S. C. Bock

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Cloning and expression of the cDNA for human antithrombin mI

R. Lawn, K. Wion, G. Vehar, 2022 .

Pleiotropic effects of antithrombin strand 1C substitution mutations.

M. Hultin, M. Boisclair, D. Lane, 1992, The Journal of clinical investigation.

Molecular genetic survey of 16 kindreds with hereditary antithrombin III deficiency.

E. Prochownik, S. C. Bock, SC Bock, 1987, Blood.

Structure and Evolution of the Human Antithrombin III Gene

E. Prochownik, S. C. Bock, 1985 .

Cloning and expression of the cDNA for human antithrom, bin III

R. Lawn, G. Vehar, S. C. Bock, 1982 .

The role of Arg46 and Arg47 of antithrombin in heparin binding.

I. Björk, V. Arocas, S. C. Bock, 1999, Biochemistry.

Lysine 114 of Antithrombin Is of Crucial Importance for the Affinity and Kinetics of Heparin Pentasaccharide Binding*

S. Olson, I. Björk, S. Raja, 2001, The Journal of Biological Chemistry.

Elimination of P1 Arginine 393 Interaction with Underlying Glutamic Acid 255 Partially Activates Antithrombin III for Thrombin Inhibition but Not Factor Xa Inhibition*

A. Lu, M. A. Jairajpuri, S. C. Bock, 2002, The Journal of Biological Chemistry.

Molecular Genetics of Human Antithrombin Iii Deficiencies

E. Prochownik, J. Marrinan, S. C. Bock, 1985 .

The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change.

S. Olson, I. Björk, S. C. Bock, 1997, Biochemistry.

Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells.

I. Björk, E. Ersdal-Badju, A. Lu, 1995, The Biochemical journal.

Two-dimensional electrophoresis of small-molecular-weight proteins.

M. Goldsmith, S. C. Bock, M. Koehler, 1979, Analytical biochemistry.

Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site [Erratum to document cited in CA109(9):69344b]

J. Marrinan, E. Radziejewska, S. C. Bock, 1989 .

Examining the interactions of Galahad™ compound with viruses to develop a novel inactivated influenza A virus vaccine

P. Azadi, D. Belnap, D. Barnard, 2022, Heliyon.

CpG mutations in the reactive site of human C1 inhibitor.

K. Skriver, E. Radziejewska, S. C. Bock, 1989, The Journal of biological chemistry.

Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States*♦

S. Olson, P. Gettins, R. Swanson, 2015, The Journal of Biological Chemistry.

Importance of lysine 125 for heparin binding and activation of antithrombin.

U. Desai, S. Olson, P. Gettins, 2002, Biochemistry.

The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase specificity but normal heparin activation.

S. Olson, Y. Chuang, R. Swanson, 2001, Biochemistry.

The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139.

I. Björk, V. Arocas, S. C. Bock, 2000, Biochemistry.

Antithrombin III Phenylalanines 122 and 121 Contribute to Its High Affinity for Heparin and Its Conformational Activation*

U. Desai, S. Olson, A. Lu, 2003, The Journal of Biological Chemistry.

Role of Arginine 129 in Heparin Binding and Activation of Antithrombin*

U. Desai, S. Olson, I. Björk, 2000, The Journal of Biological Chemistry.

Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding.

S. Olson, I. Björk, Sophia Schedin‐Weiss, 2002, Biochemistry.

Thrombin-Antithrombin System

S. Bock, S. C. Bock, 2016 .

Identification of the Antithrombin III Heparin Binding Site*

Y. Zuo, S. Bock, V. Picard, 1997, The Journal of Biological Chemistry.

Protein inhibitors of crystal growth.

E. Kaiser, S. C. Bock, 1989, The Journal of urology.

Modification of the active site of alkaline phosphatase by site-directed mutagenesis.

S. Rokita, E. Kaiser, S. C. Bock, 1986, Science.

Antithrombin III Genetics, Structure and Function

S. Bock, S. C. Bock, 1991 .

The sequence of human serum albumin cDNA and its expression in E. coli.

P. Seeburg, J. Adelman, R. Lawn, 1981, Nucleic acids research.

A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase

Véronique Picard, Eva Ersdal-Badju, Aiqin Lu, 1994, Nucleic Acids Res..

Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide

Susan Clark Bock, Debra A. Kendall, E. Kaiser, 1986, Nature.

Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site.

J. Marrinan, E. Radziejewska, S. C. Bock, 1988, Biochemistry.

Intron structure of the human antithrombin III gene differs from that of other members of the serine protease inhibitor superfamily.

S. Orkin, E. Prochownik, S. C. Bock, 1985, The Journal of biological chemistry.

Characterization of an unusual DNA length polymorphism 5' to the human antithrombin III gene.

D. Levitan, S. C. Bock, 1983, Nucleic acids research.

Human apolipoprotein B cDNA clone isolation and demonstration that liver apolipoprotein B mRNA is 22 kilobases in length.

J. Breslow, L. Huang, J L Breslow, 1985, Proceedings of the National Academy of Sciences of the United States of America.

C1 INHIBITOR: STRUCTURE, GENETIC VARIANTS AND SERPIN HOMOLOGIES

K. Skriver, S. Bock, S. Magnusson, 1991 .

Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization.

R. Huber, E. Nielsen, R. Eddy, 1986, Biochemistry.

Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity.

S. Bock, V. Picard, E. Ersdal-Badju, 1995, Biochemistry.

Antithrombin Budapest 3 An antithrombin variant with reduced heparin affinity resulting from the substitution L99F

M. Boisclair, D. Lane, S. Thein, 1992, FEBS letters.

Substrate properties of C1 inhibitor Ma (alanine 434----glutamic acid). Genetic and structural evidence suggesting that the P12-region contains critical determinants of serine protease inhibitor/substrate status.

W. R. Wikoff, K. Skriver, A. Kaplan, 1991, The Journal of biological chemistry.

Identification of critical molecular interactions mediating heparin activation of antithrombin: implications for the design of improved heparin anticoagulants.

S. Olson, S. Bock, I. Björk, 2002, Trends in cardiovascular medicine.

Specific protein synthesis in cellular differentiation. VI: Temporal expression of chorion gene families in Bombyx mori strain C108

M. Goldsmith, S. C. Bock, K. Campo, 1986 .

Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change.

U. Desai, S. Olson, I. Björk, 2004, Biochemistry.

Cloning and expression of the cDNA for human antithrombin III.

R. Lawn, K. Wion, G. Vehar, 1982, Nucleic acids research.

Differential patterns in the temporal experession ofBombyx mori chorion genes

M. Goldsmith, D. Tiemeier, S. C. Bock, 1983, Wilhelm Roux's archives of developmental biology.

A NheI RFLP in the human antithrombin III gene (1q23-q25) (AT3).

E. Radziejewska, S. C. Bock, 1991, Nucleic acids research.

Assignment of the human antithrombin III structural gene to chromosome 1q23-25.

I. Balazs, J. Trent, S. C. Bock, 1985, Cytogenetics and cell genetics.

Disruption of a Tight Cluster Surrounding Tyrosine 131 in the Native Conformation of Antithrombin III Activates It for Factor Xa Inhibition*

M. A. Jairajpuri, S. C. Bock, R. D. Cruz, 2006, Journal of Biological Chemistry.