Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Emma J. Gehrke"'
Autor:
Emma J Gehrke, Xiafei Zhang, Sheila M Pimentel-Elardo, Andrew R Johnson, Christiaan A Rees, Stephanie E Jones, Hindra, Sebastian S Gehrke, Sonya Turvey, Suzanne Boursalie, Jane E Hill, Erin E Carlson, Justin R Nodwell, Marie A Elliot
Publikováno v:
eLife, Vol 8 (2019)
Lsr2 is a nucleoid-associated protein conserved throughout the actinobacteria, including the antibiotic-producing Streptomyces. Streptomyces species encode paralogous Lsr2 proteins (Lsr2 and Lsr2-like, or LsrL), and we show here that of the two, Lsr2
Externí odkaz:
https://doaj.org/article/5da859c6734a45f2b61730598a77d936
Autor:
Suzanne Boursalie, Sonya Turvey, Christiaan A. Rees, Stephanie Jones, Emma J. Gehrke, Erin E. Carlson, Hindra, Andrew R. Johnson, Jane E. Hill, Marie A. Elliot, Sebastian S. Gehrke, Sheila M. Pimentel-Elardo, Justin R. Nodwell, Xiafei Zhang
Publikováno v:
eLife, Vol 8 (2019)
Lsr2 is a nucleoid-associated protein conserved throughout the actinobacteria, including the antibiotic-producingStreptomyces.Streptomycesspecies encode paralogous Lsr2 proteins (Lsr2 and Lsr2-like, or LsrL), and we show here that of the two, Lsr2 ha
Autor:
Sheila M. Pimentel-Elardo, Andrew R. Johnson, Suzanne Boursalie, Justin R. Nodwell, Emma J. Gehrke, Marie A. Elliot, Sebastian S. Gehrke, Stephanie Jones, Xiafei Zhang, Hindra, Sonya Turvey, Christiaan A. Rees, Erin E. Carlson, Jane E. Hill
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2465a3dd41d9cf7001381677eb2aade6
https://doi.org/10.7554/elife.47691.034
https://doi.org/10.7554/elife.47691.034
Autor:
Yao Shen, Tamiza Nanji, Emma J. Gehrke, Melanie Gloyd, Alba Guarné, Angela Huynh, Marie A. Elliot, Aida Razi, Xiafei Zhang, Joaquin Ortega, Christopher D. Firby
Publikováno v:
Biochimica et biophysica acta. General subjects. 1863(11)
Background Nucleoid associated proteins (NAPs) are essential for chromosome condensation in bacterial cells. Despite being a diverse group, NAPs share two common traits: they are small, oligomeric proteins and their oligomeric state is critical for D