Zobrazeno 1 - 10
of 176
pro vyhledávání: '"Frederick W Dahlquist"'
Autor:
Davi R Ortega, Guoya Mo, Kwangwoon Lee, Hongjun Zhou, Jerome Baudry, Frederick W Dahlquist, Igor B Zhulin
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 11, p e1003337 (2013)
Bacterial chemotaxis is one of the best studied signal transduction pathways. CheW is a scaffold protein that mediates the association of the chemoreceptors and the CheA kinase in a ternary signaling complex. The effects of replacing conserved Arg62
Externí odkaz:
https://doaj.org/article/2b9368f8d60644a2bce96db8a77ed23d
Autor:
Nicholas L. Bartelli, Victor J. Passanisi, Karolina Michalska, Kiho Song, Dinh Q. Nhan, Hongjun Zhou, Bonnie J. Cuthbert, Lucy M. Stols, William H. Eschenfeldt, Nicholas G. Wilson, Jesse S. Basra, Ricardo Cortes, Zainab Noorsher, Youssef Gabraiel, Isaac Poonen-Honig, Elizabeth C. Seacord, Celia W. Goulding, David A. Low, Andrzej Joachimiak, Frederick W. Dahlquist, Christopher S. Hayes
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-17 (2022)
Contact-dependent growth inhibition (CDI) is an important mechanism of bacterial competition. Here, Bartelli et al. show that proteolytic processing of a CDI toxin induces a conformational switch required for translocation into target bacteria.
Externí odkaz:
https://doaj.org/article/86ac2e542326412c8e314121e49b5241
Autor:
Nicholas L. Bartelli, Victor J. Passanisi, Karolina Michalska, Kiho Song, Dinh Q. Nhan, Hongjun Zhou, Bonnie J. Cuthbert, Lucy M. Stols, William H. Eschenfeldt, Nicholas G. Wilson, Jesse S. Basra, Ricardo Cortes, Zainab Noorsher, Youssef Gabraiel, Isaac Poonen-Honig, Elizabeth C. Seacord, Celia W. Goulding, David A. Low, Andrzej Joachimiak, Frederick W. Dahlquist, Christopher S. Hayes
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-1 (2022)
Externí odkaz:
https://doaj.org/article/01fc3aaf029c427cba9b0bc69da67bf3
Autor:
Nicholas L. Bartelli, Victor J. Passanisi, Karolina Michalska, Kiho Song, Dinh Q. Nhan, Hongjun Zhou, Bonnie J. Cuthbert, Lucy M. Stols, William H. Eschenfeldt, Nicholas G. Wilson, Jesse S. Basra, Ricardo Cortes, Zainab Noorsher, Youssef Gabraiel, Isaac Poonen-Honig, Elizabeth C. Seacord, Celia W. Goulding, David A. Low, Andrzej Joachimiak, Frederick W. Dahlquist, Christopher S. Hayes
Publikováno v:
Nature communications, vol 13, iss 1
Many Gram-negative bacteria use CdiA effector proteins to inhibit the growth of neighboring competitors. CdiA transfers its toxic CdiA-CT region into the periplasm of target cells, where it is released through proteolytic cleavage. The N-terminal cyt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa2c31335a78f5ed8c16d28c27a70a6d
https://pubmed.ncbi.nlm.nih.gov/36271082
https://pubmed.ncbi.nlm.nih.gov/36271082
Autor:
Francesco Ricci, Frederick W. Dahlquist, Kevin W. Plaxco, Alessandra Troina, Davide Mariottini, Gabriel Ortega
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 32
Proc Natl Acad Sci U S A
Proc Natl Acad Sci U S A
Cooperativity enhances the responsiveness of biomolecular receptors to small changes in the concentration of their target ligand, albeit with a concomitant reduction in affinity. The binding midpoint of a two-site receptor with a Hill coefficient of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98ebb58ad3893d22b9a621d5e631930c
https://escholarship.org/uc/item/5qk927t5
https://escholarship.org/uc/item/5qk927t5
Publikováno v:
ACS sensors, vol 3, iss 7
The ability to measure the levels of diagnostically relevant proteins, such as antibodies, directly at the point of care could significantly impact healthcare. Thus motivated, we explore here the E-DNA “scaffold” sensing platform, a rapid, conven
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9675e41f8f77427a4f971df52f91c0b
https://doi.org/10.1021/acssensors.8b00311
https://doi.org/10.1021/acssensors.8b00311
Publikováno v:
Journal of the American Chemical Society. 139:17890-17901
Hydration water on the surface of a protein is thought to mediate the thermodynamics of protein-ligand interaction. For hydration water to play a role beyond modulating global protein solubility or stability, the thermodynamic properties of hydration
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15862168c830c8a988fa650e0a2ea1a1
https://doi.org/10.1021/jacs.7b08606
https://doi.org/10.1021/jacs.7b08606
Autor:
Di Kang, Kevin W. Plaxco, Demosthenes P. Morales, Sheng Sun, Frederick W. Dahlquist, Martin Kurnik
Publikováno v:
Journal of the American Chemical Society, vol 139, iss 35
Here we demonstrate a new class of reagentless, single-step sensors for monitoring protein-protein and protein-peptide interactions that is the electrochemical analog of fluorescence polarization (fluorescence anisotropy), a versatile optical approac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b77f1623f72276b0a84311c56d2b627
https://doi.org/10.1021/jacs.7b05953
https://doi.org/10.1021/jacs.7b05953
Publikováno v:
Protein Science. 26:1535-1546
Autophosphorylating histidine kinase CheA is central to signaling in bacterial chemotaxis. The kinase donates its phosphoryl group to two response regulators, CheY that controls flagellar rotation and thus motility and CheB, crucial for sensory adapt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::df41454ad33a37c2e30c4e8cd2d1721a
https://doi.org/10.1002/pro.3179
https://doi.org/10.1002/pro.3179
Autor:
Thuc-Quyen Nguyen, Nathan D. Kirchhofer, Frederick W. Dahlquist, Guillermo C. Bazan, Zachary D. Rengert
Publikováno v:
Chem. 2:240-257
Summary For emerging bioelectronic technologies, charge-transfer processes remain rate limited by energy-level mismatching and poor contacts at biotic-abiotic interfaces. Direct chemical modification of these interfaces represents an underdeveloped a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03d0633b8caf8ab2649a36a32c8d5a6e
https://doi.org/10.1016/j.chempr.2017.01.001
https://doi.org/10.1016/j.chempr.2017.01.001