Zobrazeno 1 - 10
of 142
pro vyhledávání: '"F, Polizzi"'
Autor:
Bruk Mensa, Nicholas F Polizzi, Kathleen S Molnar, Andrew M Natale, Thomas Lemmin, William F DeGrado
Publikováno v:
eLife, Vol 10 (2021)
Transmembrane signaling proteins couple extracytosolic sensors to cytosolic effectors. Here, we examine how binding of Mg2+ to the sensor domain of an E. coli two component histidine kinase (HK), PhoQ, modulates its cytoplasmic kinase domain. We use
Externí odkaz:
https://doaj.org/article/d5bc844519104cae8d3da4e41b6883b8
Autor:
Paola Bisignano, Chiara Ghezzi, Hyunil Jo, Nicholas F. Polizzi, Thorsten Althoff, Chakrapani Kalyanaraman, Rosmarie Friemann, Matthew P. Jacobson, Ernest M. Wright, Michael Grabe
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Sodium-dependent glucose transporters (SGLTs) transport sugars across the plasma membrane and play important roles in renal sugar reabsorption. Here authors develop structural models of human SGLT1/2 (hSGLT1/2) in complex with inhibitors which helps
Externí odkaz:
https://doaj.org/article/028c1db90c9e4f9fab9c0de09fee91eb
Autor:
Nicholas F. Polizzi, Fabio Pirro, Nathan W. Schmidt, Michael J. Therien, Lijun Liu, Marco Chino, Michael Grabe, William F. DeGrado, Angela Lombardi, James Lincoff, Zachary X Widel
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 52
Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 52
Significance A major mechanism of evolution involves fusing genes that encode single-domain proteins to create multidomain structures that achieve new functions. Here, we develop methods to design multidomain proteins entirely from scratch and achiev
Publikováno v:
Science
A new tool in the protein design toolbox Protein design can compute protein folds from first principles. However, designing new proteins that are functional remains challenging, in part because designing binding interactions requires simultaneous opt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3c3e02da1b0bc9ff551b114325d095a
https://europepmc.org/articles/PMC7526616/
https://europepmc.org/articles/PMC7526616/
Autor:
David N. Beratan, Alison M Maxwell, Yibing Wu, Michael J. Therien, William F. DeGrado, Jeff Rawson, Thomas Lemmin, Shao-Qing Zhang, Nicholas F. Polizzi
Publikováno v:
Nature Chemistry. 9:1157-1164
If we truly understand proteins, we should be able to design functional proteins purposefully from scratch. While the de novo design of proteins has seen many successes1–11, no small molecule ligand- or organic cofactor-binding protein has been des
Publikováno v:
Journal of the American Chemical Society. 139:8412-8415
Challenging photochemistry demands high-potential visible-light-absorbing photo-oxidants. We report (i) a highly electron-deficient Ru(II) complex (eDef-Rutpy) bearing an E1/20/+ potential more than 300 mV more positive than that of any established R
Autor:
Yosuke Kanai, Thomas J. Meyer, Nicholas F. Polizzi, Ninghao Zhou, Andrew M. Moran, Yanming Liu, Michael J. Therien, Animesh Nayak, Olivia F. Williams, Bing Shan, Dillon C. Yost
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 116(33)
The direction of electron flow in molecular optoelectronic devices is dictated by charge transfer between a molecular excited state and an underlying conductor or semiconductor. For those devices, controlling the direction and reversibility of electr
Autor:
William F. DeGrado, Alex Sternisha, Karen P. Fong, Nicholas F. Polizzi, Sophia K. Tan, Kyungchul Yoon, Joel S. Bennett, Joanna S.G. Slusky
Publikováno v:
Biochemistry
Biochemistry, vol 58, iss 30
Biochemistry, vol 58, iss 30
Integrin αIIbβ3, a transmembrane heterodimer, mediates platelet aggregation when it switches from an inactive to an active ligand-binding conformation following platelet stimulation. Central to regulating αIIbβ3 activity is the interaction betwee
Autor:
Lijun Liu, Nicholas F. Polizzi, Yibing Wu, William F. DeGrado, Jessica L. Thomaston, Jun Wang
Publikováno v:
J Am Chem Soc
Journal of the American Chemical Society, vol 141, iss 29
Journal of the American Chemical Society, vol 141, iss 29
The amantadine-resistant S31N mutant of the influenza A M2 proton channel has become prevalent in currently circulating viruses. Here, we have solved an X-ray crystal structure of M2(22–46) S31N that contains two distinct conformational states with