytokine receptor signalling

Ihle, J. N. (1995) · Nature · doi:10.1038/377591a0 · Cited by 1,201

Leptin activation of Stat3 in the hypothalamus of wild-type and ob/ob mice but not db/db mice.

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Structure and function of a new STAT-induced STAT inhibitor

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Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway

Akira, S., Nishio, Y., Inoue, M., Wang, X.-J., We, S., Matsusaka, T., Yoshida, K., Sudo, T., Naruto, M., & Kishimoto, T. (1994) · Cell · doi:10.1016/0092-8674(94)90235-6 · Cited by 1,019

Genomic organization of the gene for mouse PIASγ and analysis of its promoter

Sturm, S., Koch, M., & White, F. A. (2001) · Gene · doi:10.1016/s0378-1119(01)00363-8 · Cited by 4

Erythropoietin receptor signaling processes

Ghaffari, S., Huang, L. J.-S., Zhang, J., & Lodish, H. F. (2006) · Birkhäuser-Verlag eBooks · doi:10.1007/3-7643-7543-4_5 · Cited by 4

Specific presence of intracellular citrullinated proteins in rheumatoid arthritis synovium: relevance to antifilaggrin autoantibodies

Ho (2001) · Pure Amsterdam UMC · doi:10.1002/1529-0131(200110)44:10 · Cited by 3

Insights from Interleukin-6 trans-signaling and implications for the control of cytokine activity

Rose‐John, S. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2026.120109 · Cited by 3

Recent Progress in the Study of Leptin and Its Scientific Significance

高, 文. (2014) · Bioprocess · doi:10.12677/bp.2014.41001 · Cited by 3

Identification of protein inhibitor of activated STAT 4, a novel host interacting partner that involved in bovine viral diarrhea virus growth

Gong, X., Chen, Q., & Zheng, F. (2020) · Virology Journal · doi:10.1186/s12985-020-01330-0 · Cited by 3

A protein inhibitor of activated STAT (CgPIAS) negatively regulates the expression of ISGs by inhibiting STAT activation in oyster Crassostrea gigas

Wang, S., Li, Y., Qiao, X., Jin, Y., Liu, R., Wang, L., & Song, L. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.11.020 · Cited by 3

The expression of protein inhibitor of activated signal transducers and activators of transcription 3 in the evolutionary process of gastric cancer

Liu, L., Yan, M.-G., Yang, D.-H., Sun, W., & Zhang, J. (2011) · European Journal of Internal Medicine · doi:10.1016/j.ejim.2011.04.002 · Cited by 3

Truncated adenomatous polyposis coli (APC) tumour suppressor protein can undergo tyrosine phosphorylation

Norris, A. L., Clissold, P. M., Askham, J. M., Morrison, E. E., Moncur, P. H., McCall, S. H., Coletta, P. L., Meredith, D. M., & Markham, A. F. (2000) · European Journal of Cancer · doi:10.1016/s0959-8049(99)00305-6 · Cited by 3

Differential resistance of melanoma cells to treatment with recombinant IFN-alpha2b and leukocyte IFN.

Ruuth, K., Berglund, A., Munoz-Ritchie, V. G., & Lundgren, E. (2007) · PubMed · Cited by 3

Mechanisms and Biological Consequences of STAT Signaling by Cytokines that Share the Common Cytokine Receptor γ Chain, γc

Lin, J., & Leonard, W. J. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_29 · Cited by 3

Transient Maternal IL-6 boosts glutamatergic synapses and disrupts hippocampal connectivity in the offspringPreprint

Mirabella, F., Desiato, G., Mancinelli, S., Fossati, G., Rasile, M., Morini, R., Markicevic, M., Grimm, C., Amegandjin, C. A., Termanini, A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.02.364356 · Cited by 3

STAT Proteins as Molecular Targets for Cancer Therapy

Buettner, R., Kortylewski, M., Pardoll, D. M., Yu, H., & Jove, R. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_41 · Cited by 3

The JAK/STAT conundrum with mutational heterogeneity, immune defects, and the emergence of targeted therapies

Demirkaya, D. B., Colak, B. C., Sefer, A. P., & Barış, S. (2025) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2025.2543475 · Cited by 3

Stat3 Oncogenic Signaling in Glioblastoma Multiforme

Haque, S. J., & Sharma, P. (2009) · Humana Press eBooks · doi:10.1007/978-1-60327-553-8_37 · Cited by 2

Attenuation of Multifocal Cell Survival Signaling by Bioactive Phytochemicals in the Prevention and Therapy of Cancer

Banerjee, S., Azmi, A. S., Bao, B., & Sarkar, F. H. (2013) · Evidence-based anticancer complementary and alternative medicine · doi:10.1007/978-94-007-6443-9_10 · Cited by 2

Historical Development of STAT3 Inhibitors and Early Results in Clinical Trials

Yu, C., Jove, R., & Turkson, J. (2016) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-42949-6_4 · Cited by 2

The RKIP and STAT3 Axis in Cancer Chemotherapy: Opposites Attract

Chatterjee, D., Sabo, E., Resnick, M. B., Yeung, K. C., & Chin, Y. E. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-474-2_10 · Cited by 2

gp130-mediated signalling as a therapeutic target

Ohtani, T., Ishihara, K., Atsumi, T., Yoshida, Y., Nishida, K., Narimatsu, M., Shirogane, T., Hibi, M., & Hirano, T. (2000) · Emerging Therapeutic Targets · doi:10.1517/14728222.4.4.459 · Cited by 2

Signaling through the Jak-Stat pathway: Regulation of tyrosine kinase activity

Saharinen, P. (2002) · Työväentutkimus Vuosikirja · Cited by 2

Evolutionary Conserved Regulatory Mechanisms of the Jak/Stat Pathway

Grönholm, J. (2012) · Tampere University Institutional Repository (Tampere University) · Cited by 2

REGULATION OF STAT5 ACTIVATION

Paukku, K. (2003) · Työväentutkimus Vuosikirja · Cited by 1

Negative-feedback Regulations Of Cytokine Signals

Kishimoto, T., Narazaki, M., & Naka, T. (2000) · CRC Press eBooks · doi:10.1201/9780203904244.ch9 · Cited by 2

A True Jak of All Trades

Sandberg, E. M., Wallace, T. A., Godeny, M. D., & Sayeski, P. P. (2004) · Cited by 2

Leptin Signaling in the Cardiovascular System

Karmazyn, M., Purdham, D. M., Rajapurohitam, V., & Zeidan, A. (2008) · Springer eBooks · doi:10.1007/978-0-387-09552-3_20 · Cited by 2

STAT3/Snail Signaling and Progression of Hypoxia Tolerance in Breast Cancer Cells

Andreeva, O. E., Sorokin, D. V., Scherbakov, A. M., Vinokurova, S., Kopnin, P., Elkina, N. V., Fedorova, M. D., Katargin, A. N., Елкин, Д. С., & Ma, K. (2025) · Biochemistry (Moscow) · doi:10.1134/s0006297925601315 · Cited by 1

STUDIES ON THE T CELL SUPPRESSIVE AND ANTI-ANGIOGENIC ACTIVITIES OF THE DIETARY PHYTOCHEMICAL PIPERINE

Doucette, C. D. (2013) · DalSpace (Dalhousie University) · Cited by 1

Transcription Factors STAT5 and STAT3

Čulig, Z., Pestell, R. G., & Nevalainen, M. T. (2008) · Humana Press eBooks · doi:10.1007/978-1-60327-079-3_12 · Cited by 1

Natural Compounds Are Smart Players in Context to Anticancer Potential of Receptor Tyrosine Kinases: An In Silico and In Vitro Advancement

Singh, P., Kumar, S., & Bast, F. (2017) · Translational medicine research · doi:10.1007/978-94-024-1045-7_8 · Cited by 1

Effects of flavonoids from Allium mongolicum Regel on cell apoptosis, cell cycle and STAT1 mRNA expression in peripheral blood lymphocytes of sheep

Qie, M., Wang, T., manda, & Ao, C. (2021) · Journal of Applied Animal Research · doi:10.1080/09712119.2021.2011294 · Cited by 1

MicroRNAs and Cancer Signaling Pathways

Manjari, K. S., Srilekha, A., Khan, I. A., & Prasad, D. (2022) · Springer eBooks · doi:10.1007/978-981-16-9186-7_2 · Cited by 1

Targeting Signal Transducer and Activator of Transcription (STAT) for Anticancer Therapy

Santos, F. P. D. S., Hazan‐Halevy, I., & Estrov, Z. E. (2011) · Springer eBooks · doi:10.1007/978-1-4614-0730-0_13 · Cited by 1

Cytokine signaling

Szente, B. E. (2003) · Elsevier eBooks · doi:10.1016/b978-012689663-3/50008-9 · Cited by 1

Recent Progress in the Study of Leptin and Its Scientific Significance

Gao, W., Zhang, H., Jiang, W., & Zhu, W. (2014) · Cited by 1

Efeitos da exposição crônica à poluição atmosférica urbana sobre a receptividade uterina: estudo morfo-funcional do remodelamento celular do endométrio e expressão de fatores envolvidos na preparação para implantação embrionária

de Castro, K. R. (2013) · doi:10.11606/d.5.2013.tde-05112013-155805 · Cited by 1

Androgen Receptor Interacting Proteins: Co-Activators And Co-Repressors

Heinlein, C., Sampson, E., & Chang, C. (2002) · Springer eBooks · doi:10.1007/978-1-4615-1161-8_4

Understanding acquired resistance to Lapatinib in breast cancer cells

Tseng, J. (2010) · Digital Commons-TMC (Texas Medical Center) · Cited by 1

STAT-Dependent Gene Expression without Tyrosine Phosphorylation

Chatterjee‐Kishore, M., Yang, J. B., & Stark, G. R. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_23 · Cited by 1

Transcriptional Regulation in the Peripheral Nervous System and the Role of STAT3 in Axon Regeneration

Smith, R. P. (2008) · Cited by 1

Mechanisms and Biological Roles of STAT Activation by the IL-6 Family of Cytokines

Kamimura, D., & Hirano, T. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_11 · Cited by 1

Cytokine-Mediated Inflammation and Other Actions in the Central Nervous System

Campbell, I. L. (2002) · Springer eBooks · doi:10.1007/978-3-662-05073-6_5 · Cited by 1

Constitutively Active STATs and Cellular Transformation

Dechow, T. N., & Bromberg, J. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_40 · Cited by 1

IL-6/gpl30/Stat3

Taub, R. A. (2005) · Springer eBooks · doi:10.1007/3-540-27194-5_7 · Cited by 1

Antiangiogenic Therapy for Melanoma

Parker, V. P. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-159-6_13 · Cited by 1

Identification of Novel STAT3 Target Genes Associated with Oncogenesis

Haviland, R. (2011) · Digital Commons - University of South Florida (University of South Florida) · Cited by 1

The Neuropeptide VIP and the IL-6 Family of Cytokines in Bone - Effects on Bone Resorption, Cytokine Expression and Receptor Signalling in Osteoblasts and Bone Marrow Stromal Cells

Persson, E. (2005) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1

The Role of Interleukin-6 in the Febrile Response

Hamzic, N. (2013) · DiVA (Linkoping University) · Cited by 1

Regulation of Cytokine Signaling During Macrophage Differentiation and Activation

Junttila, I. (2005) · Tampere University Institutional Repository (Tampere University) · Cited by 1

Post-translational Modifications in Regulation of Jak-stat Pathway

Ungureanu, D. (2005) · Tampere University Institutional Repository (Tampere University) · Cited by 1

SOCS Proteins and Cytokine Signalling: The many Faces of the SOCS Box

Piessevaux, J. (2008) · Ghent University Academic Bibliography (Ghent University) · Cited by 1

Candidate genes for obesity and related phenotypes

Swarbrick, M. M. (2002) · UWA Profiles and Research Repository (UWA) · Cited by 1

Cytokine-Activated JAK-STAT Signaling in the Mouse Immune System

Liu, B., & Shuai, K. (2007) · Elsevier eBooks · doi:10.1016/b978-012369454-6/50085-6 · Cited by 1

Inhibitors Of The Janus Kinase – Signal Transducers And Activators Of Transcription ( Jak/ Stat) Signaling Pathway

Starr, R. (2000) · CRC Press eBooks · doi:10.1201/9780203904244.ch10 · Cited by 1

THE ROLE OF LIGAND IN THE INTERACTION OF ANDROGEN RECEPTOR WITH DNA AND COACTIVATORS

Karvonen, U. (2003) · Työväentutkimus Vuosikirja · Cited by 1

Novel mechanisms of Stat3 activation

Arulanandam, R. (2010) · QSpace (Queen's University Library) · Cited by 1

Probing Septin Function Through Interaction Screens: Identification of Novel Septins and Possible Regulatory Mechanisms

Steels, J. D. (2008) · TSpace (University of Toronto) · Cited by 1

Charakterisierung von Punktmutanten in der Linker-Domäne des humanen STAT1-Proteins

Grebe, J. (2016) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5750 · Cited by 1

Die Rolle der Linker-Domäne von STAT1 bei der Regulation transkriptioneller Antworten im Interferon-Signalweg

Bolten, J. C. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4113 · Cited by 1

Molekulare Determinanten zur sequenzspezifischen DNA-Bindung des Transkriptionsfaktors STAT1

Hüntelmann, B. (2018) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6655 · Cited by 1

Signalling from Tyrosine Kinases in the Developing Neurons and Glia of the Mammalian Brain

Cattaneo, E. F., & Gulisano, M. (2000) · Results and problems in cell differentiation · doi:10.1007/978-3-540-48002-0_9 · Cited by 1

Cytokine Signaling in Tissue Engineering

Meyer, T., Ruppert, V., & Maisch, B. (2009) · Springer eBooks · doi:10.1007/978-3-540-77755-7_7

STATs in Cytokine-mediated Transcriptional Regulation

Shuai, K. (2007) · Springer eBooks · doi:10.1007/978-0-387-40049-5_10

Negative Regulators of STAT Function in Drosophila

Henriksen, M. A., & Betz, A. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_38

Protection against Angiotensin II-induced endothelial dysfunction and hypertension via small molecule inhibitors of signal transducer and activator of transcription 3

Johnson, A. W. (2012) · doi:10.17077/etd.ydzu98x2

Negative Regulation of the JAK/STAT Signaling Pathway

Eyles, J. L., & Hilton, D. J. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50436-8

Einfluss von metabolisch wirksamen Hormonen auf die IL-6-induzierte Signaltransduktion

Khouri, C., & Schaper, F. (2012) · RWTH Publications (RWTH Aachen)

Regulation of molecular processes in diffuse large b-cell lymphoma

Högfeldt, T. (2013) · Figshare

Efecto de la sobrenutrición neonatal en la respuesta aguda a la leptina en los periodos prepuberal y peripuberal

González, D. (2014) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

Erythropoietin and Erythropoietin Receptor: History, Structure, Interactions, and Intracellular Signal Transduction

Ghaffari, S., & Constantinescu, S. N. (2004) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm2011

Probing the Tyrosine Phosphorylation State in Breast Cancer by Src Homology 2 Domain Binding

Mayer, B. J. (2004) · Defense Technical Information Center (DTIC) · doi:10.21236/ada428932

SUMO-SPECIFIC PROTEASE 1 CONTROLS LYMPHOID DEVELOPMENT THROUGH REGULATION OF SUMOYLATION/ ACETYLATION SWITCH IN STAT5

Nguyen, T. V. (2011)

SUMO-1 conjugation in normal and stress conditions in vivo

Mikkonen, L. (2013) · Työväentutkimus Vuosikirja

LOSS OF GPRC5A ENHANCES SURVIVAL IN NORMAL AND MALIGNANT LUNG EPITHELIAL CELLS BY ELICITING PERSISTENT STAT3 ACTIVATION INDUCED BY AUTOCRINE LIF

Chen, Y. (2010) · Digital Commons-TMC (Texas Medical Center)

Bedeutung genetischer Polymorphismen in den Genen des Transportproteins SLC6A14, des Leptinrezeptors, des Adiponektins und des Adiponektin-Rezeptors für das Risiko, unter Antipsychotikatherapie Übergewicht zu erleiden

Torno, E.-C. (2012) · doi:10.53846/goediss-1179

Interferon signaling in chronic hepatitis C : mechanisms and implications for therapy

Sarasin-Filipowicz, M. (2008) · edoc (University of Basel) · doi:10.5451/unibas-004702485

PTEN Regulates Beta-Catenin in Androgen Signaling: Implication in Prostate Cancer Progression

Sun, Z. (2004) · doi:10.21236/ada425958

Isolation of Natural Nrf2 Activators from American Ginseng

Abdalrahman, A. (2014) · Scholar Commons (University of South Carolina)

Funktionalität des Interferon TypI- und TypII-Signalwegs in Burkitt-Lymphom-Zellen

Mergler, J. (2008) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.8940

Transcription Factors Stat5a/b and Stat3 in Prostate Cancer Growth and Metastases

Mirtti, T. K., Talati, P. G., & Nevalainen, M. T. (2011) · Springer eBooks · doi:10.1007/978-94-007-2558-4_10

Funktionelle Analysen deregulierter Signalwege transformierter B-Lymphozyten - Das Epstein-Barr-Virus-Onkogen LMP1

Pinkert‐Leetsch, D. (2007) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-213

Inhibition of Radiation-Induced Lung Adenocarcinoma Cell Metastasis by Adenovirus of PIAS3 Overexpression Driven by Radiation-Inducible Promoter (Ad-pig3RRP-PIAS3)

Gao, L., Yu, Q., Li, F., Feng, J.-B., Lu, X., Liu, Q.-J., & Xu, S. (2014) · Journal of Cancer Therapy · doi:10.4236/jct.2014.514136

Inhibition of IL-6-induced STAT3 activation in myeloma cells by protein kinase a

Song, L., Li, Y., & Shen, B. (2001) · Chinese Journal of Cancer Research · doi:10.1007/s11670-001-0039-3

Mutual regulation of EBV LMP1 and CD99 in the pathogenesis of EBV‐associated Hodgkin lymphomas

Min, H. S., Lee, I., & Park, S. H. (2008) · Basic and Applied Pathology · doi:10.1111/j.1755-9294.2008.00001.x

Studies of JAK/STAT signaling in Atlantic salmon

Sobhkhez, M. (2014) · NORA - Norwegian Open Research Archives

Review Signaling by STATs

Ivashkiv, L. B., & Hu, X. (2013)

PIAS3 (protein inhibitor of activated STAT, 3)

Spoden, G. A., & Zwerschke, W. (2011) · Atlas of Genetics and Cytogenetics in Oncology and Haematology · doi:10.4267/2042/44937

Signal Transduction Pathways That Regulate Neural Stem Cell Division and Differentiation

Conti, L., & Cattaneo, E. F. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-298-2_6

Small nuclear RING finger protein SNURF\RNF4 in gonad development and testicular tumors

Hirvonen-Santti, S. J. (2003) · Työväentutkimus Vuosikirja

Pathophysiologie der Blutbildung bei Patienten mit Thrombocytopenia absent radii (TAR)-Syndrom

Wannack, M. (2011) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-14663

Inhibition of Deubiquitinase Activity and Ubiquitination of Jak2 Blocks Cytokine Signaling and Induces Tumor Cell Apoptosis

Kapuria, V. (2010) · Digital Commons-TMC (Texas Medical Center)

Caffeic Acid Phenethyl Ester Suppresses IFN-γ-Induced STAT1 Activation and Gene Expression in Endothelial Cells

Cheng, J. (2012)

MOLECULAR DETERMINANTS OF ANDROGEN ACTION

Santti, H. (2004) · Työväentutkimus Vuosikirja

Interactions Transcription Factor, STAT3 Network of Monomeric IgE: Effect on Microphthalmia Immunological Trigger of Mast Cells by

Sonnenblick, A., Levy, C., & Razin, E. (2011)

Function of PIAS proteins in steroid receptor-dependent signaling

Kotaja, N. (2002) · Työväentutkimus Vuosikirja

Stat3 and Tumor Cell Proliferation

Fakultät, P.-N. (2004)

Jak2 TYROSINE KINASE: NEW INSIGHTS REGARDING STRUCTURE, FUNCTION, AND PHARMACOLOGY

Sandberg, E. M. (2004)

The Jak-Stat Pathway of Cytokine Signaling

Croker, B. A., & Nicola, N. A. (2004) · Humana Press eBooks · doi:10.1007/978-1-59259-747-5_3

Drug Discovery Approaches Targeting the JAK/STAT Pathway

Seidel, H. M., & Rosen, J. (2003) · Springer eBooks · doi:10.1007/978-94-017-3000-6_45

Suppressor of cytokine signaling 4 and 5 in zebrafish development

Trengove, M. C. (2015)

The regulation of gp130 surface expression on monocytes : implications in chronic inflammation

Honke, N., Idm, P., Fischer, R., & Tenbrock, K. (2014) · RWTH Publications (RWTH Aachen)

Identifying a common molecular mechanism for inhibition of MITF and STAT3 by PIAS3

Levy, C., Lee, Y. N., Nechushtan, H., Schueler‐Furman, O., Sonnenblick, A., Hacohen, S., & Razin, E. (2005) · Blood · doi:10.1182/blood-2005-08-3325 · Cited by 36

The enigma of the role of Protein inhibitor of Activated STAT3 (PIAS3) in the immune response

Yagil, Z., Nechushtan, H., Kay, G., Yang, C. M., Kemeny, D. M., & Razin, E. (2010) · Trends in Immunology · doi:10.1016/j.it.2010.01.005 · Cited by 52

PIAS

(2008) · Springer eBooks · doi:10.1007/978-3-540-47648-1_4566

Molecular interactions between STAT3 and protein inhibitor of activated STAT3, and androgen receptor

Yamamoto, T., Sato, N., Sekine, Y., Yumioka, T., Imoto, S., Junicho, A., Fuse, H., & Matsuda, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01026-x · Cited by 24

A New Role for the STAT3 Inhibitor, PIAS3

Levy, C., Nechushtan, H., & Razin, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109236200 · Cited by 92