Know more

Our use of cookies

Cookies are a set of data stored on a user’s device when the user browses a web site. The data is in a file containing an ID number, the name of the server which deposited it and, in some cases, an expiry date. We use cookies to record information about your visit, language of preference, and other parameters on the site in order to optimise your next visit and make the site even more useful to you.

To improve your experience, we use cookies to store certain browsing information and provide secure navigation, and to collect statistics with a view to improve the site’s features. For a complete list of the cookies we use, download “Ghostery”, a free plug-in for browsers which can detect, and, in some cases, block cookies.

Ghostery is available here for free: https://www.ghostery.com/fr/products/

You can also visit the CNIL web site for instructions on how to configure your browser to manage cookie storage on your device.

In the case of third-party advertising cookies, you can also visit the following site: http://www.youronlinechoices.com/fr/controler-ses-cookies/, offered by digital advertising professionals within the European Digital Advertising Alliance (EDAA). From the site, you can deny or accept the cookies used by advertising professionals who are members.

It is also possible to block certain third-party cookies directly via publishers:

Cookie type

Means of blocking

Analytical and performance cookies

Realytics
Google Analytics
Spoteffects
Optimizely

Targeted advertising cookies

DoubleClick
Mediarithmics

The following types of cookies may be used on our websites:

Mandatory cookies

Functional cookies

Social media and advertising cookies

These cookies are needed to ensure the proper functioning of the site and cannot be disabled. They help ensure a secure connection and the basic availability of our website.

These cookies allow us to analyse site use in order to measure and optimise performance. They allow us to store your sign-in information and display the different components of our website in a more coherent way.

These cookies are used by advertising agencies such as Google and by social media sites such as LinkedIn and Facebook. Among other things, they allow pages to be shared on social media, the posting of comments, and the publication (on our site or elsewhere) of ads that reflect your centres of interest.

Our EZPublish content management system (CMS) uses CAS and PHP session cookies and the New Relic cookie for monitoring purposes (IP, response times).

These cookies are deleted at the end of the browsing session (when you log off or close your browser window)

Our EZPublish content management system (CMS) uses the XiTi cookie to measure traffic. Our service provider is AT Internet. This company stores data (IPs, date and time of access, length of the visit and pages viewed) for six months.

Our EZPublish content management system (CMS) does not use this type of cookie.

For more information about the cookies we use, contact INRA’s Data Protection Officer by email at cil-dpo@inra.fr or by post at:

INRA
24, chemin de Borde Rouge –Auzeville – CS52627
31326 Castanet Tolosan CEDEX - France

Dernière mise à jour : Mai 2018

Menu Logo Principal

WallTraC

Zone de texte éditable et éditée et rééditée

Kate Cameron

Kate Cameron was appointed as ESR in WallTraC at the University of Lisbon on 1 October 2011 for a period of 3 years.

Kate Cameron

PhD project: Structure and function of novel cohesin-dockerin complexes: role of tailor made nanomachines in plant cell wall hydrolysis

Research interests:Biotechnology Molecular Biology, Plant cell wall (Deconstruction), Cellulosomes, Protein-Protein Interactions (Cohesin-Dockerins), CAZymes (Carbohydrate active enzymes)

Organisation: University of Lisbon

Contact:kate.cameron44(at)gmail.com

Thesis

Structure and function relationships in novel cohesin-dockerin complexes. Defended on 29 January 2015.

pdf  Download the abstract

Scientific papers in peer-reviewed journals

K. Camerona, Shabir Najmudina, Victor D. Alvesa, Edward A. Bayerb, Steven P. Smithc, Pedro Bulea, Helen Wallerd, Luís M.A. Ferreiraa, H.J. Gilbertd, and C.M.G.A. Fontesa (aU.Lisbon, bWeizmann Institute of Science, cQueen's University, dU.Newcastle). Cell-surface attachment of bacterial multi-enzyme complexes involves highly dynamic protein-protein anchors. The Journal Of Biological Chemistry Vol.290, NO.21, pp 13578-13590 (2015)

pdf  Download the abstract

P. Bule, A. Correia, K. Cameron, V.D. Alves, V. Cardoso, C.M.G.A. Fontes and Shabir Najmudin (U.Lisbon).Overexpression, purification, crystallization and preliminary X-ray characterization of the fourth scaffoldin A cohesin from Acetivibrio cellulolyticus in complex with a dockerin from a family 5 glycoside hydrolase. Acta Cryst. F, Vol.70, Issue 8, pp 1065-1067 (2014)

pdf   Download the abstract

K. Cameron, V. D. Alves, P. Bule, L.M.A Ferreira, C.M.G.A. Fontes & S. Najmudin (U.Lisbon). Purification, crystallization and preliminary X-ray characterization of the third ScaB cohesin in complex with an ScaA X-dockerin from Acetivibrio cellulolyticus. Acta Crytallographica Section F. F70, 656-658 (2014)

pdf   Download the abstract

Y. Hamberga, V. Ruimy-Israelia, B. Dassaa, Y. Baraka,b, R. Lamedc, K. Camerond, C.M.G.A. Fontesd, E.A. Bayera and D.B. Frieda (aWeizmann Institute of Science, bTel Aviv University, cU.Lisbon). Elaborate cellulosome architecture of Acetivibrio cellulolyticus revealed by selective screening of cohesin–dockerin interactions. PeerJ Vol.2, pp e636 (2014)

pdf   Download the abstract

M.A. Curriea, K. Cameronb, F.M.V. Diasb, H.L. Spencera, E.A. Bayerc, C.M.G.A. Fontesb, S.P. Smitha, Z. Jiaa (aQueen's University, bU.Lisbon, cWeizmann Institute of Science).Small Angle X-ray Scattering Analysis of Clostridium thermocellum Cellulosome N-terminal Complexes Reveals a Highly Dynamic Structure. The Journal Of Biological Chemistry Vol.288, NO.11, pp 7978–7985 (2013)

pdf   Download the abstract

K. Cameron, V. D. Alves, P. Bule, L.M.A Ferreira, C.M.G.A. Fontes & S. Najmudin (U.Lisbon). Purification, crystallization and preliminary X-ray characterization of the Acetivibrio cellulolyticus type I cohesin ScaC in complex with the ScaB dockerin. Acta Crystallographica Section F. F68, 1030–1033 (2012)

pdf   Download the abstract

Oral presentations

K. Camerona, L.M.A. Ferreiraa, S. Najmudina, H.J. Gilbertb and C.M.G.A. Fontesa (aU. Lisbon, bU.Newcastle). Structural and functional characterization of the type I cohesin-dockerin interaction from Acetivibrio cellulolyticus. Presented at WallTraC symposium in May 2014 in Paris (FR)

pdf  Download Structural and functional characterization of the type I cohesin-dockerin interaction from Acetivibrio cellulolyticus.

Posters

K. Camerona, S. Najmudina, V.D. Alvesa, L.M.A. Ferreiraa, E.A. Bayerb, H.J. Gilbertc and C.M.G.A. Fontesa (aU.Lisbon, bWeizmann Institute of Science, cU.Newcastle). Minor structural changes at the dockerin surface modulate type I cohesin-dockerin specificity in Acetivibrio cellulolyticus cellulosome. Presented at the 5th International Conference on Biosynthesis of Plant Cell Wall on July, 27-31, 2014 in Palm Cove (AU)

pdf  Download Minor structural changes at the dockerin surface modulate type I cohesin-dockerin specificity in Acetivibrio cellulolyticus cellulosome

K. Cameron, C.M.G.A. Fontes and S. Najmudin (U.Lisbon). Crystal Structure of the first Type I ScaB Cohesin from Bacteroides cellulosolvens Cellulosome. Presented at the 3rd ENURS and ESRF-day on April 8, 2014 in Lisbon (PT)

pdf   Download Crystal Structure of the first Type I ScaB Cohesin from Bacteroides cellulosolvensCellulosome

K. Camerona, V. D. Alvesa, P. Bulea, L. M.A. Ferreiraa, H. J. Gilbertb, E. A. Bayerc,C. M.G.A. Fontesa and S. Najmudina (aU.Lisbon, bU.Newcastle, cWeizmann Institute of Science). Structural characterization of Acetivibrio cellulolyticus type I cohesin ScaC in complex with the ScaB dockerin. Presented at the 2nd ENURS and ESRF-day on February 14-15, 2013 in Lisbon (PT); and at the 10th Carbohydrate Bioengineering Meeting on April, 21-24, 2013 in Prague (CZ).

pdf   Download Structural characterization of Acetivibrio cellulolyticus type I cohesin ScaC in complex with the ScaB dockerin