The N-terminal domains of Bacillus subtilis CopA do not form a stable complex in the absence of their inter-domain linker

Autor: Liang Zhou, Geoffrey R. Moore, Nick E. Le Brun, Kristine L. Kay, Oliver Hecht

Publikováno v: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866:275-282

Copper-transporting P-type ATPases, which play important roles in trafficking Cu(I) across membranes for the biogenesis of copper proteins or for copper detoxification, contain a variable number of soluble metal-binding domains at their N-termini. It

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb838a2b6510a9ee7ba05140eba94f31
https://doi.org/10.1016/j.bbapap.2017.11.008

Cu(I)- and proton-binding properties of the first N-terminal soluble domain of Bacillus subtilis CopA

Autor: Liang Zhou, Geoffrey R. Moore, Oliver Hecht, Nick E. Le Brun, Chloe Singleton

Publikováno v: FEBS Journal. 279:285-298

CopA, a P-type ATPase transporter involved in copper detoxification in Bacillus subtilis, contains two soluble Atx1-like domains separated by a short linker at its N-terminus, an arrangement that occurs widely in copper transporters from both prokary

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::14e9d8aa7074d388c6fb3252f43cef7d
https://doi.org/10.1111/j.1742-4658.2011.08422.x

Characterization and Function of the First Antibiotic Isolated from a Vent Organism: The Extremophile Metazoan Alvinella pompejana

Autor: Florence Pradillon, Christoph Gelhaus, Céline Boidin-Wichlacz, Costantino Vetriani, Aurélie Tasiemski, Andreas Tholey, Françoise Gaill, Oliver Hecht, Matthias Leippe, Sascha Jung, Didier Jollivet, Chien-Wen Hung, Joachim Grötzinger, Virginie Cuvillier-Hot, Frank D. Sönnichsen

Publikováno v: PLoS ONE
PLoS ONE, Public Library of Science, 2014, 9 (4), pp.e95737. ⟨10.1371/journal.pone.0095737⟩
Plos One (1932-6203) (Public Library Science), 2014-04, Vol. 9, N. 4, P. 1-10
PLoS ONE, Vol 9, Iss 4, p e95737 (2014)
PLoS ONE, 2014, 9 (4), pp.e95737. ⟨10.1371/journal.pone.0095737⟩

International audience; The emblematic hydrothermal worm Alvinella pompejana is one of the most thermo tolerant animal known on Earth. It relies on a symbiotic association offering a unique opportunity to discover biochemical adaptations that allow a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e388631883474cd1943feabcaaabfc4a
https://hal.sorbonne-universite.fr/hal-01101011/file/Tasiemski_2014_Characterization.pdf

Immunoglobulin class switching appears to be regulated by B-cell antigen receptor-specific T-cell action

Autor: Hans, Lange, Oliver, Hecht, Michael, Zemlin, Ahmad, Trad, Radu I, Tanasa, Harry W, Schroeder, Hilmar, Lemke

Publikováno v: European journal of immunology. 42(4)

Antigen affinity is commonly viewed as the driving force behind the selection for dominant clonotypes that can occur during the T cell-dependent processes of class switch recombination (CSR) and immune maturation. To test this view, we analyzed the v

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7cf107bb0ea588644d0dfb47bff80dca
https://pubmed.ncbi.nlm.nih.gov/22531925

Characterisation of the interaction of colicin A with its co-receptor TolA

Autor: Christopher N. Penfold, Oliver Hecht, Ying Zhang, Geoffrey R. Moore, Chan Li, Richard James

Publikováno v: FEBS letters. 584(11)

Colicin A enters Escherichia coli cells through interaction with endogenous TolA and TolB proteins. In vitro, binding of the colicin A translocation domain to TolA leads to unfolding of TolA. Through NMR studies of the colicin A translocation domain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4b253261d938c2af70cf5211b4baa99
https://pubmed.ncbi.nlm.nih.gov/20433837