Characterization of a solubilized cell surface binding protein on macrophages specific for proteins modified nonenzymatically by advanced glycosylated end products

1988 ◽  
Vol 263 (2) ◽  
pp. 418-423 ◽  
Author(s):  
Steven Radoff ◽  
Helen Vlassara ◽  
Anthony Cerami
Keyword(s):  
Cell Surface ◽  
Binding Protein ◽  
Surface Binding ◽  
Cell Surface Binding ◽  
End Products

scholarly journals Characterization of cell surface binding protein for the infection of marine birnavirus

2002 ◽  
Vol 68 (sup2) ◽  
pp. 1245-1246
Author(s):  
MASAYUKI IMAJOH ◽  
KENJI KAWAI ◽  
SHUN-ICHIROU OSHIMA
Keyword(s):  
Cell Surface ◽  
Binding Protein ◽  
Surface Binding ◽  
Cell Surface Binding ◽  
Marine Birnavirus

scholarly journals Identification of a novel cell attachment domain in the HIV-1 Tat protein and its 90-kDa cell surface binding protein.

1993 ◽  
Vol 268 (7) ◽  
pp. 5279-5284
Author(s):  
B.S. Weeks ◽  
K. Desai ◽  
P.M. Loewenstein ◽  
M.E. Klotman ◽  
P.E. Klotman ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Attachment ◽  
Binding Protein ◽  
Tat Protein ◽  
Surface Binding ◽  
Cell Surface Binding ◽  
Hiv 1

scholarly journals Reconstitution of carbonic anhydrase activity of the cell-surface-binding protein of vaccinia virus

2007 ◽  
Vol 407 (1) ◽  
pp. 61-67 ◽  
Author(s):  
Anna Ohradanova ◽  
Daniela Vullo ◽  
Juraj Kopacek ◽  
Claudia Temperini ◽  
Tatiana Betakova ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cell Surface ◽  
Vaccinia Virus ◽  
Double Mutant ◽  
Binding Protein ◽  
Viral Gene ◽  
Wild Type ◽  
Surface Binding ◽  
Histidine Residues ◽  
Cell Surface Binding

The N-terminal region of a 32 kDa cell-surface-binding protein, encoded by the D8L gene of vaccinia virus, shows sequence homology to CAs (carbonic anhydrases; EC 4.2.1.1). The active CAs catalyse the reversible hydration of CO2 to bicarbonate participating in many physiological processes. The CA-like domain of vaccinia protein [vaccCA (vaccinia virus CA-like protein)] contains one of the three conserved histidine residues required for co-ordination to the catalytic zinc ion and for enzyme activity. In the present study, we report the engineering of catalytically active vaccCA mutants by introduction of the missing histidine residues into the wild-type protein. The wild-type vaccCA was inactive as a catalyst and does not bind sulfonamide CA inhibitors. Its position on a phylogram with other hCAs (human CAs) shows a relationship with the acatalytic isoforms CA X and XI, suggesting that the corresponding viral gene was acquired from the human genome by horizontal gene transfer. The single mutants (vaccCA N92H/Y69H) showed low enzyme activity and low affinity for acetazolamide, a classical sulfonamide CA inhibitor. The activity of the double mutant, vaccCA N92H/Y69H, was much higher, of the same order of magnitude as that of some human isoforms, namely CA VA and CA XII. Moreover, its affinity for acetazolamide was high, comparable with that of the most efficient human isoenzyme, CA II (in the low nanomolar range). Multiplication of vaccinia virus in HeLa cells transfected with the vaccCA N92H/Y69H double mutant was approx. 2-fold more efficient than in wild-type vaccCA transfectants, suggesting that the reconstitution of the enzyme activity improved the virus life cycle.

scholarly journals Identification of a Cell Surface-binding Protein for the Core Protein of the Basement Membrane Proteoglycan

1989 ◽  
Vol 264 (21) ◽  
pp. 12467-12471
Author(s):  
B Clément ◽  
B Segui-Real ◽  
J R Hassell ◽  
G R Martin ◽  
Y Yamada
Keyword(s):  
Basement Membrane ◽  
Cell Surface ◽  
Core Protein ◽  
Binding Protein ◽  
Surface Binding ◽  
The Core ◽  
Cell Surface Binding ◽  
A Cell

scholarly journals Cell surface-binding sites for progesterone mediate calcium uptake in human sperm.

1991 ◽  
Vol 266 (28) ◽  
pp. 18655-18659 ◽  
Author(s):  
P.F. Blackmore ◽  
J. Neulen ◽  
F. Lattanzio ◽  
S.J. Beebe
Keyword(s):  
Cell Surface ◽  
Binding Sites ◽  
Calcium Uptake ◽  
Human Sperm ◽  
Surface Binding ◽  
Cell Surface Binding
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