Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Stephan L. Ginell"'
Autor:
Patricia S. Langan, Venu Gopal Vandavasi, Kevin L. Weiss, Jonathan B. Cooper, Stephan L. Ginell, Leighton Coates
Publikováno v:
FEBS Open Bio, Vol 6, Iss 12, Pp 1170-1177 (2016)
The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it
Externí odkaz:
https://doaj.org/article/6286bd10149741c0898537416d718fab
Autor:
Patricia S. Langan, Kevin L. Weiss, Venu Gopal Vandavasi, Jerry M. Parks, Sarah J. Cooper, Stephan L. Ginell, Leighton Coates
Publikováno v:
ACS Catalysis. 8:2428-2437
The emergence and dissemination of bacterial resistance to β-lactam antibiotics via β-lactamase enzymes is a serious problem in clinical settings, often leaving few treatment options for infections resulting from multidrug-resistant superbugs. Unde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e0d45a706deff54bb06358ad37cbc32c
https://doi.org/10.1021/acscatal.7b04114
https://doi.org/10.1021/acscatal.7b04114
Autor:
Amit Kaushik, Rohini Mattoo, Trevor A Zandi, Shao-Gang Li, Nicole C. Ammerman, Joel S. Freundlich, Stephan L. Ginell, Sean Ekins, Evan P. Lloyd, Craig A. Townsend, Pankaj Kumar, Alexander L. Perryman, Gyanu Lamichhane, Drew T. Bell
Publikováno v:
Nature chemical biology
Bacterial survival requires an intact peptidoglycan layer, a three-dimensional exoskeleton that encapsulates the cytoplasmic membrane. Historically, the final steps of peptidoglycan synthesis are known to be carried out by D,D-transpeptidases, enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::660e866cdb5a732e197090789449934c
https://doi.org/10.1038/nchembio.2237
https://doi.org/10.1038/nchembio.2237
Autor:
Jonathan B. Cooper, Venu Gopal Vandavasi, Patricia S. Langan, Leighton Coates, Kevin L. Weiss, Stephan L. Ginell
Publikováno v:
FEBS Open Bio
The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d878f1772f368a02283b05d5b8e165e
https://doi.org/10.1002/2211-5463.12132
https://doi.org/10.1002/2211-5463.12132
Autor:
Shao-Gang Li, Keira A. Cohen, José Rogério A. Silva, Joel S. Freundlich, Varsha Chauhan, Pankaj Kumar, Felipe B. d’Andrea, Gyanu Lamichhane, Jerônimo Lameira, Scott Bailey, Cláudio Nahum Alves, Stephan L. Ginell
Publikováno v:
Antimicrobial Agents and Chemotherapy. 61
As a growing number of clinical isolates of Mycobacterium abscessus are resistant to most antibiotics, new treatment options that are effective against these drug-resistant strains are desperately needed. The majority of the linkages in the cell wall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2df300b786a1272605e15299abb594f5
https://doi.org/10.1128/aac.00866-17
https://doi.org/10.1128/aac.00866-17
Publikováno v:
Journal of Synchrotron Radiation. 22:172-174
A practical method for operating existing undulator synchrotron beamlines at photon energies considerably higher than their standard operating range is described and applied at beamline 19-ID of the Structural Biology Center at the Advanced Photon So
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::133499a2a1158861c20cf5906394654b
https://doi.org/10.1107/s1600577514022619
https://doi.org/10.1107/s1600577514022619
Autor:
Eduardo Howard, Alexandra Cousido-Siah, Alain Van Dorsselaer, Alberto Podjarny, Isabelle Hazemann, Andrzej Joachimiak, Andre Mitschler, F.X. Ruiz, Cédric Atmanene, Sarah Sanglier-Cianférani, Stephan L. Ginell, Tatiana Petrova
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 80:2552-2561
The relationship between the structures of protein–ligand complexes existing in the crystal and in solution, essential in the case of fragment-based screening by X-ray crystallography (FBS-X), has been often an object of controversy. To address thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::86c933c85da514b69ee1133d1618b20a
https://doi.org/10.1002/prot.24136
https://doi.org/10.1002/prot.24136
Autor:
Tong Wang, Jianping Zheng, Nadrian C. Seeman, Yi Chen, Pamela E. Constantinou, Nam Nguyen, Stephan L. Ginell, Chengde Mao, Ruojie Sha, Jens J. Birktoft
Publikováno v:
Journal of Molecular Recognition. 25:234-237
DNA is a highly effective molecule for controlling nanometer-scale structure. The convenience of using DNA lies in the programmability of Watson-Crick base-paired secondary interactions, useful both to design branched molecular motifs and to connect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c973f731e64509f41b5a0dd1fdb6dd3
https://doi.org/10.1002/jmr.2183
https://doi.org/10.1002/jmr.2183
Autor:
Stephan L. Ginell, Kevin L. Weiss, Tobias E. Schrader, Leighton Coates, Andreas Ostermann, Stephen J. Tomanicek, Venu Gopal Vandavasi, P. T. Erskine, Jonathan B. Cooper
Publikováno v:
Journal of medicinal chemistry. 59(1)
The catalytic mechanism of class A β-lactamases is often debated due in part to the large number of amino acids that interact with bound β-lactam substrates. The role and function of the conserved residue Lys 73 in the catalytic mechanism of class
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9051abcc0d2330abd878e2865f6e0b5
https://pubmed.ncbi.nlm.nih.gov/26630115
https://pubmed.ncbi.nlm.nih.gov/26630115
Autor:
Krzysztof Lazarski, Isabelle Hazemann, Andrzej Joachimiak, Andre Mitschler, Youngchang Kim, Tatiana Petrova, Grazyna Joachimiak, Alexandra Cousido-Siah, Stephan L. Ginell, Alberto Podjarny, Vladimir Y. Lunin
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 66:1075-1091
Overall and site-specific X-ray-induced damage to porcine pancreatic elastase was studied at atomic resolution at temperatures of 100 and 15 K. The experiments confirmed that irradiation causes small movements of protein domains and bound water molec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0e8577e66070ae5e06ef63f0da76ae6
https://doi.org/10.1107/s0907444910033986
https://doi.org/10.1107/s0907444910033986