1-7 of 7
M B Feinstein
Close
Save search
Follow your search
Access your saved searches in your account
Would you like to receive an alert when new items match your search?
Close Modal
Sort by
Articles

Purification and characterization of the human type 1 Ins(1,4,5) P 3 receptor from platelets and comparison with receptor subtypes in other normal and transformed blood cells

Available to Purchase
F O'Rourke, E Matthews, M B Feinstein
Journal: Biochemical Journal
Biochem J (1995) 312 (2): 499–503.
https://doi.org/10.1042/bj3120499
Published: 01 December 1995
View articletitled, Purification and characterization of the human type 1 Ins(1,4,5) P 3 receptor from platelets and comparison with receptor subtypes in other normal and transformed blood cells
Open the PDF for Purification and characterization of the human type 1 Ins(1,4,5) P 3 receptor from platelets and comparison with receptor subtypes in other normal and transformed blood cells in another window
Articles

Thrombin-receptor agonist peptides, in contrast to thrombin itself, are not full agonists for activation and signal transduction in human platelets in the absence of platelet-derived secondary mediators

Available to Purchase
L F Lau, K Pumiglia, Y P Côté, M B Feinstein
Journal: Biochemical Journal
Biochem J (1994) 303 (2): 391–400.
https://doi.org/10.1042/bj3030391
Published: 15 October 1994
View articletitled, Thrombin-receptor agonist peptides, in contrast to thrombin itself, are not full agonists for activation and signal transduction in human platelets in the absence of platelet-derived secondary mediators
Open the PDF for Thrombin-receptor agonist peptides, in contrast to thrombin itself, are not full agonists for activation and signal transduction in human platelets in the absence of platelet-derived secondary mediators in another window
Articles

Ca 2+ release by inositol 1,4,5-trisphosphate is blocked by the K + -channel blockers apamin and tetrapentylammonium ion, and a monoclonal antibody to a 63 kDa membrane protein: reversal of blockade by K + ionophores nigericin and valinomycin and purification of the 63 kDa antibody-binding protein

Available to Purchase
F O'Rourke, K Soons, R Flaumenhauft, J Watras, C Baio-Larue, E Matthews, M B Feinstein
Journal: Biochemical Journal
Biochem J (1994) 300 (3): 673–683.
https://doi.org/10.1042/bj3000673
Published: 15 June 1994
View articletitled, Ca 2+ release by inositol 1,4,5-trisphosphate is blocked by the K + -channel blockers apamin and tetrapentylammonium ion, and a monoclonal antibody to a 63 kDa membrane protein: reversal of blockade by K + ionophores nigericin and valinomycin and purification of the 63 kDa antibody-binding protein
Open the PDF for Ca 2+ release by inositol 1,4,5-trisphosphate is blocked by the K + -channel blockers apamin and tetrapentylammonium ion, and a monoclonal antibody to a 63 kDa membrane protein: reversal of blockade by K + ionophores nigericin and valinomycin and purification of the 63 kDa antibody-binding protein in another window
Articles

Thrombin and thrombin receptor agonist peptide induce tyrosine phosphorylation and tyrosine kinases in the platelet cytoskeleton. Translocation of pp60 c - src and integrin α IIb β 3 (glycoprotein IIb/IIIa) is not required for aggregation, but is dependent on formation of large aggregate structures

Available to Purchase
K M Pumiglia, M B Feinstein
Journal: Biochemical Journal
Biochem J (1993) 294 (1): 253–260.
https://doi.org/10.1042/bj2940253
Published: 15 August 1993
View articletitled, Thrombin and thrombin receptor agonist peptide induce tyrosine phosphorylation and tyrosine kinases in the platelet cytoskeleton. Translocation of pp60 c - src and integrin α IIb β 3 (glycoprotein IIb/IIIa) is not required for aggregation, but is dependent on formation of large aggregate structures
Open the PDF for Thrombin and thrombin receptor agonist peptide induce tyrosine phosphorylation and tyrosine kinases in the platelet cytoskeleton. Translocation of pp60 c - src and integrin α IIb β 3 (glycoprotein IIb/IIIa) is not required for aggregation, but is dependent on formation of large aggregate structures in another window
Articles

Activation of signal transduction in platelets by the tyrosine phosphatase inhibitor pervanadate (vanadyl hydroperoxide)

Available to Purchase
K M Pumiglia, L F Lau, C K Huang, S Burroughs, M B Feinstein
Journal: Biochemical Journal
Biochem J (1992) 286 (2): 441–449.
https://doi.org/10.1042/bj2860441
Published: 01 September 1992
View articletitled, Activation of signal transduction in platelets by the tyrosine phosphatase inhibitor pervanadate (vanadyl hydroperoxide)
Open the PDF for Activation of signal transduction in platelets by the tyrosine phosphatase inhibitor pervanadate (vanadyl hydroperoxide) in another window
Articles

The inositol 1,4,5-trisphosphate receptor binding sites of platelet membranes. pH-dependency, inhibition by polymeric sulphates, and the possible presence of arginine at the binding site

Available to Purchase
F O'Rourke, M B Feinstein
Journal: Biochemical Journal
Biochem J (1990) 267 (2): 297–302.
https://doi.org/10.1042/bj2670297
Published: 15 April 1990
View articletitled, The inositol 1,4,5-trisphosphate receptor binding sites of platelet membranes. pH-dependency, inhibition by polymeric sulphates, and the possible presence of arginine at the binding site
Open the PDF for The inositol 1,4,5-trisphosphate receptor binding sites of platelet membranes. pH-dependency, inhibition by polymeric sulphates, and the possible presence of arginine at the binding site in another window
Articles

Release of Ca 2+ by inositol 1,4,5-trisphosphate in platelet membrane vesicles is not dependent on cyclic AMP-dependent protein kinase

Available to Purchase
F O'Rourke, G B Zavoico, M B Feinstein
Journal: Biochemical Journal
Biochem J (1989) 257 (3): 715–721.
https://doi.org/10.1042/bj2570715
Published: 01 February 1989
View articletitled, Release of Ca 2+ by inositol 1,4,5-trisphosphate in platelet membrane vesicles is not dependent on cyclic AMP-dependent protein kinase
Open the PDF for Release of Ca 2+ by inositol 1,4,5-trisphosphate in platelet membrane vesicles is not dependent on cyclic AMP-dependent protein kinase in another window