Výsledky vyhledávání - "Felipe Hornos"

Akademický článek

Enzyme–Iron Oxide Nanoassemblies: A Review of Immobilization and Biocatalytic Applications

Autor: Ángeles Valls-Chivas, Javier Gómez, Jose I. Garcia-Peiro, Felipe Hornos, Jose L. Hueso

Publikováno v: Catalysts, Vol 13, Iss 6, p 980 (2023)

In the search for new biotechnological advances, increasing attention is currently being paid to the development of magnetic nanoplatforms loaded with enzymes, since, on the one hand, they can be recovered and reused, and on the other hand, they impr

Externí odkaz: https://doaj.org/article/4d121c4ccd394b5297c6fab56bb3fb9b

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Akademický článek

The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer

Autor: José L. Neira, A. Marcela Giudici, Felipe Hornos, Arantxa Arbe, Bruno Rizzuti

Publikováno v: International Journal of Molecular Sciences, Vol 19, Iss 12, p 3902 (2018)

The 191-residue-long LrtA protein of Synechocystis sp. PCC 6803 is involved in post-stress survival and in stabilizing 70S ribosomal particles. It belongs to the hibernating promoting factor (HPF) family, intervening in protein synthesis. The protein

Externí odkaz: https://doaj.org/article/343b41f19cef4f1fa258030a15fceb6c

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The muscle-relaxing C-terminal peptide from troponin I populates a nascent helix, facilitating binding to tropomyosin with a potent therapeutic effect

Autor: Han-Zhong Feng, Felipe Hornos, Jian Ping Jin, Martina Palomino-Schätzlein, Bruno Rizzuti, José L. Neira, David F. Wieczorek

Publikováno v: Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
Zaguán: Repositorio Digital de la Universidad de Zaragoza
Universidad de Zaragoza
JOURNAL OF BIOLOGICAL CHEMISTRY
r-CIPF. Repositorio Institucional Producción Científica del Centro de Investigación Principe Felipe (CIPF)
Universitat Rovira i virgili (URV)
The Journal of Biological Chemistry

The conserved C-terminal end segment of troponin I (TnI) plays a critical role in regulating muscle relaxation. This function is retained in the isolated C-terminal 27 amino acid peptide (residues 184-210) of human cardiac TnI (HcTnI-C27): When added

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::009fc79036334ac9d5af5ed53edbd703
http://zaguan.unizar.es/record/101648

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Human importin α3 and its N-terminal truncated form, without the importin-β-binding domain, are oligomeric species with a low conformational stability in solution

Autor: Juan Román Luque-Ortega, Bruno Rizzuti, José L. Neira, Clara Díaz-García, Javier Gómez, Arantxa Arbe, Manuel Prieto, Jade K. Forwood, A. Marcela Giudici, Juan L. Iovanna, Ana Coutinho, Felipe Hornos, Carlos Alfonso, Ana Cámara-Artigas

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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[Background]: Eukaryotic cells have a continuous transit of macromolecules between the cytoplasm and the nucleus. Several carrier proteins are involved in this transport. One of them is importin α, which must form a complex with importin β to accom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::371f92e6f3b8357a0daa2d397d2df645
https://pubmed.ncbi.nlm.nih.gov/32234409

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The isolated armadillo-repeat domain of Plakophilin 1 is a monomer in solution with a low conformational stability

Autor: Juan Carlos Álvarez-Pérez, Inés Díaz-Cano, María Esther Fárez-Vidal, José G. Hernández-Cifre, Sergio Martínez-Rodríguez, A. Marcela Giudici, Ana Cámara-Artigas, José L. Neira, Felipe Hornos

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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10 pags., 6 figs., 1 tab.
Plakophilin 1 (PKP1) is a member of the armadillo repeat family of proteins. It serves as a scaffold component of desmosomes, which are key structural components for cell–cell adhesion. We have embarked on the biophys

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d110e3882951ebef05e6221f9450e004
https://doi.org/10.1016/j.jsb.2020.107569

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Competitive inhibition of protein adsorption to silica surfaces by their coating with high density charge polyelectrolytes

Autor: Rocío Esquembre, Felipe Hornos, Javier Gómez

Publikováno v: Colloids and Surfaces B: Biointerfaces. 191:110993

The adsorption of proteins to silica surface is a common process mainly governed by the electrostatic attractive interaction between the pH-dependent negatively silica surface and the positive charges of the biomolecule. This process often reduces th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cb3fccb28e434dd7d0dacd07f15e942
https://doi.org/10.1016/j.colsurfb.2020.110993

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The histidine phosphocarrier protein, HPr, binds to the highly thermostable regulator of sigma D protein, Rsd, and its isolated helical fragments

Autor: Ana Cámara-Artigas, Concetta Cozza, Olga Abian, José L. Neira, Adrián Velázquez-Campoy, Felipe Hornos

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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The phosphotransferase system (PTS) controls the preferential use of sugars in bacteria and it is also involved in other processes, such as chemotaxis. It is formed by a protein cascade in which the first two proteins are general (namely, EI and HPr)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46b2afea32edd9f412598a4e3027b6b2
http://hdl.handle.net/10261/167335

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The Monomeric Species of the Regulatory Domain of Tyrosine Hydroxylase Has a Low Conformational Stability

Autor: Javier Gómez, Ana Cámara-Artigas, Felipe Hornos, Julio Bacarizo, José L. Neira

Publikováno v: Biochemistry. 55(24)

Tyrosine hydroxylase (TyrH) catalyzes the hydroxylation of tyrosine to form 3,4-dihydroxyphenylalanine, the first step in the synthesis of catecholamine neurotransmitters. The protein contains a 159-residue regulatory domain (RD) at its N-terminus th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::083da79b0a389bec41c570b867ff6066
https://pubmed.ncbi.nlm.nih.gov/27224548

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