Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Tomas Jacso"'
Publikováno v:
Bioorganic & Medicinal Chemistry. 27:115043
High-throughput screening of small-molecule libraries has led to the identification of thiadiazoles as a new class of inhibitors against Staphylococcus aureus sortase A (SrtA). N-(5-((4-nitrobenzyl)thio)-1,3,4-thiadiazol-2-yl)nicotinamide (IC50 = 3.8
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34e02830d44e5bbcae45085694c10c17
https://doi.org/10.1016/j.bmc.2019.115043
https://doi.org/10.1016/j.bmc.2019.115043
Autor:
Martin L. Daus, Erwin Schneider, Sandro Keller, Tomas Jacso, Bernd Reif, Mathias Grote, Peter Schmieder
Publikováno v:
Biochemistry. 48:2216-2225
The Escherichia coli maltose transporter belongs to the ATP binding cassette (ABC) transporter superfamily. Recently, the crystal structure of the full transporter MalFGK2 in complex with the maltose binding protein (MBP) was determined [Oldham, M. L
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d27b4db68ed0bb5992587739d8774640
https://doi.org/10.1021/bi801376m
https://doi.org/10.1021/bi801376m
Autor:
Sebastian Fiedler, Sandro Keller, Andi Mainz, Tom Baerwinkel, Benjamin Bardiaux, Tomas Jacso, Hartmut Oschkinat, Uwe Fink, Jana Broecker, Carolyn Vargas, Bernd Reif
Publikováno v:
Journal of the American Chemical Society. 135(50)
In vitro protein-folding studies using chemical denaturants such as urea are indispensible in elucidating the forces and mechanisms determining the stability, structure, and dynamics of water-soluble proteins. By contrast, α-helical membrane-associa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8d89d388848c02982f0c2966b2680e7
https://pubmed.ncbi.nlm.nih.gov/24261476
https://pubmed.ncbi.nlm.nih.gov/24261476
Publikováno v:
The journal of biological chemistry, 287(21): 17040-17049
J. Biol. Chem. 287, 17040-17049 (2012)
J. Biol. Chem. 287, 17040-17049 (2012)
In a recent study we described the second periplasmic loop P2 of the transmembrane protein MalF (MalF-P2) of the maltose ATP-binding cassette transporter (MalFGK(2)-E) as an important element in the recognition of substrate by the maltose-binding pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d338233c051839528c5001ac6ed40c01
https://repository.publisso.de/resource/frl:6403020
https://repository.publisso.de/resource/frl:6403020
Autor:
Franz X. Schmid, Michael Wunderlich, Stephanie Thoms, Klaas E.A. Max, Tomas Jacso, Udo Heinemann, Hauke Lilie, Bernd Reif
Publikováno v:
Journal of molecular biology. 391(5)
In previous work, a strongly stabilized variant of the beta1 domain of streptococcal protein G (Gbeta1) was obtained by an in vitro selection method. This variant, termed Gbeta1-M2, contains the four substitutions E15V, T16L, T18I, and N37L. Here we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96903d6323a1c5352c1c0349fc0a73ba
https://pubmed.ncbi.nlm.nih.gov/19527728
https://pubmed.ncbi.nlm.nih.gov/19527728
Publikováno v:
Biomolecular NMR assignments. 3(1)
We have assigned the (1)H, (15)N, (13)C backbone resonances of the second periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter of Escherichia coli/Salmonella which is important for the recognition of the maltose bin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1b5d8908d3f8c96bb3536eac704b924
https://pubmed.ncbi.nlm.nih.gov/19636938
https://pubmed.ncbi.nlm.nih.gov/19636938
Autor:
W. Trent Franks, Uwe Fink, Jana Broecker, Hartmut Oschkinat, Tomas Jacso, Bernd Reif, Sandro Keller, Honor May Rose
Membrane proteins in their native cellular membranes are accessible by dynamic nuclear polarization magic angle spinning solid-state NMR spectroscopy without the need of purification and reconstitution (see picture). Dynamic nuclear polarization is e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a12f084dc09c2dd0941edaa60e971d3d