Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Wendy A. Breyer"'
Autor:
John Corbett, William Daly, Justin Collins, Louis P. Cornacchione, Wendy A. Breyer, Diego Galan, Arthur Glasfeld, Michael Wysota, Grace A. Spatafora, Patrick Tivnan, Dillon B. Nye, Talya Levitz
Publikováno v:
Journal of bacteriology. 197(22)
Streptococcus mutans is the causative agent of dental caries, a significant concern for human health, and therefore an attractive target for therapeutics development. Previous work in our laboratory has identified a homodimeric, manganese-dependent r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d07832e03ce88e34d749f8f2bc1249b1
https://pubmed.ncbi.nlm.nih.gov/26350131
https://pubmed.ncbi.nlm.nih.gov/26350131
Autor:
Brian W. Matthews, Wendy A. Breyer
Publikováno v:
Protein Science. 10:1699-1711
The structures of a number of processive enzymes have been determined recently. These proteins remain attached to their polymeric substrates and may perform thousands of rounds of catalysis before dissociating. Based on the degree of enclosure of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f507a4c0b730b29a233661601ab26faa
https://doi.org/10.1110/ps.10301
https://doi.org/10.1110/ps.10301
Autor:
Brian W. Matthews, Wendy A. Breyer
Publikováno v:
Nature Structural Biology. 7:1125-1128
Exonuclease I (ExoI) from Escherichia coli is a monomeric enzyme that processively degrades single stranded DNA in the 3′ to 5′ direction and has been implicated in DNA recombination and repair. Determination of the structure of ExoI to 2.4 A res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7faa0d0385537b60be0932fc2f62acc1
https://doi.org/10.1038/81978
https://doi.org/10.1038/81978
Autor:
Walter A. Baase, Ciro Cecconi, Julie A. Haack, Ingrid R. Vetter, Brian W. Matthews, Carlos Bustamante, Guoliang Yang, Frederick W. Dahlquist, Wendy A. Breyer
Publikováno v:
Proceedings of the National Academy of Sciences. 97:139-144
Recent advances in single molecule manipulation methods offer a novel approach to investigating the protein folding problem. These studies usually are done on molecules that are naturally organized as linear arrays of globular domains. To extend thes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03be763d5d108418691af084ae7f8c72
https://doi.org/10.1073/pnas.97.1.139
https://doi.org/10.1073/pnas.97.1.139
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 55:129-138
The structure of a hemihedrally twinned protein crystal with two molecules in the asymmetric unit was solved by molecular replacement. The protein, a site-specific mutant of the N-terminal half-molecule of human lactoferrin, is able to undergo an int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc1263768c3d766abaa0b037dba04116
https://doi.org/10.1107/s0907444998009640
https://doi.org/10.1107/s0907444998009640
Autor:
William E. Draper, Wendy A. Breyer, Rebecca K. Phillips, Kate E. Stoll, Seth M. Cohen, Richard G. Brennan, Howard F. Jenkinson, Joseph I. Kliegman, Hattie K. Brown, Rhoda A. T. Brew-Appiah, Nicholas S. Jakubovics, Misha V. Golynskiy, Arthur Glasfeld
Manganese is an essential nutrient for many pathogenic bacteria and has been linked to virulence in a number of species (1–3). A cofactor for a variety of enzymes involved in fighting oxidative stress, manganese is taken up in bacteria by NRAMP and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8a54112d01e25140cdbe59cc9a19d6b
https://europepmc.org/articles/PMC3586275/
https://europepmc.org/articles/PMC3586275/
Publikováno v:
MedEdPORTAL, Vol 2 (2006)
This video tutorial presents all aspects of performing the lumbar puncture procedure. Topics covered in the video include: indications and contraindications; risks and complications; preparing, positioning, and interacting with the patient; necessary
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c7ce137f149f41873e958a0685bc9eb
https://doi.org/10.15766/mep_2374-8265.326
https://doi.org/10.15766/mep_2374-8265.326
Publikováno v:
Medical education. 39(4)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed79464fc8ef893eac4a7632736f8bf8
https://pubmed.ncbi.nlm.nih.gov/15813768
https://pubmed.ncbi.nlm.nih.gov/15813768
Autor:
Geoffrey B. Jameson, Wendy A. Breyer, Bryan F. Anderson, Edward N. Baker, Catherine L. Day, John W. Tweedie
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 58(Pt 6 Pt 2)
Human lactoferrin is an iron-binding protein with a bilobal structure. Each lobe contains a high-affinity binding site for a single Fe(3+) ion and an associated CO(3)(2-) ion. Although iron binds very tightly, it can be released at low pH, with an ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::629058e82df3211704fdb7e21179e042
https://pubmed.ncbi.nlm.nih.gov/12037297
https://pubmed.ncbi.nlm.nih.gov/12037297
Publikováno v:
Journal of molecular biology. 302(4)
To investigate the relative importance of size and polarizability in ligand binding within proteins, we have determined the crystal structures of pseudo wild-type and cavity-containing mutant phage T4 lysozymes in the presence of argon, krypton, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd3f29b08a0eb691b6253898581f2379
https://pubmed.ncbi.nlm.nih.gov/10993735
https://pubmed.ncbi.nlm.nih.gov/10993735