Výsledky vyhledávání - "Baerbel S. Blaum"

Biophysical analysis of sialic acid recognition by the complement regulator Factor H

Autor: Thilo Stehle, Christoph Q. Schmidt, Agnes L. Hipgrave Ederveen, Baerbel S. Blaum, Markus J. Harder, Manfred Wuhrer

Publikováno v: Glycobiology, 28(10), 765-773

Complement factor H (FH), an elongated and substantially glycosylated 20-domain protein, is a soluble regulator of the complement alternative pathway (AP). It contains several glycan binding sites which mediate recognition of α2-3-linked sialic acid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::606b7b0e229f60a8231ed1538265201c
https://hdl.handle.net/1887/79225

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Spin ballet for sweet encounters : saturation-transfer difference NMR and X-ray crystallography complement each other in the elucidation of protein–glycan interactions

Autor: Baerbel S. Blaum, Ursula Neu, Thomas Peters, Thilo Stehle

Publikováno v: Acta Crystallographie Section F Structural Biology and Crystallization Communications
Acta Crystallographica. Section F, Structural Biology Communications

Proton-based saturation-transfer difference NMR (STD-NMR) is a technique that has proven to be particularly useful in the elucidation of protein–glycan interactions. This article explains the method for non-NMR spectroscopists and uses a number of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc77a609b124044636cae09a26ac4cae
https://hdl.handle.net/21.11116/0000-0001-ED72-421.11116/0000-0001-ED74-2

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Structural and Functional Characterization of the Product of Disease-Related Factor H Gene Conversion

Autor: Conny M. Johansson, Dušan Uhrín, Andrew P. Herbert, Paul N. Barlow, Jonathan P. Hannan, David J. Kavanagh, Baerbel S. Blaum, Hugh P. Morgan

Publikováno v: Biochemistry. 51:1874-1884

Numerous complement factor H (FH) mutations predispose patients to atypical hemolytic uremic syndrome (aHUS) and other disorders arising from inadequately regulated complement activation. No unifying structural or mechanistic consequences have been a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db0d57e7a7af5a70c4f556c6266ad1ef
https://doi.org/10.1021/bi201689j

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Preparation of heparin/heparan sulfate oligosaccharides with internal N-unsubstituted glucosamine residues for functional studies

Autor: John T. Gallagher, Jon A. Deakin, Malcolm Lyon, Wei Zheng, Baerbel S. Blaum, Dušan Uhrín

Publikováno v: Glycoconjugate Journal. 28:525-535

The rare N-unsubstituted glucosamine (GlcNH (3)(+)) residues in heparan sulfate (HS) have important biological and pathophysiological roles. However, it is difficult to prepare naturally-occuring, GlcNH(3)(+)-containing oligosaccharides from HS becau

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65b3dd57d354f0e90ad32ec0e705e207
https://doi.org/10.1007/s10719-011-9352-3

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Structural basis for sialic acid-mediated self-recognition by complement factor H

Autor: Baerbel S. Blaum, Dušan Uhrín, Andrew P. Herbert, Thilo Stehle, David J. Kavanagh, Jonathan P. Hannan

Publikováno v: Nature chemical biology. 11(1)

The serum protein complement factor H (FH) ensures downregulation of the complement alternative pathway, a branch of innate immunity, upon interaction with specific glycans on host cell surfaces. Using ligand-based NMR, we screened a comprehensive se

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d8053d399812ceebd78fcfe4eef2fe8
https://pubmed.ncbi.nlm.nih.gov/25402769

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Structures of Merkel cell polyomavirus VP1 complexes define a sialic acid binding site required for infection

Autor: Baerbel S. Blaum, Holger Hengel, Rachel M. Schowalter, Warren W. Wakarchuk, Makoto Kiso, Hiromune Ando, Christopher B. Buck, Ursula Neu, Dennis Macejak, Thomas Peters, Niklas Arnberg, Robert L. Garcea, Thilo Stehle, Akihiro Imamura, Michel Gilbert

Publikováno v: PLoS Pathogens
PLoS Pathogens, Vol 8, Iss 7, p e1002738 (2012)

The recently discovered human Merkel cell polyomavirus (MCPyV or MCV) causes the aggressive Merkel cell carcinoma (MCC) in the skin of immunocompromised individuals. Conflicting reports suggest that cellular glycans containing sialic acid (Neu5Ac) ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45f3bbe1ffa06e1730740c051fad9f09
https://pubmed.ncbi.nlm.nih.gov/22910713

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Structural basis for engagement by complement factor H of C3b on a self surface

Autor: Christoph Q. Schmidt, Hugh P. Morgan, Haydyn D. T. Mertens, Paul N. Barlow, Mara Guariento, Jonathan P. Hannan, Conny M. Johansson, Dmitri I. Svergun, Dominic Gillespie, David J. Kavanagh, Dušan Uhrín, Andrew P. Herbert, Baerbel S. Blaum

Publikováno v: Morgan, H P, Schmidt, C Q, Guariento, M, Blaum, B S, Gillespie, D, Herbert, A P, Kavanagh, D, Mertens, H D T, Svergun, D I, Johansson, C M, Uhrin, D, Barlow, P N & Hannan, J P 2011, ' Structural basis for engagement by complement factor H of C3b on a self surface ', Nature Structural & Molecular Biology, vol. 18, no. 4, pp. 463-470 . https://doi.org/10.1038/nsmb.2018
Nature structural & molecular biology

Complement factor H (FH) attenuates C3b molecules tethered via their thioester domains to selfsurfaces and thereby protects host tissues. FH is a cofactor for initial C3b proteolysis that ultimately yields a surface-attached fragment (C3d), correspon

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3399e91cbf5bb9e0712d8f8502479f7
https://www.pure.ed.ac.uk/ws/files/7508297/NSMB_2011_Barlow.pdf

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