Výsledky vyhledávání - "Ian C. Boulton"

Induction of HIV-1 long terminal repeat-mediated transcription by Neisseria gonorrhoeae

Autor: Jodi Pongoski, Scott D. Gray-Owen, Adrienne Chen, Alan Cochrane, Ian C. Boulton

Publikováno v: Scopus-Elsevier

Gonorrhoea enhances the transmission of HIV through increased viral shedding and the increased probability of seroconversion among previously HIV-negative individuals. However, the mechanism(s) underlying these influences remain poorly understood. We

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8d17ae20c59560fd56fddaca1bdea50
https://doi.org/10.1097/00002030-200303070-00019

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Neisserial binding to CEACAM1 arrests the activation and proliferation of CD4+ T lymphocytes

Autor: Scott D. Gray-Owen, Ian C. Boulton

Publikováno v: Nature Immunology

Infection with Neisseria gonorrhoeae can trigger an intense inflammatory response, yet there is little specific immune response or development of immune memory. In addition, gonorrhea typically correlates with a transient reduction in T lymphocyte co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::711033bab57e9500cc9a2109e0105cba
https://doi.org/10.1038/ni769

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Purified meningococcal transferrin-binding protein B interacts with a secondary, strain-specific, binding site in the N-terminal lobe of human transferrin

Autor: Ian C. Boulton, Christopher L. Joannou, Beatrice Gorinsky, Mark D. Retzer, Anthony B. Schryvers, Robert W. Evans, Andrew Gorringe

Publikováno v: Biochemical Journal. 339:143-149

Neisseria meningitidis, grown in iron-limited conditions, produces two transferrin-binding proteins (TbpA and TbpB) that independently and specifically bind human serum transferrin (hTF) but not bovine serum transferrin (bTF). We have used surface pl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c1f6db3bc532aa100da051964365a87b
https://doi.org/10.1042/bj3390143

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CRIMALDDI: platform technologies and novel anti-malarial drug targets

Autor: Donatella Taramelli, Steve A. Ward, Christian Doerig, Henri Vial, Ian C Boulton, Kelly Chibale

Publikováno v: Malaria Journal

The Coordination, Rationalization, and Integration of antiMALarial drug Discovery & Development Initiatives (CRIMALDDI) Consortium, funded by the EU Framework Seven Programme, has attempted, through a series of interactive and facilitated workshops,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::099b1121e014793378597a24b9075ad8
https://archive.lstmed.ac.uk/5280/1/Malaria_J_12_396.pdf

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CRIMALDDI: a co-ordinated, rational, and integrated effort to set logical priorities in anti-malarial drug discovery initiatives

Autor: Steve A. Ward, Ian C Boulton, Solomon Nwaka, Kelly Chibale, Christian Doerig, Michael Lanzer, Donatella Taramelli, Ian Bathurst, Henri Vial

Publikováno v: Malaria Journal
Malaria Journal, 2010, 9 (1), pp.202. ⟨10.1186/1475-2875-9-202⟩
Malaria Journal, BioMed Central, 2010, 9 (1), pp.202. ⟨10.1186/1475-2875-9-202⟩
Malaria Journal, Vol 9, Iss 1, p 202 (2010)
Europe PubMed Central

Despite increasing efforts and support for anti-malarial drug R&D, globally anti-malarial drug discovery and development remains largely uncoordinated and fragmented. The current window of opportunity for large scale funding of R&D into malaria is li

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39168f491a4de60d8ce947d5eb17ce00
https://archive.lstmed.ac.uk/1688/1/MalJ_2010_1475-2875-9-202.pdf

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Neisserial outer membrane vesicles bind the coinhibitory receptor carcinoembryonic antigen-related cellular adhesion molecule 1 and suppress CD4+ T lymphocyte function

Autor: Denise Halliwell, Henry K. Wong, Ian C. Boulton, Andrew Gorringe, Scott D. Gray-Owen, Ofer Mandelboim, Karen M. Reddin, Hannah S. W. Lee

Publikováno v: Infection and immunity. 75(9)

Pathogenic Neisseria bacteria naturally liberate outer membrane “blebs,” which are presumed to contribute to pathology, and the detergent-extracted outer membrane vesicles (OMVs) from Neisseria meningitidis are currently employed as meningococcal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::471072bcb78315363cd26d666e9869e4
https://pubmed.ncbi.nlm.nih.gov/17620353

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Identification of Discrete Domains within Gonococcal Transferrin-Binding Protein A That Are Necessary for Ligand Binding and Iron Uptake Functions

Autor: Mary Kate Yost, Ian C. Boulton, James E. Anderson, Cynthia Nau Cornelissen

The availability of free iron in vivo is strictly limited, in part by the iron-binding protein transferrin. The pathogenicNeisseriaspp. can sequester iron from this protein, dependent upon two iron-repressible, transferrin-binding proteins (TbpA and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed444c1a2faafd5ee2f206fc029c803c
https://europepmc.org/articles/PMC97808/

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Antigenic and Sequence Diversity in Gonococcal Transferrin-Binding Protein A

Autor: Cynthia Nau Cornelissen, Ian C. Boulton, James E. Anderson, P F Sparling

Neisseria gonorrhoeaeis a gram-negative pathogen that is capable of satisfying its iron requirement with human iron-binding proteins such as transferrin and lactoferrin. Transferrin-iron utilization involves specific binding of human transferrin at t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1690e89d3f67dd7b504d8ac7946dd576
https://europepmc.org/articles/PMC98422/

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A dynamic model of the meningococcal transferrin receptor

Autor: Robert W. Evans, Andrew Gorringe, Ian C. Boulton, J.K Shergill, Christopher L. Joannou

Publikováno v: Journal of theoretical biology. 198(4)

Iron is an essential nutrient for all organisms and consequently, the ability to bind transferrin and sequester iron from his source constitutes a distinct advantage to a blood-borne bacterial pathogen. Levels of free iron are strictly limited in hum

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c896995208ff15e199e7ecb4dc07a1e5
https://pubmed.ncbi.nlm.nih.gov/10373350

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