Výsledky vyhledávání - "MESH: Thymosin"

Dynamics of the intrinsically disordered protein NUPR1 in isolation and in its fuzzy complexes with DNA and prothymosin α

Autor: José L. Neira, Bruno Rizzuti, Caterina Ricci, Juan L. Iovanna, Maria Grazia Ortore, Martina Palomino-Schätzlein

Publikováno v: Biochimica et Biophysica Acta Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, 2019, 1867 (11), pp.140252. ⟨10.1016/j.bbapap.2019.07.005⟩
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2019, 1867 (11), pp.140252. ⟨10.1016/j.bbapap.2019.07.005⟩
Digital.CSIC. Repositorio Institucional del CSIC
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13 pags., 7 figs.
Intrinsically disordered proteins (IDPs) explore diverse conformations in their free states and, a few of them, also in their molecular complexes. This functional plasticity is essential for the function of IDPs, although their

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c4bf27d671b40c74833f256f69b2426
https://pubmed.ncbi.nlm.nih.gov/31325636

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Longitudinal Analysis of Gene Expression in Porcine Skeletal Muscle After Post-Injection Local Injury

Autor: Pierre-Louis Toutain, François Hatey, Pierre J. Ferré, Magali SanCristobal, Agnès Bonnet, Gwenola Tosser-Klopp, Laurence Liaubet, Didier Concordet, Emmanuelle Uro-Coste, Hervé P. Lefebvre

Publikováno v: Pharmaceutical Research
Pharmaceutical Research, American Association of Pharmaceutical Scientists, 2007, 24 (8), pp.1480-9. ⟨10.1007/s11095-007-9266-8⟩
Pharmaceutical Research, 2007, 24 (8), pp.1480-9. ⟨10.1007/s11095-007-9266-8⟩
Pharmaceutical Research / Pharmaceutical Research (Dordrecht)
Pharmaceutical Research / Pharmaceutical Research (Dordrecht), 2007, 24 (8), pp.1480-9. ⟨10.1007/s11095-007-9266-8⟩

International audience; PURPOSE: The purpose of this study is to describe the time course of gene expression in a skeletal muscle local injury induced by an intramuscular (IM) injection, and to compare the dynamics of gene expression with pathologica

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6b9ba314b202f22100ab07f58a190e6
https://doi.org/10.1007/s11095-007-9266-8

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Structure, function, and evolution of the beta-thymosin/WH2 (WASP-Homology2) actin-binding module

Autor: Maud Hertzog, Carine van Heijenoort, Louis Renault, Marcel Knossow, Dominique Didry, Eric Guittet, Marie-France Carlier, François-Xavier Cantrelle

Publikováno v: Annals of the New York Academy of Sciences
Annals of the New York Academy of Sciences, Wiley, 2007, 1112, pp.67-75. ⟨10.1196/annals.1415.037⟩

International audience; beta-thymosins are acknowledged G-actin sequesterers. However, in the recent years, the conserved beta-thymosins/WH2 actin-binding module, has been identified in a large number of proteins that all interact with actin and play

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::758c5f8d8a5b7feee886cbdaff54d928
https://hal.archives-ouvertes.fr/hal-00260203

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The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly

Autor: Maud, Hertzog, Carine, van Heijenoort, Dominique, Didry, Martin, Gaudier, Jérôme, Coutant, Benoît, Gigant, Gérard, Didelot, Thomas, Préat, Marcel, Knossow, Eric, Guittet, Marie-France, Carlier

Publikováno v: Cell
Cell, Elsevier, 2004, 117 (5), pp.611-23. ⟨10.1016/S0092-8674(04)00403-9⟩

The widespread beta-thymosin/WH2 actin binding domain has versatile regulatory properties in actin dynamics and motility. beta-thymosins (isolated WH2 domain) maintain monomeric actin in a "sequestered" nonpolymerizable form. In contrast, when repeat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::12d3134cc57f113d1e3015f961b57844
https://hal.archives-ouvertes.fr/hal-00121857

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Ciboulot Regulates Actin Assembly during Drosophila Brain Metamorphosis

Autor: Marie-France Carlier, Thomas Preat, Isabelle Boquet, Rajaa Boujemaa

Publikováno v: Cell
Cell, Elsevier, 2000, 102 (6), pp.797-808. ⟨10.1016/S0092-8674(00)00068-4⟩

A dynamic actin cytoskeleton is essential for the remodeling of cell shape during development, but the specific roles of many actin partners remain unclear. Here we characterize a novel actin binding protein, Ciboulot (Cib), which plays a major role

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Structure and function of a thymic peptide is mimicked by Plasmodium falciparum peptides

Autor: Denise Mattei, M. Dardenne, Benno Müller-Hill, Thierry Fandeur, L. Pereira da Silva, Philippe Dubois, Odile Mercereau-Puijalon, Thierry Blisnick

Publikováno v: Annales de l'Institut Pasteur. Immunology
Annales de l'Institut Pasteur. Immunology, Elsevier Science, 1988, 139 (5), pp.557-567. ⟨10.1016/0769-2625(88)90100-6⟩
Annales de l'Institut Pasteur. Immunology, 1988, 139 (5), pp.557-567. ⟨10.1016/0769-2625(88)90100-6⟩

International audience; Numerous Plasmodium falciparum antigens contain repetitive amino acid sequences. Two blood stage antigens, Pf11-1 and Pf332, were characterized in our laboratories and present high cross-reactivities, defining a family of cros

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81d742de76165c262136d85b78c89cac
https://hal.archives-ouvertes.fr/hal-03246327

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