Výsledky vyhledávání - "Tyrosine-Protein Phosphatase (Tyrosine Phosphatase)"

Akademický článek

The KIM-family protein-tyrosine phosphatases use distinct reversible oxidation intermediates: Intramolecular or intermolecular disulfide bond formation

Autor: Machado, Luciana E. S. F., Shen, Tun-Li, Page, Rebecca, Peti, Wolfgang

The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes hematopoietic protein-tyrosine phosphatase (HePTP), striatal-enriched protein-tyrosine phosphatase (STEP), and protein-tyrosine phosphatase receptor type R (PT

Externí odkaz: http://hdl.handle.net/10150/624478
http://arizona.openrepository.com/arizona/handle/10150/624478

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Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains

Autor: Iain M. Hay, Maria Shamin, Eve R. Caroe, Ahmed S. A. Mohammed, Dmitri I. Svergun, Cy M. Jeffries, Stephen C. Graham, Hayley J. Sharpe, Janet E. Deane

Publikováno v: The journal of biological chemistry 299(1), 102750 (2023). doi:10.1016/j.jbc.2022.102750

The journal of biological chemistry 299(1), 102750 (2023). doi:10.1016/j.jbc.2022.102750
Type IIB receptor protein tyrosine phosphatases are cell surface transmembrane proteins that engage in cell adhesion via their extracellular domains (ECDs)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e556fd20d8bf9090fa59b97c084d8d8
https://pubmed.ncbi.nlm.nih.gov/36436563

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PTPN2 regulates the activation of KRAS and plays a critical role in proliferation and survival of KRAS-driven cancer cells

Autor: Zhizhou Xia, Yun Tan, Ruibao Ren, Peihong Wang, Donghe Li, Zhangsen Huang, Ruihong Zhang, Ping Liu, Mingzhu Liu, Bo Jiao

Publikováno v: The Journal of Biological Chemistry

RAS genes are the most commonly mutated in human cancers and play critical roles in tumor initiation, progression, and drug resistance. Identification of targets that block RAS signaling is pivotal to develop therapies for RAS-related cancer. As RAS

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4a1bd4b0bd32acb6e8b74277449e436
http://europepmc.org/articles/PMC7939389

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Akademický článek

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Spatial proteomics reveal that the protein phosphatase PTP1B interacts with and may modify tyrosine phosphorylation of the rhomboid protease RHBDL4

Autor: Ikeda, K, Freeman, M

Publikováno v: The Journal of Biological Chemistry

Rhomboid-like proteins are evolutionarily conserved, ubiquitous polytopic membrane proteins, including the canonical rhomboid intramembrane serine proteases and also others that have lost protease activity during evolution. We still have much to lear

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::9f24a20d5f1f94ef1258b2c58f093745
http://ora.ox.ac.uk/objects/uuid:

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Both intrinsic substrate preference and network context contribute to substrate selection of classical tyrosine phosphatases

Autor: Jaap Heringa, Elena Santonico, Michele Tinti, Mike Schutkowski, Rob Hooft van Huijsduijnen, Antonia Masch, A. Palma, Serena Paoluzi, Luisa Castagnoli, Gianni Cesareni, Bernd W. Brandt

Publikováno v: Journal of Biological Chemistry, 292(12), 4942-4958. American Society for Biochemistry and Molecular Biology Inc.
Palma, A, Tinti, M, Paoluzi, S, Santonico, E, Brandt, B W, Hooft Van Huijsduijnen, R, Masch, A, Heringa, J, Schutkowski, M, Castagnoli, L & Cesareni, G 2017, ' Both intrinsic substrate preference and network context contribute to substrate selection of classical tyrosine phosphatases ', Journal of Biological Chemistry, vol. 292, no. 12, pp. 4942-4958 . https://doi.org/10.1074/jbc.M116.757518

Reversible tyrosine phosphorylation is a widespread posttranslational modification mechanism underlying cell physiology. Thus, understanding the mechanisms responsible for substrate selection by kinases and phosphatases is central to our ability to m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d39c9dde45eaf3947fbaf9033323a41c
https://research.vu.nl/en/publications/68e81ddb-dab5-4bd0-b869-3be55091bcde

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Structure of the WipA protein reveals a novel tyrosine protein phosphatase effector from

Autor: Nikos, Pinotsis, Gabriel, Waksman

Publikováno v: The Journal of Biological Chemistry

Legionnaires' disease is a severe form of pneumonia caused by the bacterium Legionella pneumophila. L. pneumophila pathogenicity relies on secretion of more than 300 effector proteins by a type IVb secretion system. Among these Legionella effectors,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c7bbc8b963917c4f59db31580323c339
https://pubmed.ncbi.nlm.nih.gov/28389563

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γ-Secretase and Presenilin Mediate Cleavage and Phosphorylation of Vascular Endothelial Growth Factor Receptor-1

Autor: Xiaoping Qi, Qing Ruan, William W. Hauswirth, Song Han, Li Liu, Michael E. Boulton, Maria B. Grant, Zhijuan Chen, Jun Cai, Sanford L. Boye

Publikováno v: The Journal of Biological Chemistry

Background: γ-Secretase regulates VEGFR1 signaling. Results: Transmembrane cleavage of VEGFR1 occurs at valine 767, and VE-PTP dephosphorylation of activated VEGFR1 requires full-length presenilin 1. Conclusion: γ-Secretase cleaves VEGFR1, and full

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6c0c280364eb7c565651b746727ab0e
https://doi.org/10.1074/jbc.m111.296590

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Human Siglec-5 Inhibitory Receptor and Immunoglobulin A (IgA) Have Separate Binding Sites in Streptococcal β Protein

Autor: Thomas Areschoug, Therése Nordström, Elin Movert, Anders I. Olin, Syed Raza Ali, Victor Nizet, Ajit Varki

Publikováno v: The Journal of Biological Chemistry

Sialic acid-binding immunoglobulin-like lectins (Siglecs) are receptors believed to be important for regulation of cellular activation and inflammation. Several pathogenic microbes bind specific Siglecs via sialic acid-containing structures at the mi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cc07963085d19919e55569438d8c472
https://doi.org/10.1074/jbc.m111.251728

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Identification of New Substrates of the Protein-tyrosine Phosphatase PTP1B by Bayesian Integration of Proteome Evidence

Autor: Aurelio Pio Nardozza, Michele Tinti, Salvatore Corallino, Stefano Costa, Emanuela Ferrari, Andrew Chatr-aryamontri, Arnaud Ceol, Luisa Castagnoli, Gianni Cesareni

Publikováno v: The Journal of Biological Chemistry

There is growing evidence that tyrosine phosphatases display an intrinsic enzymatic preference for the sequence context flanking the target phosphotyrosines. On the other hand, substrate selection in vivo is decisively guided by the enzyme-substrate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b540074e99c826e0f06f5f282a741b94
https://doi.org/10.1074/jbc.m110.157420

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