The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme

Autor: Ahn, Minkoo, Hagan, Christine L., Bernardo-Gancedo, Ana, De Genst, Erwin, Newby, Francisco N., Christodoulou, John, Dhulesia, Anne, Dumoulin, Mireille, Robinson, Carol V., Dobson, Christopher M., Kumita, Janet R.

Publikováno v: In Biophysical Journal 6 December 2016 111(11):2358-2367

Structure of a low-population intermediate state in the release of an enzyme product

Autor: Alfonso De Simone, Francesco A Aprile, Anne Dhulesia, Christopher M Dobson, Michele Vendruscolo

Publikováno v: eLife, Vol 4 (2015)

Enzymes can increase the rate of biomolecular reactions by several orders of magnitude. Although the steps of substrate capture and product release are essential in the enzymatic process, complete atomic-level descriptions of these steps are difficul

Externí odkaz: https://doaj.org/article/cfa25ee8d4834facbee8cc774bfd8fac

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.

Autor: Francesco A Aprile, Anne Dhulesia, Florian Stengel, Cintia Roodveldt, Justin L P Benesch, Paolo Tortora, Carol V Robinson, Xavier Salvatella, Christopher M Dobson, Nunilo Cremades

Publikováno v: PLoS ONE, Vol 8, Iss 6, p e67961 (2013)

Oligomerization in the heat shock protein (Hsp) 70 family has been extensively documented both in vitro and in vivo, although the mechanism, the identity of the specific protein regions involved and the physiological relevance of this process are sti

Externí odkaz: https://doaj.org/article/2ed38829261348cb83530af159a2c8db

Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species

Autor: Tuomas P. J. Knowles, Janet R. Kumita, Anne Dhulesia, Christopher M. Dobson, Giuliana Fusco, Paolo Arosio, Paolo Tortora, Francesco A. Aprile, Serene W. Chen, Nunilo Cremades, Michele Vendruscolo

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname

The Hsp70 family of chaperones plays an essential role in suppressing protein aggregation in the cell. Here we investigate the factors controlling the intrinsic ability of human Hsp70 to inhibit the elongation of amyloid fibrils formed by the Parkins

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98045d5382e5c43f07fc2e20b5e6e96a
http://hdl.handle.net/10261/165287

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain

Autor: Paolo Tortora, Carol V. Robinson, Francesco A. Aprile, Christopher M. Dobson, Anne Dhulesia, Florian Stengel, Cintia Roodveldt, Nunilo Cremades, Xavier Salvatella, Justin L. P. Benesch

Publikováno v: Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
Digital.CSIC. Repositorio Institucional del CSIC
PLoS ONE, Vol 8, Iss 6, p e67961 (2013)
PLoS ONE

Oligomerization in the heat shock protein (Hsp) 70 family has been extensively documented both in vitro and in vivo, although the mechanism, the identity of the specific protein regions involved and the physiological relevance of this process are sti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::513ef82df13eea8d9eaa5f29e6760c60
https://doi.org/10.1371/journal.pone.0067961