Zobrazeno 1 - 10
of 218
pro vyhledávání: '"Marianne Schiffer"'
Autor:
Leonor Morgado, Sílvia Lourenço, Yuri Y Londer, Marianne Schiffer, P Raj Pokkuluri, Carlos A Salgueiro
Publikováno v:
PLoS ONE, Vol 9, Iss 8, p e105566 (2014)
PpcA is the most abundant member of a family of five triheme cytochromes c7 in the bacterium Geobacter sulfurreducens (Gs) and is the most likely carrier of electrons destined for outer surface during respiration on solid metal oxides, a process that
Externí odkaz:
https://doaj.org/article/fab479a456804d3e8d7b100acc95bc69
Autor:
Matthias Endres, Janaka N. Edirisinghe, Ruiying Wu, Marianne Schiffer, Marianne E. Cuff, Christopher S. Henry, P.R. Pokkuluri, Gyorgy Babnigg, Rosemarie Wilton, Andrzej Joachimiak
Publikováno v:
Protein Science. 26:857-869
We report the structural and biochemical characterization of a novel periplasmic ligand-binding protein, Dret_0059, from Desulfohalobium retbaense DSM 5692, an organism isolated from Lake Retba, in Senegal. The structure of the protein consists of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5221b5d7227c508b477d782ce8643702
https://doi.org/10.1002/pro.3134
https://doi.org/10.1002/pro.3134
Autor:
Kemin Tan, Nassif Tabaja, William J. Ball, Angela J. Ahrendt, Andrew B. Norman, M. Zhou, Terence L. Kirley, Rosemarie Wilton, Andrzej Joachimiak, P.R. Pokkuluri, N. E. C. Duke, Marianne Schiffer
Publikováno v:
Acta Crystallogr F Struct Biol Commun
A high-affinity anti-cocaine monoclonal antibody, designated h2E2, is entering phase 1 clinical trials for cocaine abuse therapy. To gain insight into the molecular details of its structure that are important for binding cocaine and cocaine metabolit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64fb51ae472beca13ec3cd2a157550b9
https://pubmed.ncbi.nlm.nih.gov/31702583
https://pubmed.ncbi.nlm.nih.gov/31702583
Autor:
X. Yang, Joana M. Dantas, Carlos A. Salgueiro, P. Raj Pokkuluri, Yuri Y. Londer, Ana P. Fernandes, N. E. C. Duke, Marianne Schiffer, Pilar C. Portela
Publikováno v:
The journal of physical chemistry. B. 123(14)
The triheme cytochrome PpcA from Geobacter sulfurreducens is highly abundant under several growth conditions and is important for extracellular electron transfer. PpcA plays a central role in transferring electrons resulting from the cytoplasmic oxid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d46b28e9083b01f5b00a0e0b50782c9
https://pubmed.ncbi.nlm.nih.gov/30875222
https://pubmed.ncbi.nlm.nih.gov/30875222
Autor:
Karen L. Mulfort, P. Raj Pokkuluri, Nina Ponomarenko, David M. Tiede, Oleksandr Kokhan, Marianne Schiffer
Publikováno v:
The Journal of Physical Chemistry B. 119:7612-7624
PpcA, a tri-heme cytochrome c7 from Geobacter sulfurreducens, was investigated as a model for photosensitizer-initiated electron transfer within a multi-heme "molecular wire" protein architecture. Escherichia coli expression of PpcA was found to be t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33d7eba348b2f0993abc6d016cad4859
https://doi.org/10.1021/jp511558f
https://doi.org/10.1021/jp511558f
Autor:
Andrzej Joachimiak, Marianne Schiffer, Rosemarie Wilton, Gyorgy Babnigg, P. Raj Pokkuluri, Jeff Dwulit-Smith, Jessica Bearden, Jamey C. Mack, N. E. C. Duke, Hendrik Szurmant, Ella Rakowski
Publikováno v:
MicrobiologyOpen
Anaeromyxobacter dehalogenans is a δ-proteobacterium found in diverse soils and sediments. It is of interest in bioremediation efforts due to its dechlorination and metal-reducing capabilities. To gain an understanding on A. dehalogenans' abilities
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::926cd304e75a5525e8577c596679546e
https://doi.org/10.1002/mbo3.112
https://doi.org/10.1002/mbo3.112
Autor:
P.R. Pokkuluri, Peter Biely, Michael A. Cotta, Xin-Liang Li, Stephen J. Wood, Marianne Schiffer, N. E. C. Duke
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:2588-2592
The structure of the catalytic domain of glucuronoyl esterase Cip2 from the fungus H. jecorina was determined at a resolution of 1.9 Å. This is the first structure of the newly established carbohydrate esterase family 15. The structure has revealed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3d53dddb53cfcb80de401e68b46f0cf
https://doi.org/10.1002/prot.23088
https://doi.org/10.1002/prot.23088
Autor:
Gyorgy Babnigg, Marianne Schiffer, P. Raj Pokkuluri, Minyi Gu, Changsoo Chang, Hendrik Szurmant, Christine Tesar, Andrzej Joachimiak
Publikováno v:
Journal of Bacteriology. 192:1156-1159
We present the crystal structure of the extracytoplasmic domain of the Bacillus subtilis PhoR sensor histidine kinase, part of a two-component system involved in adaptation to low environmental phosphate concentrations. In addition to the PhoR struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9dda6ea61f9004ef05467145bcdd91b
https://doi.org/10.1128/jb.01508-09
https://doi.org/10.1128/jb.01508-09
Autor:
Yuri Y. Londer, X. Yang, N. E. C. Duke, P.R. Pokkuluri, Jill Erickson, Valerie Orshonsky, Marianne Schiffer, G. Johnson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1797(2):222-232
Periplasmic cytochromes c(7) are important in electron transfer pathway(s) in Fe(III) respiration by Geobacter sulfurreducens. The genome of G. sulfurreducens encodes a family of five 10-kDa, three-heme cytochromes c(7). The sequence identity between
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dbd2b615a5c64d199d7275c087bf224
Autor:
Leonor Morgado, Carlos A. Salgueiro, Ana P. Fernandes, Marianne Schiffer, Yuri Y. Londer, P. Raj Pokkuluri
Publikováno v:
Biochemical Journal. 420:485-492
Multihaem cytochromes that could form protein “nanowires” were identified in the Geobacter sulfurreducens genome, and represent a new type of multihaem cytochrome. The sequences of these proteins, two with 12 haems (GSU1996, GSU0592) and one with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::166b6f4cba78a29a2663ea711f3d4f8a
https://doi.org/10.1042/bj20082428
https://doi.org/10.1042/bj20082428