Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Sara L. Milam"'
Autor:
Sara L. Milam, Katie Porter, Masaki Osawa, Yaodong Chen, Chandra P. Joshi, Anne Marie Augustus, Katherine W. Osteryoung, Harold P. Erickson
Publikováno v:
Journal of Biological Chemistry. 292:5207-5215
FtsZ is a homolog of eukaryotic tubulin and is present in almost all bacteria and many archaea, where it is the major cytoskeletal protein in the Z ring, required for cell division. Unlike some other cell organelles of prokaryotic origin, chloroplast
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a123378f284f315402331d528f156bf0
https://doi.org/10.1074/jbc.m116.767715
https://doi.org/10.1074/jbc.m116.767715
Autor:
Christian Krebs, James R. Doroghazi, Sara L. Milam, Deepa Balasubramanian, Joerg Freigang, Jelena Zaitseva, Daniel Vaknin, Nicholas B. Duck
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 116(8)
The crystal structure of the Gram-negative insecticidal protein, GNIP1Aa, has been solved at 2.5-Å resolution. The protein consists of two structurally distinct domains, a MACPF (membrane attack complex/PerForin) and a previously uncharacterized typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5a210ea20c2d67f4cdc0e507d26dc02
https://pubmed.ncbi.nlm.nih.gov/30728296
https://pubmed.ncbi.nlm.nih.gov/30728296
Autor:
Yaodong, Chen, Katie, Porter, Masaki, Osawa, Anne Marie, Augustus, Sara L, Milam, Chandra, Joshi, Katherine W, Osteryoung, Harold P, Erickson
Publikováno v:
The Journal of biological chemistry. 292(13)
FtsZ is a homolog of eukaryotic tubulin and is present in almost all bacteria and many archaea, where it is the major cytoskeletal protein in the Z ring, required for cell division. Unlike some other cell organelles of prokaryotic origin, chloroplast
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2b431342de6955d99631db5e9e5ec73b
https://pubmed.ncbi.nlm.nih.gov/28174299
https://pubmed.ncbi.nlm.nih.gov/28174299
FtsZ protofilaments (pfs) form the bacterial cytokinetic Z ring. Previous work suggested that a conformational change from straight to curved pfs generated the constriction force. In the simplest model, the C-terminal membrane tether is on the outsid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8fe757b7f92b0c7c874b37af40ffa56
https://europepmc.org/articles/PMC5310649/
https://europepmc.org/articles/PMC5310649/
Publikováno v:
Biophysical Journal. 103(1):59-68
FtsZ, the primary cytoskeletal element of the Z ring, which constricts to divide bacteria, assembles into short, one-stranded filaments in vitro. These must be further assembled to make the Z ring in bacteria. Conventional electron microscopy (EM) ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c674bee793eb2e4c2181042124e7825
Publikováno v:
Biochemistry. 51:3100-3109
We have investigated the inhibition by SulA of the assembly of Escherichia coli FtsZ. Using quantitative GTPase and fluorescence assays, we found that SulA inhibition resulted in an increase in the apparent critical concentration for FtsZ assembly. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69200dbb46119b747f1b65f23bbe319f
https://doi.org/10.1021/bi201669d
https://doi.org/10.1021/bi201669d
Autor:
A. Clay Clark, Sara L. Milam
Publikováno v:
Protein Science. 18:2500-2517
Caspases are vital to apoptosis and exist in the cell as inactive zymogens. Dimerization is central to procaspase activation because the active sites are comprised of loops from both monomers. Although initiator procaspases are stable monomers until
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bbdd34bbf297c951e12dabbd4e8003f
https://doi.org/10.1002/pro.259
https://doi.org/10.1002/pro.259
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 110(48)
Bacteriophages take over host resources primarily via the activity of proteins expressed early in infection. One of these proteins, produced by the Escherichia coli phage T7, is gene product (Gp) 0.4. Here, we show that Gp0.4 is a direct inhibitor of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::848d150eb991b64791a23e88ee4a590b
https://pubmed.ncbi.nlm.nih.gov/24218612
https://pubmed.ncbi.nlm.nih.gov/24218612
Autor:
Sara L. Milam, Harold P. Erickson
Publikováno v:
The Journal of biological chemistry. 288(33)
FtsZ from most bacteria assembles rapidly in vitro, reaching a steady-state plateau in 5–10 s after addition of GTP. A recent study used a novel dynamic light-scattering technique to assay the assembly of FtsZ from Caulobacter crescentus (CcFtsZ) a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e862523f3bac47cbbebe712d4886e072
https://pubmed.ncbi.nlm.nih.gov/23824192
https://pubmed.ncbi.nlm.nih.gov/23824192