Zobrazeno 1 - 7
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pro vyhledávání: '"Moracho, Natalia"'
Autor:
Muñoz-Sáez, Emma1 (AUTHOR) emma.munoz@universidadeuropea.es, Moracho, Natalia2 (AUTHOR) natalia.moracho@universidadeuropea.es, Learte, Ana I. R.3 (AUTHOR) anaisabel.rodriguez@universidadeuropea.es, Collignon, Alice4,5 (AUTHOR) agnes.noel@uliege.be, Arroyo, Alicia G.6 (AUTHOR) agarroyo@cib.csic.es, Noel, Agnés4 (AUTHOR), Sounni, Nor Eddine4,5 (AUTHOR) vvnesounni@uliege.be, Sánchez-Camacho, Cristina7 (AUTHOR) vvnesounni@uliege.be
Publikováno v:
International Journal of Molecular Sciences. Jun2023, Vol. 24 Issue 12, p9944. 14p.
Akademický článek
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Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Moracho, Natalia, Learte, Ana I. R., Muñoz‐Sáez, Emma, Marchena, Miguel A., Cid, María A., Arroyo, Alicia G., Sánchez‐Camacho, Cristina
Publikováno v:
Developmental Dynamics; Feb2022, Vol. 251 Issue 2, p240-275, 36p
Autor:
Emma Muñoz-Sáez, María Antonia Cid, Alicia G. Arroyo, Ana I R Learte, Miguel A Marchena, Natalia Moracho, Cristina Sánchez-Camacho
Publikováno v:
ABACUS. Repositorio de Producción Científica
Universidad Europea (UEM)
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Universidad Europea (UEM)
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
instname
36 p.-3 fig.-2tab.
Membrane-type matrix metalloproteinases (MT-MMPs) are cell membrane-tethered proteinases that belong to the family of the MMPs. Apart from their roles in degradation of the extracellular milieu, MT-MMPs are able to activate th
Membrane-type matrix metalloproteinases (MT-MMPs) are cell membrane-tethered proteinases that belong to the family of the MMPs. Apart from their roles in degradation of the extracellular milieu, MT-MMPs are able to activate th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1012708bb725a42c6907d1af9c67c03
https://hdl.handle.net/11268/10382
https://hdl.handle.net/11268/10382
Publikováno v:
Cells
Volume 10
Issue 9
ABACUS. Repositorio de Producción Científica
Universidad Europea (UEM)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Cells, Vol 10, Iss 2448, p 2448 (2021)
Volume 10
Issue 9
ABACUS. Repositorio de Producción Científica
Universidad Europea (UEM)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Cells, Vol 10, Iss 2448, p 2448 (2021)
26 p.-9 fig.
MT1-MMP/MMP14 belongs to a subgroup of the matrix metalloproteinases family that presents a transmembrane domain, with a cytosolic tail and the catalytic site exposed to the extracellular space. Deficient mice for this enzyme result
MT1-MMP/MMP14 belongs to a subgroup of the matrix metalloproteinases family that presents a transmembrane domain, with a cytosolic tail and the catalytic site exposed to the extracellular space. Deficient mice for this enzyme result
Autor:
Emma Muñoz-Sáez, Natalia Moracho, Ana I. R. Learte, Alice Collingnon, Alicia G. Arroyo, Agnés Noel, Nor Eddine Sounni, Cristina Sánchez-Camacho
14 p.-1 fig.
MT4-MMP (or MMP-17) belongs to the Membrane-Type Matrix Metalloproteinases (MT-MMPs), a distinct subset of the MMP family that is anchored to the cell surface by a glycosylphosphatidylinositol (GPI) motif. Its expression in a variet
MT4-MMP (or MMP-17) belongs to the Membrane-Type Matrix Metalloproteinases (MT-MMPs), a distinct subset of the MMP family that is anchored to the cell surface by a glycosylphosphatidylinositol (GPI) motif. Its expression in a variet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::055b0c9f27a00602096306f643945a7d
https://hdl.handle.net/11268/12153
https://hdl.handle.net/11268/12153