Výsledky vyhledávání - "Patrick W. Bilder"

Antibodies against Immunodominant Antigens of Mycobacterium tuberculosis in Subjects with Suspected Tuberculosis in the United States Compared by HIV Status

Autor: Susanne Burger, Suman Laal, Eric Leibert, Patrick W. Bilder, Steven C. Almo, Elisabeth Jenny-Avital, Jacqueline M. Achkar, Arturo Casadevall, Xian Yu

Publikováno v: Clinical and Vaccine Immunology. 17:384-392

The immunodominance of Mycobacterium tuberculosis proteins malate synthase (MS) and MPT51 has been demonstrated in case-control studies with patients from countries in which tuberculosis (TB) is endemic. The value of these antigens for the serodiagno

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90e96d9a7ef521998ff5516b9ae84983
https://doi.org/10.1128/cvi.00503-09

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Structure of the Ternary Complex of Phosphomevalonate Kinase: The Enzyme and Its Family

Autor: John Lawrence Andreassi, Thomas S. Leyh, Matthew W. Vetting, Patrick W. Bilder, Steven L. Roderick

Publikováno v: Biochemistry. 48:6461-6468

The isoprenoid family of compounds contains roughly 25,000 distinct natural products (1, 2), and the classes within the family are often chemically sufficiently diverse to provide the extensive functional overlap often seen in robust metabolic system

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8fb002b16cc2b4a717a17ef042632fb
https://doi.org/10.1021/bi900537u

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Crystal structure of theStreptococcus pneumoniaemevalonate kinase in complex with diphosphomevalonate

Autor: Thomas S. Leyh, Patrick W. Bilder, Steven L. Roderick, John Lawrence Andreassi, Matthew W. Vetting

Publikováno v: Protein Science. 16:983-989

Streptococcus pneumoniae, a ubiquitous gram-positive pathogen with an alarming, steadily evolving resistance to frontline antimicrobials, poses a severe global health threat both in the community and in the clinic. The recent discovery that diphospho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cb8ab01391b84d516fe0947e4d7bb16
https://doi.org/10.1110/ps.072755707

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Crystal Structure of the Ancient, Fe−S Scaffold IscA Reveals a Novel Protein Fold

Autor: Huangen Ding, Patrick W. Bilder, Marcia E. Newcomer

Publikováno v: Biochemistry. 43:133-139

IscA belongs to an ancient family of proteins responsible for iron-sulfur cluster assembly in essential metabolic pathways preserved throughout evolution. We report here the 2.3 A resolution crystal structure of Escherichia coli IscA, a novel fold in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3108de9f47c1a8f8dd26eedaad1da0b
https://doi.org/10.1021/bi035440s

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Mycobacterium tuberculosis Universal Stress Protein Rv2623 Regulates Bacillary Growth by ATP-Binding: Requirement for Establishing Chronic Persistent Infection

Autor: Guofeng Zhu, Melvin So, Patrick W. Bilder, Joshua E. Drumm, Steve C. Almo, John D. Chan, Ian M. Orme, Kaixia Mi, Angelo Izzo, Meihao Sun, Randall J. Basaraba, Helle Bielefeldt-Ohmann, Jihyeon Lim, Thomas S. Leyh, JoAnn M. Tufariello

Publikováno v: PLoS Pathogens, Vol 5, Iss 9 (2009)
PLoS Pathogens

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66f72b82c363d88f9697ec942f2124cf
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2759388/?tool=EBI

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The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme

Autor: Grover L. Waldrop, Marcia E. Newcomer, Loola Al-Kassim, Graeme Bainbridge, Jeffrey F. Ohren, Cindy Spessard, Susan Holley, Sandra Lightle, Patrick W. Bilder, Barry C. Finzel, Michael Melnick, Fang Sun

Publikováno v: Biochemistry. 45(6)

Acetyl-coA carboxylase (ACC) is a central metabolic enzyme that catalyzes the committed step in fatty acid biosynthesis: biotin-dependent conversion of acetyl-coA to malonyl-coA. The bacterial carboxyltransferase (CT) subunit of ACC is a target for t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef8b098a9b9fc63b4fd240805dcac6f9
https://pubmed.ncbi.nlm.nih.gov/16460018

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Mycobacterium tuberculosis Universal Stress Protein Rv2623 Regulates Bacillary Growth by ATP-Binding: Requirement for Establishing Chronic Persistent Infection

Autor: Kaixia Mi, Guofeng Zhu, Ian M. Orme, Jo Ann M. Tufariello, Randall J. Basaraba, Angelo Izzo, Joshua E. Drumm, Patrick W. Bilder, Jihyeon Lim, Helle Bielefeldt-Ohmann, Steve C. Almo, Meihao Sun, Thomas S. Leyh, John Chan, Melvin So

Publikováno v: PLoS Pathogens
PLoS Pathogens, Vol 5, Iss 5, p e1000460 (2009)

Tuberculous latency and reactivation play a significant role in the pathogenesis of tuberculosis, yet the mechanisms that regulate these processes remain unclear. The Mycobacterium tuberculosis universal stress protein (USP) homolog, rv2623, is among

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cdbec0abf523791390025bfbcd72cb6
https://doi.org/10.1371/journal.ppat.1000460

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