dor_id: 4133778

506.#.#.a: Público

590.#.#.d: Los artículos enviados a "TIP Revista especializada en Ciencias químico-biológicas", se juzgan por medio de un proceso de revisión por pares

510.0.#.a: Consejo Nacional de Ciencia y Tecnología (CONACyT); Sistema Regional de Información en Línea para Revistas Científicas de América Latina, el Caribe, España y Portugal (Latindex) Scientific Electronic Library Online (SciELO); Red de Revistas Científicas de América Latina y el Caribe, España y Portugal (Redalyc); Directory of Open Access Journals (DOAJ); Web Of Science (WoS); EBSCO, Medigraphic, Indice de Revistas Latinoamericanas en Ciencias (Periódica)

561.#.#.u: https://www.zaragoza.unam.mx/

650.#.4.x: Biología y Química

336.#.#.b: article

336.#.#.3: Artículo de Investigación

336.#.#.a: Artículo

351.#.#.6: http://tip.zaragoza.unam.mx/index.php/tip/index

351.#.#.b: TIP Revista especializada en Ciencias Químico-Biológicas

351.#.#.a: Artículos

harvesting_group: RevistasUNAM

270.1.#.p: Revistas UNAM. Dirección General de Publicaciones y Fomento Editorial, UNAM en revistas@unam.mx

590.#.#.c: Open Journal Systems (OJS)

270.#.#.d: MX

270.1.#.d: México

590.#.#.b: Concentrador

883.#.#.u: https://revistas.unam.mx/catalogo/

883.#.#.a: Revistas UNAM

590.#.#.a: Coordinación de Difusión Cultural

883.#.#.1: https://www.publicaciones.unam.mx/

883.#.#.q: Dirección General de Publicaciones y Fomento Editorial, UNAM

850.#.#.a: Universidad Nacional Autónoma de México

856.4.0.u: http://tip.zaragoza.unam.mx/index.php/tip/article/view/503/432

100.1.#.a: Manzanita-Quintero, Katya; Lee-Rivera, Irene; López, Edith; López-Colomé, Ana María

524.#.#.a: Manzanita-Quintero, Katya, et al. (2022). PTP-PEST: Signaling pathways and importance as a therapeutic target in cancer. TIP Revista Especializada en Ciencias Químico-Biológicas; Vol. 25, 2022. Recuperado de https://repositorio.unam.mx/contenidos/4133778

245.1.0.a: PTP-PEST: Signaling pathways and importance as a therapeutic target in cancer

502.#.#.c: Universidad Nacional Autónoma de México

561.1.#.a: Facultad de Estudios Superiores Zaragoza, UNAM

264.#.0.c: 2022

264.#.1.c: 2022-10-20

653.#.#.a: kinases; tyrosine phosphatases; signal transduction; focal adhesion; cell migration; cinasas; fosfatasas de tirosina; transducción de señales; adhesión focal; migración celular

506.1.#.a: La titularidad de los derechos patrimoniales de esta obra pertenece a las instituciones editoras. Su uso se rige por una licencia Creative Commons BY-NC-ND 4.0 Internacional, https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode.es, para un uso diferente consultar al responsable jurídico del repositorio por medio del correo electrónico revistatip@yahoo.com

884.#.#.k: http://tip.zaragoza.unam.mx/index.php/tip/article/view/503

001.#.#.#: tip.oai:ojs.ojs.escire.net:article/503

041.#.7.h: spa

520.3.#.a: Protein tyrosine phosphatase PTP-PEST, also known as PTPN12, is ubiquitously expressed and it is regulated by the phosphorylation of serine and threonine residues. PTPN12 gene is located, in humans, in chromosome 7q11.23. The coded protein comprises an N-terminal region, followed by a tyrosine phosphatase catalytic domain, and a C-terminal tail containing sequences rich in proline, glutamic acid, serine and threonine (PEST), as well as an NPLH (asparagine, proline, leucine, histidine) sequence that functions as a docking site for proteins involved in signal transduction.PTP-PEST regulates various physiological processes such as cell migration, immune response and neuronal activity by phosphorylating multiple substrates; among them several cytoskeleton adaptor proteins such as paxillin, and others involved in signal transduction pathways, some of which have not been completely elucidated.PTP-PEST is altered in several diseases such as cancer, and has been studied as a therapeutic target. This review focuses on its classification, structure and both its physiological and pathological roles.

773.1.#.t: TIP Revista Especializada en Ciencias Químico-Biológicas; Vol. 25 (2022)

773.1.#.o: http://tip.zaragoza.unam.mx/index.php/tip/index

022.#.#.a: ISSN electrónico: 2395-8723; ISSN impreso: 1405-888X

310.#.#.a: Publicación contínua

264.#.1.b: Facultad de Estudios Superiores Zaragoza, UNAM

doi: https://doi.org/10.22201/fesz.23958723e.2022.503

handle: 00f6942b5c5de19a

harvesting_date: 2023-02-15 12:00:00.0

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file_creation_date: 2022-10-18 19:01:41.0

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245.1.0.b: PTP-PEST: Vías de señalización y su importancia como blanco terapéutico en cáncer

last_modified: 2023-02-15 12:00:00

license_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode.es

license_type: by-nc-nd

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Artículo

PTP-PEST: Signaling pathways and importance as a therapeutic target in cancer

Manzanita-Quintero, Katya; Lee-Rivera, Irene; López, Edith; López-Colomé, Ana María

Facultad de Estudios Superiores Zaragoza, UNAM, publicado en TIP Revista especializada en Ciencias Químico-Biológicas, y cosechado de Revistas UNAM

Licencia de uso

Procedencia del contenido

Cita

Manzanita-Quintero, Katya, et al. (2022). PTP-PEST: Signaling pathways and importance as a therapeutic target in cancer. TIP Revista Especializada en Ciencias Químico-Biológicas; Vol. 25, 2022. Recuperado de https://repositorio.unam.mx/contenidos/4133778

Descripción del recurso

Autor(es)
Manzanita-Quintero, Katya; Lee-Rivera, Irene; López, Edith; López-Colomé, Ana María
Tipo
Artículo de Investigación
Área del conocimiento
Biología y Química
Título
PTP-PEST: Signaling pathways and importance as a therapeutic target in cancer
Fecha
2022-10-20
Resumen
Protein tyrosine phosphatase PTP-PEST, also known as PTPN12, is ubiquitously expressed and it is regulated by the phosphorylation of serine and threonine residues. PTPN12 gene is located, in humans, in chromosome 7q11.23. The coded protein comprises an N-terminal region, followed by a tyrosine phosphatase catalytic domain, and a C-terminal tail containing sequences rich in proline, glutamic acid, serine and threonine (PEST), as well as an NPLH (asparagine, proline, leucine, histidine) sequence that functions as a docking site for proteins involved in signal transduction.PTP-PEST regulates various physiological processes such as cell migration, immune response and neuronal activity by phosphorylating multiple substrates; among them several cytoskeleton adaptor proteins such as paxillin, and others involved in signal transduction pathways, some of which have not been completely elucidated.PTP-PEST is altered in several diseases such as cancer, and has been studied as a therapeutic target. This review focuses on its classification, structure and both its physiological and pathological roles.
Tema
kinases; tyrosine phosphatases; signal transduction; focal adhesion; cell migration; cinasas; fosfatasas de tirosina; transducción de señales; adhesión focal; migración celular
Idioma
spa
ISSN
ISSN electrónico: 2395-8723; ISSN impreso: 1405-888X

Enlaces