Výsledky vyhledávání - "Nita R. Shah"

Akademický článek

Structural basis for tuning activity and membrane specificity of bacterial cytolysins

Autor: Nita R. Shah, Tomas B. Voisin, Edward S. Parsons, Courtney M. Boyd, Bart W. Hoogenboom, Doryen Bubeck

Publikováno v: Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)

Cholesterol-dependent cytolysins (CDCs) are bacterial pore-forming virulence factors. Cryo-EM structure of an early conformation of the CDC ILY from Streptococcus intermedius, bound to the human immune receptor CD59, provides insight into ILY oligome

Externí odkaz: https://doaj.org/article/bad042a16128475abd06082cd212d8e7

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Akademický článek

Integral membrane pyrophosphatases: a novel drug target for human pathogens?

Autor: Henri Xhaard, Keni Vidilaseris, Nita R. Shah, Adrian Goldman

Publikováno v: AIMS Biophysics, Vol 3, Iss 1, Pp 171-194 (2016)

Membrane-integral pyrophosphatases (mPPases) are found in several human pathogens, including Plasmodium species, the protozoan parasites that cause malaria. These enzymes hydrolyze pyrophosphate and couple this to the pumping of ions (H+ and/or Na+)

Externí odkaz: https://doaj.org/article/6f96bafa07cd42bbb233f40f5a021ee2

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Akademický článek

Insights into the mechanism of membrane pyrophosphatases by combining experiment and computer simulation

Autor: Nita R. Shah, Craig Wilkinson, Steven P. D. Harborne, Ainoleena Turku, Kun-Mou Li, Yuh-Ju Sun, Sarah Harris, Adrian Goldman

Publikováno v: Structural Dynamics, Vol 4, Iss 3, Pp 032105-032105-12 (2017)

Membrane-integral pyrophosphatases (mPPases) couple the hydrolysis of pyrophosphate (PPi) to the pumping of Na+, H+, or both these ions across a membrane. Recently solved structures of the Na+-pumping Thermotoga maritima mPPase (TmPPase) and H+-pumpi

Externí odkaz: https://doaj.org/article/317fe7dc8b6547d3aeee4f1e62d4d008

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Structural basis of light-induced redox regulation in the Calvin–Benson cycle in cyanobacteria

Autor: Charles A. R. Cotton, Doryen Bubeck, Burak V. Kabasakal, Blanca Echeverria, Ciaran McFarlane, James W. Murray, Nita R. Shah

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America

Significance The Calvin–Benson (CB) cycle in plants, algae, and cyanobacteria fixes most of the carbon in most of the biomass on Earth. The CB cycle is regulated by the redox state, which enables it to be turned off in the dark. One part of this re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4047492bfec333c0cc89b2e6f18c78fa
https://doi.org/10.1073/pnas.1906722116

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Structural basis for tuning activity and membrane specificity of bacterial cytolysins

Autor: Courtney M. Boyd, Tomas B. Voisin, Nita R. Shah, Bart W. Hoogenboom, Edward S. Parsons, Doryen Bubeck

Publikováno v: Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)

Cholesterol-dependent cytolysins (CDCs) are pore-forming proteins that serve as major virulence factors for pathogenic bacteria. They target eukaryotic cells using different mechanisms, but all require the presence of cholesterol to pierce lipid bila

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ab7e3ee7b3a761a39ad3a408771ed86
https://doi.org/10.1101/2020.06.16.154724

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Structural basis of light-induced redox regulation in the Calvin cycle

Autor: Doryen Bubeck, Burak V. Kabasakal, Ciaran McFarlane, Charles A. R. Cotton, Nita R. Shah, James W. Murray

In plants, carbon dioxide is fixed via the Calvin cycle in a tightly regulated process. Key to this regulation is the conditionally disordered protein CP12. CP12 forms a complex with two Calvin cycle enzymes, glyceraldehyde-3-phosphate dehydrogenase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e384785a81532677f20b306ee1a1cf14

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Insights into the mechanism of membrane pyrophosphatases by combining experiment and computer simulation

Autor: Yuh-Ju Sun, Adrian Goldman, Steven P. D. Harborne, Nita R. Shah, Craig Wilkinson, Ainoleena Turku, Kun-Mou Li, Sarah A. Harris

Publikováno v: Structural Dynamics
Structural Dynamics, Vol 4, Iss 3, Pp 032105-032105-12 (2017)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e13c338fc523b91cece32175a6c8e81f
http://europepmc.org/articles/PMC5336470

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Bordetella pertussis Lipid A Glucosamine Modification Confers Resistance to Cationic Antimicrobial Peptides and Increases Resistance to Outer Membrane Perturbation

Autor: Robert E. W. Hancock, Rachel C. Fernandez, Nita R. Shah

Publikováno v: Antimicrobial Agents and Chemotherapy. 58:4931-4934

Bordetella pertussis , the causative agent of whooping cough, has many strategies for evading the human immune system. Lipopolysaccharide (LPS) is an important Gram-negative bacterial surface structure that activates the immune system via Toll-like r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54e5b4406cb9afaa3fb9da6a161f0000
https://doi.org/10.1128/aac.02590-14

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Complete Bordetella avium, Bordetella hinzii and Bordetella trematum lipid A structures and genomic sequence analyses of the loci involved in their modifications

Autor: Alina Tirsoaga, Nita R. Shah, Soorej M. Basheer, Sami AlBitar-Nehme, Martin Hirst, Malcolm B. Perry, Rachel C. Fernandez, Martine Caroff, Ilaria Trento, Asmaa El Hamidi, Michelle Moksa, Alexey Novikov

Publikováno v: Innate Immunity. 20:659-672

Endotoxin is recognized as one of the virulence factors of the Bordetella avium bird pathogen, and characterization of its structure and corresponding genomic features are important for an understanding of its role in pathogenicity and for an improve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac83152dcbdf1c1992ad0a7ea46e71ab
https://doi.org/10.1177/1753425913506950

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Minor Modifications to the Phosphate Groups and the C3′ Acyl Chain Length of Lipid A in Two Bordetella pertussis Strains, BP338 and 18-323, Independently Affect Toll-like Receptor 4 Protein Activation

Autor: Nita R. Shah, Martine Caroff, Alexey Novikov, Rachel C. Fernandez, Sami AlBitar-Nehme, Emma J. Kim, Nico Marr

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (17), pp.11751-60. ⟨10.1074/jbc.M112.434365⟩

International audience; Lipopolysaccharides (LPS) of Bordetella pertussis are important modulators of the immune system. Interaction of the lipid A region of LPS with the Toll-like receptor 4 (TLR4) complex causes dimerization of TLR4 and activation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a32810ef9faec275dcfac0b8ee14032
https://doi.org/10.1074/jbc.m112.434365

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