Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Jonathan Remis"'
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
C9orf72:SMCR8:WDR41 complex has been reported to have GAP activity for both ARF family proteins and the RAB proteins RAB8A and RAB11A. Here the authors provide structural and biochemical evidence for a specific function of the C9orf72 complex as an A
Externí odkaz:
https://doaj.org/article/68ecccfd058a41458fb45ddd911e60ed
Publikováno v:
Bio-Protocol, Vol 6, Iss 2 (2016)
Outer membrane vesicles (OMVs) represent a unique sub-cellular compartment of bacteria that may act as a scaffold for various extracellular activities, including intercellular signaling. Myxococcus xanthus (M. xanthus) is a predatory bacterium that e
Externí odkaz:
https://doaj.org/article/b53ba07bb1c4413c8a0199fc349b6ef7
Autor:
Christoph Schaudinn, Paul Stoodley, Luanne Hall-Stoodley, Amita Gorur, Jonathan Remis, Siva Wu, Manfred Auer, Stefan Hertwig, Debbie Guerrero-Given, Fen Ze Hu, Garth D Ehrlich, John William Costerton, Douglas H Robinson, Paul Webster
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e100002 (2014)
The overwhelming majority of bacteria live in slime embedded microbial communities termed biofilms, which are typically adherent to a surface. However, when several Staphylococcus epidermidis strains were cultivated in static liquid cultures, macrosc
Externí odkaz:
https://doaj.org/article/e44d0a29ed50425f837bdc4351f31163
Autor:
Jeremy J. Axelrod, Petar N. Petrov, Jessie T. Zhang, Jonathan Remis, Bart Buijsse, Robert M. Glaeser, Holger Mȕller
Publikováno v:
bioRxiv
We identify thermal magnetic field fluctuations, caused by thermal electron motion (“Johnson noise”) in electrically conductive materials, as a potential resolution limit in transmission electron microscopy with a phase plate. Specifically, resol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53f502879679e118787f1bbb76d35074
https://doi.org/10.1101/2023.02.12.528160
https://doi.org/10.1101/2023.02.12.528160
Publikováno v:
Biophysical Journal. 122:316a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c61d872d95a86c49cc2cdb589eed1737
https://doi.org/10.1016/j.bpj.2022.11.1775
https://doi.org/10.1016/j.bpj.2022.11.1775
Autor:
Jeremy Axelrod, Jeske Dioquino, Petar Petrov, Jonathan Remis, Robert M. Glaeser, Holger Mueller
Publikováno v:
Biophysical Journal. 121:130a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac506b5b594987dc156bb1b0127a6599
https://doi.org/10.1016/j.bpj.2021.11.2080
https://doi.org/10.1016/j.bpj.2021.11.2080
Publikováno v:
Proceedings of the National Academy of Sciences. 102:18932-18937
To explore the structural basis of the unique selectivity spectrum and conductance of the transmembrane channel protein AqpM from the archaeon Methanothermobacter marburgensis , we determined the structure of AqpM to 1.68-Å resolution by x-ray cryst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f476d3aef500de3beceaa1236d34e051
https://doi.org/10.1073/pnas.0509469102
https://doi.org/10.1073/pnas.0509469102
Autor:
Larry J. W. Miercke, Shahram Khademi, Robert M. Stroud, David Akhavan, John Lee, William Harries, Yaneth Robles, Joseph D. O'Connell, Jonathan Remis
Publikováno v:
Current opinion in structural biology, vol 13, iss 4
The aqua (glycero) porins conduct water (and glycerol) across cell membranes. The structure of these channels reveals a tripathic channel that supports a hydrophobic surface and, opposite to this, a line of eight hydrogen-bond acceptors and four hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3158837fa025bad097be7bbd81771a7
https://doi.org/10.1016/s0959-440x(03)00114-3
https://doi.org/10.1016/s0959-440x(03)00114-3
Autor:
Larry J. W. Miercke, Yaneth Robles-Colmenares, Shahram Khademi, Joseph D. O'Connell, Jonathan Remis, Robert M. Stroud
Publikováno v:
Science (New York, N.Y.), vol 305, iss 5690
The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite pola
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3e7969891a9f988d27dea309ee90488
https://pubmed.ncbi.nlm.nih.gov/15361612
https://pubmed.ncbi.nlm.nih.gov/15361612