M. Griffith

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Treatment of Hemophilia A with a Highly Purified Factor VIII Concentrate Prepared by Anti-FVIIIc Immunoaffinity Chromatography

H. Kingdon, E. Gomperts, J. Addiego, 1992, Thrombosis and Haemostasis.

Identification of the molecular defect in factor IX Chapel Hill: substitution of histidine for arginine at position 145.

M. Griffith, C. Noyes, H. Roberts, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Structural evidence for leucine at the reactive site of heparin cofactor II.

M. Griffith, C. Noyes, F. Church, 1985, Biochemistry.

Cleavage and activation of human prothrombin by Echis carinatus venom.

M. Griffith, E. Briet, C. Noyes, 1982, Thrombosis Research.

Reactive site peptide structural similarity between heparin cofactor II and antithrombin III.

M. Griffith, C. Noyes, F. Church, 1985, The Journal of biological chemistry.

Kinetics of the heparin-enhanced antithrombin III/thrombin reaction. Evidence for a template model for the mechanism of action of heparin.

M. Griffith, 1982, The Journal of biological chemistry.

Measurement of human factor IXa activity in an isolated factor X activation system.

M. Griffith, H. Roberts, R. Lundblad, 1982, Thrombosis research.

Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin.

M. Griffith, M. Speight, Michael J. Griffith, 1983, Archives of biochemistry and biophysics.

The heparin-enhanced antithrombin III/thrombin reaction is saturable with respect to both thrombin and antithrombin III.

M. Griffith, 1982, The Journal of biological chemistry.

Structure-function relationships in heparin cofactor II: chemical modification of arginine and tryptophan and demonstration of a two-domain structure.

M. Griffith, F. Church, G. Villanueva, 1986, Archives of biochemistry and biophysics.

Comparison of lipid binding and kinetic properties of normal, variant, and gamma-carboxyglutamic acid modified human factor IX and factor IXa.

B. Lentz, M. Griffith, D. Monroe, 1985, Biochemistry.

Evidence for essential lysines in heparin cofactor II.

M. Griffith, F. Church, 1984, Biochemical and biophysical research communications.

Dermatan sulfate and heparin can be fractionated by affinity for heparin cofactor II.

M. Griffith, G. Marbet, 1983, Biochemical and biophysical research communications.

Measurement of the heparin enhanced-antithrombin III/thrombin reaction rate in the presence of synthetic substrate.

M. Griffith, 1982, Thrombosis research.

Dissociation of antithrombin III--thrombin complex. Formation of active and inactive antithrombin III.

M. Griffith, R. Lundblad, 1981, Biochemistry.

Acceleration by calcium of the inactivation of thrombin by plasma proteinase inhibitors.

J. C. Roberts, M. Griffith, R. Lundblad, 1981, Thrombosis research.

Effect of monovalent cations on the heparin-enhanced antithrombin III/thrombin reaction.

H. Kingdon, M. Griffith, R. Lundblad, 1980, Thrombosis research.

Inhibition of the heparin-antithrombin III/thrombin reaction by active site blocked-thrombin.

H. Kingdon, M. Griffith, R. Lundblad, 1979, Biochemical and biophysical research communications.

Fractionation of heparin by affinity chromatography on covalently-bound human α-thrombin☆

H. Kingdon, M. Griffith, R. Lundblad, 1978 .

The liver as a site for interferon production in response to poly I:poly C.

M. Griffith, W. E. Magee, 1972, Life sciences. Pt. 2: Biochemistry, general and molecular biology.

Heparin cofactor activities in a family with hereditary antithrombin III deficiency: evidence for a second heparin cofactor in human plasma.

G. White, M. Griffith, F. Dombrose, 1983, Blood.

Characterization of the defect in activation of factor IX Chapel Hill by human factor XIa.

M. Griffith, C. Noyes, R. Lundblad, 1981, Journal of Clinical Investigation.

Regulation of factor IXa in vitro in human and mouse plasma and in vivo in the mouse. Role of the endothelium and the plasma proteinase inhibitors.

M. Griffith, H. Roberts, H. Fuchs, 1983, The Journal of clinical investigation.

N-GLYCAN SIALYLATION IS IMPORTANT FOR IN VIVO RECOVERY OF RECOMBINANT FACTOR IX

A. Kumar, S. Waugh, M. Griffith, 2007 .

PREPARATION OF HIGH SPECIFIC ACTIVITY PLASMA AHF BY ANTI-FVIIIc IMMUNOAFFINITY CHROMATOGRAPHY

Ing Ren Tsang, G. Neslund, M. Griffith, 1987 .

In-process controls and characterization of recombinate antihemophilic factor (recombinant)

H. Kingdon, S. L. Liu, M. Griffith, 1991, Annals of Hematology.

Kinetic analysis of the heparin-enhanced antithrombin III/thrombin reaction. Reaction rate enhancement by heparin-thrombin association.

M. Griffith, 1979, The Journal of biological chemistry.

Affinity labeling of the active site of Escherichia coli glutamine synthetase by 5'-p-fluorosulfonylbenzoyladenosine.

H. Kingdon, M. Griffith, W. Foster, 1981, Journal of Biological Chemistry.

Structural and enzymatic properties of Escherichia coli glutamine synthetase subjected to limited proteolysis.

H. Kingdon, M. Griffith, C. Noyes, 1985, Current topics in cellular regulation.

Interaction of substrates with glutamine synthetase after limited proteolysis.

H. Kingdon, M. Griffith, C. Noyes, 1984, Biochemistry.

Covalent modification of human alpha-thrombin with pyridoxal 5'-phosphate. Effect of phosphopyridoxylation on the interaction of thrombin with heparin.

M. Griffith, 1979, The Journal of biological chemistry.

Chapter 9A Inhibitors: antithrombin III and heparin

M. Griffith, 1986 .

Inhibition of chymotrypsin by heparin cofactor II.

M. Griffith, C. Noyes, F. Church, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Enzymatic inactivation of heparin cofactor II by a proteinase (proteinase-1) isolated from Echis carinatus venom.

M. Griffith, C. Noyes, F. Church, 1985, Thrombosis research.

The interaction of heparin with human alpha-thrombin: effect on the hydrolysis of anilide tripeptide substrates.

H. Kingdon, M. Griffith, R. Lundblad, 1979, Archives of biochemistry and biophysics.

Activation of normal and abnormal human factor IX with trypsin.

M. Griffith, D. Monroe, C. Noyes, 1985, Archives of biochemistry and biophysics.

Ultrapure plasma factor VIII produced by anti-FVIIIc immunoaffinity chromatography and solvent/detergent viral inactivation. Characterization of the Method M process and Hemofil M antihemophilic factor (human)

M. Griffith, 1991, Annals of Hematology.

Structure-function relations in platelet-thrombin reactions. Inhibition of platelet-thrombin interactions by lysine modification.

G. White, M. Griffith, R. Lundblad, 1981, The Journal of biological chemistry.

Treatment of Hemophilia A with a Highly Purified Factor Vlll Goncentrate

H. Kingdon, E. Gomperts, S. Courter, 2018 .

Acetate kinase from Veillonella alcalescens. Regulation by succinate and substrates.

M. Griffith, J. Nishimura, 1979, Journal of Biological Chemistry.

[37] Acetate kinase from Veillonella alcalescens: EC 2.7.2.1 ATP:acetate phosphotransferase

M. Griffith, J. Nishimura, 1981 .

Megakaryocyte-targeted synthesis of the integrin beta(3)-subunit results in the phenotypic correction of Glanzmann thrombasthenia.

J. Olsen, P. Bray, W. Bell, 2000, Blood.

Characterization of the clotting activities of structurally different forms of activated factor IX. Enzymatic properties of normal human factor IXa alpha, factor IXa beta, and activated factor IX Chapel Hill.

M. Griffith, E. Briet, C. Noyes, 1985, The Journal of clinical investigation.

Effects of nerve growth factor from the venon of Vipera russelli on sensory and sympathetic ganglia from the embryonic chick in culture.

M. Griffith, C. A. Vernon, M. Lamont, 1974, Journal of embryology and experimental morphology.

Characterization of the Clotting Activities of Structurally Different Forms of Activated Factor IX Enzymatic Properties of Normal Human Factor IXaae, Factor lXaB, and Activated Factor lXChapol Hill

M. Griffith, E. Briet, C. Noyes, 2022 .

Tissue Thromboplastin Induced Reversible DIC and Heparin-Enhanced Inhibitors in Dogs

M. Griffith, G. Marbet, 1986, Thrombosis and Haemostasis.

Structural and functional characteristics of activated human factor IX after chemical modification of gamma-carboxyglutamic acid residues.

R. Hiskey, M. Griffith, C. Noyes, 1985, The Journal of biological chemistry.