Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Aimee M, Eldridge"'
Autor:
Danielle H. Dube, Aimee M. Eldridge, Kanokwan Champasa, Elizabeth A. Stemmler, Scott A. Longwell
Publikováno v:
Molecular & Cellular Proteomics : MCP
Virulence of the gastric pathogen Helicobacter pylori (Hp) is directly linked to the pathogen's ability to glycosylate proteins; for example, Hp flagellin proteins are heavily glycosylated with the unusual nine-carbon sugar pseudaminic acid, and this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffd49e8f5d0fad1bd6820ff793b68fba
https://doi.org/10.1074/mcp.m113.029561
https://doi.org/10.1074/mcp.m113.029561
Publikováno v:
Journal of Pharmaceutical Sciences. 101:1391-1399
The purpose of this study was to probe the fate of a model antigen, a cysteine-free mutant of bacteriophage T4 lysozyme, to the level of fine structural detail, as a consequence of its interaction with an aluminum (Al)-containing adjuvant. Fluorescen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ca0faa03db9283deec4f62b99f894a8
https://doi.org/10.1002/jps.23039
https://doi.org/10.1002/jps.23039
Autor:
Deborah S. Wuttke, Aimee M. Eldridge
Publikováno v:
Nucleic Acids Research
The Saccharomyces cerevisiae protein Cdc13 tightly and specifically binds the conserved G-rich single-stranded overhang at telomeres and plays an essential role in telomere end-protection and length regulation. The 200 residue DNA-binding domain of C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::094bee33b452a0d1538472513a0532a7
https://doi.org/10.1093/nar/gkn017
https://doi.org/10.1093/nar/gkn017
Publikováno v:
Biochemistry. 45:871-879
The single-strand overhang present at telomeres plays a critical role in mediating both the capping and telomerase regulation functions of telomeres. The telomere end-binding proteins, Cdc13 in Saccharomyces cerevisiae, Pot1 in higher eukaryotes, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5c0082e87c09f3f15ecd2156918425e
https://doi.org/10.1021/bi0512703
https://doi.org/10.1021/bi0512703
Autor:
Hyun-Seo Kang, Robert P. Gunsalus, Frederick W. Dahlquist, Eric F. Johnson, Aimee M. Eldridge
Publikováno v:
Biochemistry. 41:15173-15180
DNA binding by the effector domain (NarLC) of the response regulator, NarL, is modulated by the phosphorylation state of the receiver domain (NarLN). The receiver domain appears to block the site of DNA binding in the nonphosphorylated state. Phospho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d5ddb012734108d3403eeabaed8f3b3
https://doi.org/10.1021/bi026254+
https://doi.org/10.1021/bi026254+
Autor:
Aimee M. Eldridge, Walter A. Baase, Brain W. Matthews, Nadine C. Gassner, Sheila D. Snow, Devin L. Drew, Leigh Ann Lipscomb
Publikováno v:
Protein Science. 7:765-773
The substitution of methionines with leucines within the interior of a protein is expected to increase stability both because of a more favorable solvent transfer term as well as the reduced entropic cost of holding a leucine side chain in a defined
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a7a372106ca25e2e1a80a7f2de72fe8
https://doi.org/10.1002/pro.5560070326
https://doi.org/10.1002/pro.5560070326
Publikováno v:
Biochemistry. 41(51)
DNA binding by the effector domain (NarLC) of the response regulator, NarL, is modulated by the phosphorylation state of the receiver domain (NarLN). The receiver domain appears to block the site of DNA binding in the nonphosphorylated state. Phospho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::466ee0404961e7923dc1a67f94eee6fd
https://pubmed.ncbi.nlm.nih.gov/12484754
https://pubmed.ncbi.nlm.nih.gov/12484754
Autor:
Leigh Ann Lipscomb, Nadine C. Gassner, Sheila D. Snow, Aimee M. Eldridge, Walter A. Baase, L. Drew, Brian W. Matthews
Publikováno v:
Protein Science. 7:1481-1481
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c82a3b773e54478b64082f927f363ee1
https://doi.org/10.1002/pro.5560070627
https://doi.org/10.1002/pro.5560070627