Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Kelly M Storek"'
Autor:
Kelly M Storek, Joyce Chan, Rajesh Vij, Nancy Chiang, Zhonghua Lin, Jack Bevers III, Christopher M Koth, Jean-Michel Vernes, Y Gloria Meng, JianPing Yin, Heidi Wallweber, Olivier Dalmas, Stephanie Shriver, Christine Tam, Kellen Schneider, Dhaya Seshasayee, Gerald Nakamura, Peter A Smith, Jian Payandeh, James T Koerber, Laetitia Comps-Agrar, Steven T Rutherford
Publikováno v:
eLife, Vol 8 (2019)
Outer membrane proteins (OMPs) in Gram-negative bacteria dictate permeability of metabolites, antibiotics, and toxins. Elucidating the structure-function relationships governing OMPs within native membrane environments remains challenging. We constru
Externí odkaz:
https://doaj.org/article/ce2cff4a5d574858abb6291276ed9aec
Autor:
Dawei Sun, Kelly M. Storek, Dimitry Tegunov, Ying Yang, Christopher P. Arthur, Matthew Johnson, John G. Quinn, Weijing Liu, Guanghui Han, Hany S. Girgis, Mary Kate Alexander, Austin K. Murchison, Stephanie Shriver, Christine Tam, Hiroshi Ijiri, Hiroko Inaba, Tatsuya Sano, Hayato Yanagida, Junichi Nishikawa, Christopher E. Heise, Wayne J. Fairbrother, Man-Wah Tan, Nicholas Skelton, Wendy Sandoval, Benjamin D. Sellers, Claudio Ciferri, Peter A. Smith, Patrick C. Reid, Christian N. Cunningham, Steven T. Rutherford, Jian Payandeh
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract BamA is the central component of the essential β-barrel assembly machine (BAM), a conserved multi-subunit complex that dynamically inserts and folds β-barrel proteins into the outer membrane of Gram-negative bacteria. Despite recent advanc
Externí odkaz:
https://doaj.org/article/bf48c6d78a39468c81c644c4c61faa56
Autor:
Paul White, Samuel F. Haysom, Matthew G. Iadanza, Anna J. Higgins, Jonathan M. Machin, James M. Whitehouse, Jim E. Horne, Bob Schiffrin, Charlotte Carpenter-Platt, Antonio N. Calabrese, Kelly M. Storek, Steven T. Rutherford, David J. Brockwell, Neil A. Ranson, Sheena E. Radford
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
The folding of outer membrane proteins (OMPs) is catalyzed by the βbarrel assembly machinery (BAM). Here, structural and functional analyses of BAM stabilized in distinct conformations elucidate the roles of lateral gate opening and interactions of
Externí odkaz:
https://doaj.org/article/bf4f9d65548640299d6a3b164c8b8b9d
Autor:
Kimberly K. Kajihara, Homer Pantua, Hilda Hernandez-Barry, Meredith Hazen, Kiran Deshmukh, Nancy Chiang, Rachana Ohri, Erick R. Castellanos, Lynn Martin, Marissa L. Matsumoto, Jian Payandeh, Kelly M. Storek, Kellen Schneider, Peter A. Smith, Michael F. T. Koehler, Siao Ping Tsai, Richard Vandlen, Kelly M. Loyet, Gerald Nakamura, Thomas Pillow, Dhaya Seshasayee, Sharookh B. Kapadia, Wouter L. W. Hazenbos
Publikováno v:
mBio, Vol 12, Iss 3 (2021)
Antibiotic treatment of life-threatening P. aeruginosain vitroP. aeruginosa
Externí odkaz:
https://doaj.org/article/55553da6bf96462684a50c1126fff190
Publikováno v:
ACS Omega. 8:12558-12564
Autor:
Laura K. Jennings, Julia E. Dreifus, Courtney Reichhardt, Kelly M. Storek, Patrick R. Secor, Daniel J. Wozniak, Katherine B. Hisert, Matthew R. Parsek
Publikováno v:
Cell Reports, Vol 34, Iss 8, Pp 108782- (2021)
Summary: In cystic fibrosis (CF) airways, Pseudomonas aeruginosa forms cellular aggregates called biofilms that are thought to contribute to chronic infection. To form aggregates, P. aeruginosa can use different mechanisms, each with its own pathogen
Externí odkaz:
https://doaj.org/article/150aff539d3d43ecbb606938179d3c2d
Autor:
Rajesh Vij, Zhonghua Lin, Nancy Chiang, Jean-Michel Vernes, Kelly M. Storek, Summer Park, Joyce Chan, Y. Gloria Meng, Laetitia Comps-Agrar, Peng Luan, Sophia Lee, Kellen Schneider, Jack Bevers, Inna Zilberleyb, Christine Tam, Christopher M. Koth, Min Xu, Avinash Gill, Marcy R. Auerbach, Peter A. Smith, Steven T. Rutherford, Gerald Nakamura, Dhaya Seshasayee, Jian Payandeh, James T. Koerber
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
Abstract Outer membrane proteins (OMPs) in Gram-negative bacteria are essential for a number of cellular functions including nutrient transport and drug efflux. Escherichia coli BamA is an essential component of the OMP β-barrel assembly machinery a
Externí odkaz:
https://doaj.org/article/987be71cec3148fcbac3acf988d53af6
Autor:
Anh Miu, Benjamin D. Sellers, Maria Ruiz-Gonzalez, Jian Payandeh, Peter Liu, L. Martin, Kerry R Buchholz, Dewakar Sangaraju, Guanghui Han, Mark S. Hunter, Elizabeth Skippington, Wendy Sandoval, Emily J. Hanan, Cameron L. Noland, Trisha Dela Vega, Daniel P. DePonte, Erik Verschueren, Danielle L. Swem, Min Xu, Sheerin K. Shahidi-Latham, Nicholas N. Nickerson, Summer Park, Steven T. Rutherford, Nicholas J. Skelton, Qingling Li, Janina Reeder, Kelly M. Storek, Cornelius Gati, Thomas Clairfeuille
Publikováno v:
Nature. 584:479-483
Lipopolysaccharide (LPS) resides in the outer membrane of Gram-negative bacteria where it is responsible for barrier function1,2. LPS can cause death as a result of septic shock, and its lipid A core is the target of polymyxin antibiotics3,4. Despite
Autor:
James Whitehouse, Steven T. Rutherford, Jonathan Machin, Jim E. Horne, Antonio N. Calabrese, Matthew G. Iadanza, David J. Brockwell, Paul White, Anna J. Higgins, Bob Schiffrin, Kelly M. Storek, Charlotte Carpenter-Platt, Sheena E. Radford, Neil A. Ranson, Samuel F. Haysom
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit BamA assists in OMP folding, and the contribution of m
Autor:
Donghong Yan, Cameron L. Noland, Jingyu Diao, Peter Liu, Anand Kumar Katakam, Mike Reichelt, Haruhiko Ogawa, Cary D. Austin, Susan L. Gloor, Yutian Peng, Min Xu, Hayato Yanagida, Patrick C Reid, Jing Kang, Rie Komura, Homer Pantua, Kelly M. Storek, Yiming Xu, Michael Volny, Wendy Sandoval, Jeremy Murray, Nicholas N. Nickerson, Steven T. Rutherford, Junichi Nishikawa, Tatsuya Sano, Hiroko Inaba, Sharookh B. Kapadia, Christian N. Cunningham
Publikováno v:
Journal of Bacteriology
Lipoprotein diacylglyceryl transferase (Lgt) catalyzes the first step in the biogenesis of Gram-negative bacterial lipoproteins which play crucial roles in bacterial growth and pathogenesis. We demonstrate that Lgt depletion in a clinical uropathogen