Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Lindsey A, Flanagan"'
Autor:
Rebecca J. Hall, Lindsey A. Flanagan, Michael J. Bottery, Vicki Springthorpe, Stephen Thorpe, Alistair C. Darby, A. Jamie Wood, Gavin H. Thomas
Publikováno v:
mBio, Vol 10, Iss 1 (2019)
ABSTRACT The tsetse fly is the insect vector for the Trypanosoma brucei parasite, the causative agent of human African trypanosomiasis. The colonization and spread of the trypanosome correlate positively with the presence of a secondary symbiotic bac
Externí odkaz:
https://doaj.org/article/c0668f1dd80e47818646dc391404b3f5
Autor:
Vicki Springthorpe, Jamie Wood, Alistair C. Darby, Lindsey A. Flanagan, Rebecca J Hall, Gavin H. Thomas, Michael J. Bottery, Stephen Thorpe
Publikováno v:
Access Microbiology. 1
The development of new microbial growth and analytical techniques is becoming increasingly relevant in relation to ‘unculturable’ organisms. This may involve the modification of existing methods or the development of new, custom procedures. One i
Publikováno v:
Chemelectrochem
[NiFe] hydrogenases are electrocatalysts that oxidize H2 at a rapid rate without the need for precious metals. All membrane‐bound [NiFe] hydrogenases (MBH) possess a histidine residue that points to the electron‐transfer iron sulfur cluster close
Autor:
Lindsey A, Flanagan, Alison, Parkin
Publikováno v:
Biochemical Society Transactions
Hydrogenases are enzymes of great biotechnological relevance because they catalyse the interconversion of H2, water (protons) and electricity using non-precious metal catalytic active sites. Electrochemical studies into the reactivity of NiFe membran
Autor:
Serge Crouzy, Didier Boturyn, Cheickna Cissé, Isabelle Michaud-Soret, Lindsey A. Flanagan, Sylvia Vitale, Sophie Mathieu, Patrice Catty, Mohamed B. Ould Abeih
Publikováno v:
ACS Chemical Biology
ACS Chemical Biology, 2014, 9 (12), pp.2779-2786. ⟨10.1021/cb5005977⟩
ACS Chemical Biology, American Chemical Society, 2014, 9 (12), pp.2779-2786. ⟨10.1021/cb5005977⟩
ACS Chemical Biology, 2014, 9 (12), pp.2779-2786. ⟨10.1021/cb5005977⟩
ACS Chemical Biology, American Chemical Society, 2014, 9 (12), pp.2779-2786. ⟨10.1021/cb5005977⟩
International audience; The FUR protein (ferric uptake regulator) is an iron-dependent global transcriptional regulator. Specific to bacteria, FUR is an attractive antibacterial target since virulence is correlated to iron bioavailability. Recently,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::354ddccd81fe8b2babacbb2314596353
https://hal.science/hal-01110447
https://hal.science/hal-01110447