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

Por De Simone, Alfonso, Aprile, Francesco A, Dhulesia, Anne, Dobson, Christopher M, Vendruscolo, Michele
Publicado no eLife (2015)

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

Por De Simone, Alfonso, Dhulesia, Anne, Soldi, Gemma, Vendruscolo, Michele, Hsu, Shang-Te Danny, Chiti, Fabrizio, Dobson, Christopher M.
Publicado em 2011

Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation

Por Ahn, Minkoo, Waudby, Christopher A., Bernardo-Gancedo, Ana, De Genst, Erwin, Dhulesia, Anne, Salvatella, Xavier, Christodoulou, John, Dobson, Christopher M., Kumita, Janet R.
Publicado no Sci Rep (2017)

Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein**

Por Mossuto, Maria F, Bolognesi, Benedetta, Guixer, Bernat, Dhulesia, Anne, Agostini, Federico, Kumita, Janet R, Tartaglia, Gian G, Dumoulin, Mireille, Dobson, Christopher M, Salvatella, Xavier
Publicado em 2011

Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution

Por Dhulesia, Anne, Cremades, Nunilo, Kumita, Janet R., Hsu, Shang-Te Danny, Mossuto, Maria F., Dumoulin, Mireille, Nietlispach, Daniel, Akke, Mikael, Salvatella, Xavier, Dobson, Christopher M.
Publicado em 2010

The Non-Core Regions of Human Lysozyme Amyloid Fibrils Influence Cytotoxicity

Por Mossuto, Maria F., Dhulesia, Anne, Devlin, Glyn, Frare, Erica, Kumita, Janet R., de Laureto, Patrizia Polverino, Dumoulin, Mireille, Fontana, Angelo, Dobson, Christopher M., Salvatella, Xavier
Publicado em 2010

Hsp70 Oligomerization Is Mediated by an Interaction between the Interdomain Linker and the Substrate-Binding Domain

Por Aprile, Francesco A., Dhulesia, Anne, Stengel, Florian, Roodveldt, Cintia, Benesch, Justin L. P., Tortora, Paolo, Robinson, Carol V., Salvatella, Xavier, Dobson, Christopher M., Cremades, Nunilo
Publicado em 2013

A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis

Por Hagan, Christine L., Johnson, Russell J.K., Dhulesia, Anne, Dumoulin, Mireille, Dumont, Janice, De Genst, Erwin, Christodoulou, John, Robinson, Carol V., Dobson, Christopher M., Kumita, Janet R.
Publicado em 2010

Population of non-native states of lysozyme variants drives amyloid fibril formation

Por Buell, Alexander K., Dhulesia, Anne, Mossuto, Maria F., Cremades, Nunilo, Kumita, Janet R., Dumoulin, Mireille, Welland, Mark E., Knowles, Tuomas P.J., Salvatella, Xavier, Dobson, Christopher M.
Publicado no J Am Chem Soc (2011)

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

Por 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.
Publicado no Biophys J (2016)