Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Zhihai Si"'
Autor:
Hillel Haim, Zhihai Si, Navid Madani, Liping Wang, Joel R Courter, Amy Princiotto, Aemro Kassa, Marciella DeGrace, Kathleen McGee-Estrada, Megan Mefford, Dana Gabuzda, Amos B Smith, Joseph Sodroski
Publikováno v:
PLoS Pathogens, Vol 5, Iss 4, p e1000360 (2009)
Binding to the CD4 receptor induces conformational changes in the human immunodeficiency virus (HIV-1) gp120 exterior envelope glycoprotein. These changes allow gp120 to bind the coreceptor, either CCR5 or CXCR4, and prime the gp41 transmembrane enve
Externí odkaz:
https://doaj.org/article/f69f3e72cbcb44488024e00cca5951a0
Autor:
Anna Zuk, Zhihai Si, Sally Loi, Santhosh Bommegowda, Debie Hoivik, Sanjay Danthi, Gyongyi Molnar, Vilmos Csizmadia, Michael Rabinowitz
Publikováno v:
Journal of Pharmacology and Experimental Therapeutics. 383:11-24
Pharmacological inhibition of prolyl-4-hydroxylase domain (PHD) enzymes stabilizes hypoxia-inducible factors (HIFs), transcription factors that activate target genes that, among others, increase erythropoietin (EPO) synthesis, resulting in the produc
Autor:
Haim, Hillel1, Zhihai Si1, Madani, Navid1, Liping Wang1, Courter, Joel R.2, Princiotto, Amy1, Kassa, Aemro1, DeGrace, Marciella1, McGee-Estrada, Kathleen1, Mefford, Megan1, Gabuzda, Dana1, Smith III, Amos B.2, Sodroski, Joseph1,3 josephsodroski@dfci.harvard.edu
Publikováno v:
PLoS Pathogens. Apr2009, Vol. 5 Issue 4, p1-13. 13p. 7 Graphs.
Publikováno v:
Journal of Biological Chemistry. 280:26933-26940
TRIM5alpha is a cytoplasmic protein that mediates a post-entry block to infection by some retroviruses. TRIM5alpha contains a tripartite motif (TRIM), which includes RING, B-box 2, and coiled-coil domains, and a C-terminal B30.2 (SPRY) domain. We inv
Autor:
Shi Hua Xiang, Michael Farzan, Eric S. Rosenberg, Joseph Sodroski, James E. Robinson, Navid Madani, Liping Wang, Zhihai Si
Publikováno v:
Journal of Virology. 79:6068-6077
Interaction of the human immunodeficiency virus type 1 (HIV-1) gp120 envelope glycoprotein with the primary receptor, CD4, promotes binding to a chemokine receptor, either CCR5 or CXCR4. The chemokine receptor-binding site on gp120 elicits CD4-induce
Publikováno v:
Journal of Virology. 78:5448-5457
The synthetic peptide T-20, which corresponds to a sequence within the C-terminal heptad repeat region (HR2) of the human immunodeficiency virus type 1 (HIV-1) gp41 envelope glycoprotein, potently inhibits viral membrane fusion and entry. Although T-
Autor:
Jason J. Chruma, Arne Schön, Liping Wang, Amos B. Smith, Joseph Sodroski, Jason M. Cox, Ernesto Freire, Navid Madani, Irwin Chaiken, Alyssa C. Biorn, Ngoc Phan, Simon Cocklin, Jeffrey C. Klein, Zhihai Si
Publikováno v:
Proceedings of the National Academy of Sciences. 101:5036-5041
When interacting with the CD4 receptor, the HIV gp120 envelope glycoprotein undergoes conformational changes that allow binding to the chemokine receptor. Receptor binding is proposed to lead to conformational changes in the gp41 transmembrane envelo
Autor:
Dennis R. Burton, Alyssa C. Biorn, Simon Cocklin, James M. Samanen, Joseph Sodroski, Navid Madani, Zhihai Si, Ernesto Freire, Donald Van Ryk, Tijana Ivanovic, Ralph Pantophlet, Irwin Chaiken
Publikováno v:
Biochemistry. 43:1928-1938
The linear peptide 12p1 (RINNIPWSEAMM) was previously isolated from a phage display library and was found to inhibit interaction of HIV-1 gp120 with both CD4 and a CCR5 surrogate, mAb 17b [Ferrer, M., and Harrison, S. (1999) J. Virol. 73, 5795-5802].
Publikováno v:
Journal of Virology. 75:4208-4218
The simian-human immunodeficiency virus SHIV-HXBc2 contains the envelope glycoproteins of a laboratory-adapted, neutralization-sensitive human immunodeficiency virus type 1 variant, HXBc2. Serial in vivo passage of the nonpathogenic SHIV-HXBc2 genera
Autor:
Navid Madani, Zhihai Si, Kathleen McGee-Estrada, Marciela M. DeGrace, Hillel Haim, Dana Gabuzda, Joseph Sodroski, Joel R. Courter, Amos B. Smith, Megan Mefford, Liping Wang, Aemro Kassa, Amy M. Princiotto
Publikováno v:
PLoS Pathogens, Vol 5, Iss 4, p e1000360 (2009)
PLoS Pathogens
PLoS Pathogens
Binding to the CD4 receptor induces conformational changes in the human immunodeficiency virus (HIV-1) gp120 exterior envelope glycoprotein. These changes allow gp120 to bind the coreceptor, either CCR5 or CXCR4, and prime the gp41 transmembrane enve