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Items: 1 to 20 of 91

1.

Targeting gC1qR domains for therapy against infection and inflammation.

Ghebrehiwet B, Jesty J, Vinayagasundaram R, Vinayagasundaram U, Ji Y, Valentino A, Tumma N, Hosszu KH, Peerschke EI.

Adv Exp Med Biol. 2013;735:97-110. Review.

PMID:
23402021
2.

gC1qR/p33 serves as a molecular bridge between the complement and contact activation systems and is an important catalyst in inflammation.

Ghebrehiwet B, CebadaMora C, Tantral L, Jesty J, Peerschke EI.

Adv Exp Med Biol. 2006;586:95-105.

PMID:
16893067
3.

Structure-function studies using deletion mutants identify domains of gC1qR/p33 as potential therapeutic targets for vascular permeability and inflammation.

Ghebrehiwet B, Jesty J, Xu S, Vinayagasundaram R, Vinayagasundaram U, Ji Y, Valentino A, Hosszu KK, Mathew S, Joseph K, Kaplan AP, Peerschke EI.

Front Immunol. 2011 Nov 1;2. pii: 58.

4.

Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore).

Pixley RA, Espinola RG, Ghebrehiwet B, Joseph K, Kao A, Bdeir K, Cines DB, Colman RW.

Thromb Haemost. 2011 Jun;105(6):1053-9. doi: 10.1160/TH10-09-0591. Epub 2011 May 5.

5.

The contribution of gC1qR/p33 in infection and inflammation.

Peerschke EI, Ghebrehiwet B.

Immunobiology. 2007;212(4-5):333-42. Epub 2007 Jan 3.

6.

The plasma bradykinin-forming pathways and its interrelationships with complement.

Kaplan AP, Ghebrehiwet B.

Mol Immunol. 2010 Aug;47(13):2161-9. doi: 10.1016/j.molimm.2010.05.010. Review.

PMID:
20580091
7.

Pathogenic mechanisms of bradykinin mediated diseases: dysregulation of an innate inflammatory pathway.

Kaplan AP, Joseph K.

Adv Immunol. 2014;121:41-89. doi: 10.1016/B978-0-12-800100-4.00002-7. Review.

PMID:
24388213
8.

The multiligand-binding protein gC1qR, putative C1q receptor, is a mitochondrial protein.

Dedio J, Jahnen-Dechent W, Bachmann M, Müller-Esterl W.

J Immunol. 1998 Apr 1;160(7):3534-42.

9.

Cytokeratin 1 and gC1qR mediate high molecular weight kininogen binding to endothelial cells.

Joseph K, Ghebrehiwet B, Kaplan AP.

Clin Immunol. 1999 Sep;92(3):246-55.

PMID:
10479529
10.

Formation of bradykinin: a major contributor to the innate inflammatory response.

Joseph K, Kaplan AP.

Adv Immunol. 2005;86:159-208. Review.

PMID:
15705422
11.

gC1q-R/p33, a member of a new class of multifunctional and multicompartmental cellular proteins, is involved in inflammation and infection.

Ghebrehiwet B, Lim BL, Kumar R, Feng X, Peerschke EI.

Immunol Rev. 2001 Apr;180:65-77. Review.

PMID:
11414365
12.

The binding protein for globular heads of complement C1q, gC1qR. Functional expression and characterization as a novel vitronectin binding factor.

Lim BL, Reid KB, Ghebrehiwet B, Peerschke EI, Leigh LA, Preissner KT.

J Biol Chem. 1996 Oct 25;271(43):26739-44.

13.

Expression and colocalization of cytokeratin 1 and urokinase plasminogen activator receptor on endothelial cells.

Mahdi F, Shariat-Madar Z, Todd RF 3rd, Figueroa CD, Schmaier AH.

Blood. 2001 Apr 15;97(8):2342-50.

14.
15.

Interaction of high molecular weight kininogen binding proteins on endothelial cells.

Joseph K, Tholanikunnel BG, Ghebrehiwet B, Kaplan AP.

Thromb Haemost. 2004 Jan;91(1):61-70.

PMID:
14691569
16.

Interaction of factor XII and high molecular weight kininogen with cytokeratin 1 and gC1qR of vascular endothelial cells and with aggregated Abeta protein of Alzheimer's disease.

Joseph K, Shibayama Y, Nakazawa Y, Peerschke EI, Ghebrehiwet B, Kaplan AP.

Immunopharmacology. 1999 Sep;43(2-3):203-10. Review.

PMID:
10596854
17.

Isolation and characterization of the kininogen-binding protein p33 from endothelial cells. Identity with the gC1q receptor.

Herwald H, Dedio J, Kellner R, Loos M, Müller-Esterl W.

J Biol Chem. 1996 May 31;271(22):13040-7.

18.

Human umbilical vein endothelial cells possess binding sites for the globular domain of C1q.

Peerschke EI, Smyth SS, Teng EI, Dalzell M, Ghebrehiwet B.

J Immunol. 1996 Nov 1;157(9):4154-8.

PMID:
8892652
19.

Soluble gC1qR is an autocrine signal that induces B1R expression on endothelial cells.

Ghebrehiwet B, Ji Y, Valentino A, Pednekar L, Ramadass M, Habiel D, Kew RR, Hosszu KH, Galanakis DK, Kishore U, Peerschke EI.

J Immunol. 2014 Jan 1;192(1):377-84. doi: 10.4049/jimmunol.1302031. Epub 2013 Dec 6.

20.

Subcellular targeting of multiligand-binding protein gC1qR.

Dedio J, Renné T, Weisser M, Müller-Esterl W.

Immunopharmacology. 1999 Dec;45(1-3):1-5.

PMID:
10614982

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