Výsledky vyhledávání - "Huizinga, E.G."

Novel sequence variation affects GPIb α in post-diarrheal hemolytic uremic syndrome

Autor: Volokina, E., Jakobi, A.J., Urbanus, R.T, Huizinga, E.G., Sluiter, H., Middel, C., Westra, D., van Heerde, W.L., van de Kar, N., van den Heuvel, L.

Background: Hemolytic uremic syndrome (HUS) is one of the major causes of renal failure in children. In most cases the disease is caused by infection with Shiga toxin- producing Escherichia coli (STEC) and preceded by diarrhea. Only in 15% of cases S

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______101::0a5ca8a45f3ea3cf12d8046ade5cc0b9
https://dspace.library.uu.nl/handle/1874/308210

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Formation and Structure of a NAIP5-NLRC4 Inflammasome Induced by Direct Interactions with Conserved N- and C-terminal Regions of Flagellin

Autor: Halff, E.F., Diebolder, C.A., Versteeg, M., Schouten, A., Brondijk, T.H.C., Huizinga, E.G.

Publikováno v: Journal of Biological Chemistry, 287(46), 38460-38472

The NOD-like receptors NAIP5 and NLRC4 play an essential role in the innate immune response to the bacterial tail protein flagellin. Upon flagellin detection, NAIP5 and NLRC4 form a hetero-oligomeric inflammasome that induces caspase-1-dependent cell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::ac8dfd7debc7a68a9cff0c31fd9330d7
https://hdl.handle.net/1887/102749

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Implications for collagen I chain registry from the structure of the collagen von Willebrand factor A3 domain complex

Autor: Brondijk, T.H.C., Bihan, D., Farndale, R.W., Huizinga, E.G., Crystal and Structural Chemistry, Rontgen participation programme, Sub Crystal and Structural Chemistry

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 109(14), 5353. National Academy of Sciences

Fibrillar collagens, the most abundant proteins in the vertebrate body, are involved in a plethora of biological interactions. Plasma protein von Willebrand factor (VWF) mediates adhesion of blood platelets to fibrillar collagen types I, II, and III,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ab70cc7b66421490bc3f6a1949d6924
https://pubmed.ncbi.nlm.nih.gov/22440751

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The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture

Autor: Langereis, M.A., Zeng, Q., Heesters, B., Huizinga, E.G., de Groot, R.J., Rontgen participation programme, Strategic Infection Biology, Dep Infectieziekten Immunologie, Afd Chemical Biology and Drug Discovery, Sub Crystal and Structural Chemistry

Publikováno v: PLoS Pathogens, 8(1), 1. Public Library of Science
PLoS Pathogens, Vol 8, Iss 1, p e1002492 (2012)
PLoS Pathogens

The hemagglutinin-esterases (HEs), envelope glycoproteins of corona-, toro- and orthomyxoviruses, mediate reversible virion attachment to O-acetylated sialic acids (O-Ac-Sias). They do so through concerted action of distinct receptor-binding (“lect

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0a90ee5f054f5711d4b88c02f764c59
https://dspace.library.uu.nl/handle/1874/268163

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A rapid cloning method employing orthogonal end protection

Autor: Jakobi, A.J., Huizinga, E.G.

We describe a novel in vitro cloning strategy that combines standard tools in molecular biology with a basic protecting group concept to create a versatile framework for the rapid and seamless assembly of modular DNA building blocks into functional o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______101::032f12fa98e0a130bff37a71ee8b5feb
https://dspace.library.uu.nl/handle/1874/269798

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Calcium modulates force sensing by the von Willebrand factor A2 domain

Autor: Jakobi, A.J., Mashaghi, A., Tans, S.J., Huizinga, E.G., Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry

Publikováno v: Nature Communications [E], 2:385, 1. Nature Publishing Group
Nature Communications

von Willebrand factor (VWF) multimers mediate primary adhesion and aggregation of platelets. VWF potency critically depends on multimer size, which is regulated by a feedback mechanism involving shear-induced unfolding of the VWF-A2 domain and cleava

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64e8d4aded400f6bd6db221c1f08a80b
https://dspace.library.uu.nl/handle/1874/235176

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Erythrocytosis associated with a novel missense mutation in the HIF2A gene

Autor: van Wijk, R., Sutherland, S., van Wesel, A.C.W., Huizinga, E.G., Percy, M.J., Bierings, M.B., Lee, F.S., Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry

Publikováno v: Haematologica-The Hematology Journal, 95(5), 829. Ferrata Storti Foundation

The ERYTHROPOIETIN (EPO) gene is regulated by the transcription factor Hypoxia Inducible Factor- (HIF-). In this pathway, Prolyl Hydroxylase Domain protein 2 (PHD2) hydroxylates two prolyl residues in HIF-, which in turn promotes HIF- degradation by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::9c028003e63f9ef875a629882e4af67d
https://dspace.library.uu.nl/handle/1874/197057

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Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases

Autor: Langereis, M.A., Zeng, Q., Gerwig, G.J., Frey, B., von Itzstein, M., Kamerling, J.P., de Groot, R.J., Huizinga, E.G.

Hemagglutinin esterases (HEs), closely related envelope glycoproteins in influenza C and corona- and toroviruses, mediate reversible attachment to O-acetylated sialic acids (Sias). They do so by acting both as lectins and as receptor-destroying enzym

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______101::8260f07ac773005f389ae0ea8619aa83
https://dspace.library.uu.nl/handle/1874/39478

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