Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Adela M. Candel"'
Autor:
Valeria A. Risso, Sergio Martinez-Rodriguez, Adela M. Candel, Dennis M. Krüger, David Pantoja-Uceda, Mariano Ortega-Muñoz, Francisco Santoyo-Gonzalez, Eric A. Gaucher, Shina C. L. Kamerlin, Marta Bruix, Jose A. Gavira, Jose M. Sanchez-Ruiz
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
The emergence of novel catalytic functions in ancient proteins likely played a role in the evolution of modern enzymes. Here, the authors use protein sequences from Precambrian beta-lactamases and demonstrate that a single hydrophobic-to-ionizable am
Externí odkaz:
https://doaj.org/article/7c76aaa815614d3a948e230f4b0670e6
Autor:
Giuseppe Nicastro, Adela M. Candel, Michael Uhl, Alain Oregioni, David Hollingworth, Rolf Backofen, Stephen R. Martin, Andres Ramos
Publikováno v:
Cell Reports, Vol 18, Iss 5, Pp 1187-1199 (2017)
Zipcode binding protein 1 (ZBP1) is an oncofetal RNA-binding protein that mediates the transport and local translation of β-actin mRNA by the KH3-KH4 di-domain, which is essential for neuronal development. The high-resolution structures of KH3-KH4 w
Externí odkaz:
https://doaj.org/article/fc9af46783534be98494a16d4cdcbc90
Autor:
Francisco Castillo, Carles Corbi-Verge, Javier Murciano-Calles, Adela M. Candel, Ziying Han, Manuel Iglesias-Bexiga, Javier Ruiz-Sanz, Philip M. Kim, Ronald N. Harty, Jose C. Martinez, Irene Luque
Publikováno v:
Digibug. Repositorio Institucional de la Universidad de Granada
instname
instname
This research has been financed by grants BIO2016-78746-C2-1-R and PID2020-112895RB-100 from the Spanish Ministry of Education and Science (I.L.) including AEI/FEDER EU funds. R.N.H. was funded in part by National Institutes of Health grants AI138052
Autor:
Gloria Gamiz-Arco, Valeria A. Risso, Jose A. Gavira, Adela M. Candel, Beatriz Ibarra-Molero, Eric A. Gaucher, Alvaro Ingles-Prieto, Maria L. Romero-Romero, Jose M. Sanchez-Ruiz
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biochemical Journal
Digibug. Repositorio Institucional de la Universidad de Granada
instname
Biochemical Journal
Digibug. Repositorio Institucional de la Universidad de Granada
Evolution involves not only adaptation, but also the degradation of superfluous features. Many examples of degradation at the morphological level are known (vestigial organs, for instance). However, the impact of degradation on molecular evolution ha
Autor:
Liu He, Andrea Beltrán, Juan C. Gómez-Fernández, Yuqi Jiang, Alessio Ausili, Adela M. Candel, Shijun Zhang, Alejandro Torrecillas, Victoria Gomez-Murcia, José A. Teruel
Publikováno v:
Colloids Surf B Biointerfaces
Curcumin and two bivalent compounds, namely 17MD and 21MO, both obtained by conjugation of curcumin with a steroid molecule that acts as a membrane anchor, were comparatively studied. When incorporated into 1,2-dipalmitoyl-sn-glycero-3-phosphocholine
Autor:
M. Luisa Romero-Romero, Jose M. Sanchez-Ruiz, Gloria Gamiz-Arco, Adela M. Candel, Beatriz Ibarra-Molero
Publikováno v:
Proceedings of the National Academy of Sciences. 114
Tzul et al. (1) report different unfolding rates and similar folding rates for a number of thioredoxins. The authors interpret this result as evidence of the principle of minimal frustration. Their study includes several resurrected Precambrian thior
Autor:
Marta Bruix, Francisco Santoyo-Gonzalez, David Pantoja-Uceda, Mariano Ortega-Muñoz, Jose M. Sanchez-Ruiz, Shina Caroline Lynn Kamerlin, Sergio Martínez-Rodríguez, Valeria A. Risso, Dennis M. Krüger, Jose A. Gavira, Adela M. Candel, Eric A. Gaucher
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature Communications
'Nature Communications ', vol: 8, pages: 16113-1-16113-13 (2017)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature Communications
'Nature Communications ', vol: 8, pages: 16113-1-16113-13 (2017)
Protein engineering studies often suggest the emergence of completely new enzyme functionalities to be highly improbable. However, enzymes likely catalysed many different reactions already in the last universal common ancestor. Mechanisms for the eme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ee0937e9d229b9332b6f0323f5d02c1
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-331231
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-331231
Autor:
Sandra Villegas, Javier Murciano-Calles, Jose C. Martinez, Adela M. Candel, Marta Marin-Argany
Publikováno v:
Biophysical Journal. 103(4):738-747
The temperature-induced misfolding pathway of PDZ3, the third PDZ domain of the PSD95 neuronal protein, is populated by a trimeric β-sheet-rich intermediate state that leads to a stepwise and reversible formation of supramacromolecular structures. U
Publikováno v:
Biophysical Journal. 94(11):4393-4404
The interpretation of phi-values has led to an understanding of the folding transition state ensemble of a variety of proteins. Although the main guidelines and equations for calculating phi are well established, there remains some controversy about
Autor:
Salvador Casares, Adela M. Candel, Jose C. Martinez, F.M Martı́n-Sierra, Vladimir V. Filimonov, Francisco Conejero-Lara
Publikováno v:
FEBS Letters. 553:328-332
We have designed a chimeric protein by connecting a circular permutant of the alpha-spectrin SH3 domain to the proline-rich decapeptide APSYSPPPPP with a three-residue link. Our aim was to obtain a single-chain protein with a tertiary fold that would