Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways

Yohannes T. Ghebremariam; Odutayo O. Odunuga; Kristen Janse; Girish J. Kotwal

doi:10.1196/annals.1352.024

Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways

Yohannes T. Ghebremariam
, Odutayo O. Odunuga
, Kristen Janse
, Girish J. Kotwal

Producción científica: Article › revisión exhaustiva

Idioma original	English
Páginas (desde-hasta)	113-122
Número de páginas	10
Publicación	Annals of the New York Academy of Sciences
Volumen	1056
DOI	https://doi.org/10.1196/annals.1352.024
Estado	Published - 2005
Publicado de forma externa	Sí

ASJC Scopus Subject Areas

General Neuroscience
General Biochemistry,Genetics and Molecular Biology
History and Philosophy of Science

Acceder al documento

10.1196/annals.1352.024

Otros archivos y enlaces

Citar esto

Ghebremariam, Y. T., Odunuga, O. O., Janse, K., & Kotwal, G. J. (2005). Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways. Annals of the New York Academy of Sciences, 1056, 113-122. https://doi.org/10.1196/annals.1352.024

Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways. / Ghebremariam, Yohannes T.; Odunuga, Odutayo O.; Janse, Kristen et al.
En: Annals of the New York Academy of Sciences, Vol. 1056, 2005, p. 113-122.

Producción científica: Article › revisión exhaustiva

Ghebremariam, YT, Odunuga, OO, Janse, K & Kotwal, GJ 2005, 'Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways', Annals of the New York Academy of Sciences, vol. 1056, pp. 113-122. https://doi.org/10.1196/annals.1352.024

Ghebremariam YT, Odunuga OO, Janse K, Kotwal GJ. Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways. Annals of the New York Academy of Sciences. 2005;1056:113-122. doi: 10.1196/annals.1352.024

Ghebremariam, Yohannes T. ; Odunuga, Odutayo O. ; Janse, Kristen et al. / Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways. En: Annals of the New York Academy of Sciences. 2005 ; Vol. 1056. pp. 113-122.

@article{1f0bfc370ec14bdd9a95683c3b6b3d7b,

title = "Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways",

keywords = "100-Fold potency, Complement, Heparin, Humanized rVCPs, Site-directed mutagenesis, rVCP",

author = "Ghebremariam, \{Yohannes T.\} and Odunuga, \{Odutayo O.\} and Kristen Janse and Kotwal, \{Girish J.\}",

year = "2005",

doi = "10.1196/annals.1352.024",

language = "English",

volume = "1056",

pages = "113--122",

}

TY - JOUR

T1 - Humanized recombinant vaccinia virus complement control protein (hrVCP) with three amino acid changes, H98Y, E102K, and E120K creating an additional putative heparin binding site, is 100-fold more active than rVCP in blocking both classical and alternative complement pathways

AU - Ghebremariam, Yohannes T.

AU - Odunuga, Odutayo O.

AU - Janse, Kristen

AU - Kotwal, Girish J.

PY - 2005

Y1 - 2005

KW - 100-Fold potency

KW - Complement

KW - Heparin

KW - Humanized rVCPs

KW - Site-directed mutagenesis

KW - rVCP

UR - https://www.scopus.com/pages/publications/29744456997

UR - https://www.scopus.com/pages/publications/29744456997#tab=citedBy

U2 - 10.1196/annals.1352.024

DO - 10.1196/annals.1352.024

M3 - Article

C2 - 16387681

AN - SCOPUS:29744456997

SN - 0077-8923

VL - 1056

SP - 113

EP - 122

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

ER -