Zobrazeno 1 - 10
of 83
pro vyhledávání: '"F. Akif Tezcan"'
Autor:
Sanahan Vijayakumar, Robert G. Alberstein, Zhiyin Zhang, Yi-Sheng Lu, Adriano Chan, Charlotte E. Wahl, James S. Ha, Deborah E. Hunka, Gerry R. Boss, Michael J. Sailor, F. Akif Tezcan
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract The sensitivity and responsiveness of living cells to environmental changes are enabled by dynamic protein structures, inspiring efforts to construct artificial supramolecular protein assemblies. However, despite their sophisticated structur
Externí odkaz:
https://doaj.org/article/c97e1474484349a58911265108dfaca3
Autor:
Lindsey Spiegelman, Adrian Bahn-Suh, Elizabeth T Montaño, Ling Zhang, Greg L Hura, Kathryn A Patras, Amit Kumar, F Akif Tezcan, Victor Nizet, Susan E Tsutakawa, Partho Ghosh
Publikováno v:
PLoS Pathogens, Vol 18, Iss 9, p e1010829 (2022)
Multidrug-resistant (MDR) Enterococcus faecalis are major causes of hospital-acquired infections. Numerous clinical strains of E. faecalis harbor a large pathogenicity island that encodes enterococcal surface protein (Esp), which is suggested to prom
Externí odkaz:
https://doaj.org/article/6211ff82813b4dc687149646b2ae16f0
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
As nanoscale building blocks, proteins offer unique advantages, including monodispersity and atomically tunable interactions, but their self-assembly is limited compared to inorganic or polymeric nanoparticles. Here, the authors show modular self-ass
Externí odkaz:
https://doaj.org/article/42a0cecdb4204f568afd5f6acaab507a
Autor:
Rohit H. Subramanian, Sarah J. Smith, Robert G. Alberstein, Jake B. Bailey, Ling Zhang, Giovanni Cardone, Lauri Suominen, Mohamed Chami, Henning Stahlberg, Timothy S. Baker, F. Akif Tezcan
Publikováno v:
ACS Central Science, Vol 4, Iss 11, Pp 1578-1586 (2018)
Externí odkaz:
https://doaj.org/article/d5650ff98fc34885a71646c140838313
Role of Serine Coordination in the Structural and Functional Protection of the Nitrogenase P-Cluster
Publikováno v:
J Am Chem Soc
Nitrogenase catalyzes the multi-electron reduction of dinitrogen to ammonia. Electron transfer in the catalytic protein (MoFeP) proceeds through a unique [8Fe-7S] cluster (P-cluster) to the active site (FeMoco). In the reduced, all-ferrous (PN) state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c1d5f6b659f6375daa7a6938f640b3a
https://doi.org/10.1021/jacs.2c09480
https://doi.org/10.1021/jacs.2c09480
Publikováno v:
Biochemistry
Metals can play key roles in stabilizing protein structures, but ensuring their proper incorporation is a challenge when a metalloprotein is overexpressed in a non-native cellular environment. Here, we have used computational protein design tools to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80a49917f4608ac542ff0a6df80e0df9
https://doi.org/10.1021/acs.biochem.2c00369
https://doi.org/10.1021/acs.biochem.2c00369
Publikováno v:
Chemical communications (Cambridge, England), vol 58, iss 49
Chem Commun (Camb)
Chem Commun (Camb)
Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. This protein construct is shown - through extensive structural and bio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::425e74527c51c9fac4c671d5f28c6001
https://doi.org/10.1039/d2cc02440c
https://doi.org/10.1039/d2cc02440c
Autor:
Tae Su Choi, F. Akif Tezcan
Publikováno v:
J Am Chem Soc
Selective metal binding is a key requirement not only for the functions of natural metalloproteins but also for the potential applications of artificial metalloproteins in heterogeneous environments such as cells and environmental samples. The select
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a5fd236e522a66e159f113430e05d9b
https://pubmed.ncbi.nlm.nih.gov/36154053
https://pubmed.ncbi.nlm.nih.gov/36154053
Nitrogenase catalyzes the multi-electron reduction of dinitrogen to ammonia. Electron transfer in the catalytic protein (MoFeP) proceeds through a unique [8Fe-7S] cluster (P-cluster) to the active site (FeMoco). In the reduced, all-ferrous (PN) state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d7d099e36b1f1e9857dea44fac365699
https://doi.org/10.26434/chemrxiv-2022-wjqq6
https://doi.org/10.26434/chemrxiv-2022-wjqq6
Autor:
Jerika A. Chiong, F. Akif Tezcan, Yiying Li, Rohit H. Subramanian, Jie Zhu, Jake B. Bailey, Eyal Golub
Publikováno v:
Nature Protocols. 16:3264-3297
The self-assembly of proteins into sophisticated multicomponent assemblies is a hallmark of all living systems and has spawned extensive efforts in the construction of novel synthetic protein architectures with emergent functional properties. Protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b333182ec597b3a7ad7cda6ca08a194c
https://doi.org/10.1038/s41596-021-00535-z
https://doi.org/10.1038/s41596-021-00535-z