D. Meininger

发表

Distinctive molecular inhibition mechanisms for selective inhibitors of human 11beta-hydroxysteroid dehydrogenase type 1.

N. Walker, Hiroshi Yamamoto, Zhulun Wang, 2008, Bioorganic & medicinal chemistry.

Generation of protease-deficient strains and their use in heterologous protein expression.

E. Komives, D. Meininger, M. Gleeson, 1998, Methods in molecular biology.

The fifth epidermal growth factor-like domain of thrombomodulin does not have an epidermal growth factor-like disulfide bonding pattern.

E. Komives, M. Hunter, D. Meininger, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Fusion partners can increase the expression of recombinant interleukins via transient transfection in 2936E cells

Haruki Hasegawa, J. Delaney, M. Wolfson, 2010, Protein science : a publication of the Protein Society.

Large-scale expression, purification and characterization of small fragments of thrombomodulin: the roles of the sixth domain and of methionine 388.

E. Komives, M. Hunter, D. Meininger, 1995, Protein engineering.

Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors.

J. McCarter, C. Sutherland, Yichin Liu, 2011, Biochimica et biophysica acta.

Molecular basis of sphingosine kinase 1 substrate recognition and catalysis.

N. Walker, Zhulun Wang, Jinsong Liu, 2013, Structure.

AMG 595, an Anti-EGFRvIII Antibody–Drug Conjugate, Induces Potent Antitumor Activity against EGFRvIII-Expressing Glioblastoma

T. Arora, C. Kozlosky, Hua Liu, 2015, Molecular Cancer Therapeutics.

The IL-1 receptor accessory protein (AcP) is required for IL-33 signaling and soluble AcP enhances the ability of soluble ST2 to inhibit IL-33.

Dirk E. Smith, C. Gabay, M. Smithgall, 2008, Cytokine.

Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers.

C. Craik, N. Walker, T. Hoey, 2005, The Biochemical journal.

In vitro modulation of cytochrome P450 reductase supported indoleamine 2,3-dioxygenase activity by allosteric effectors cytochrome b(5) and methylene blue.

L. Wienkers, D. Rock, D. Meininger, 2010, Biochemistry.

The high-resolution crystal structure of human LCAT1

N. Walker, Zhulun Wang, S. Thibault, 2015, Journal of Lipid Research.

NMR-based structural characterization of large protein-ligand interactions

Maurizio Pellecchia, Daniel S Sem, D. Sem, 2002, Journal of biomolecular NMR.

Agonistic Human Antibodies Binding to Lecithin-Cholesterol Acyltransferase Modulate High Density Lipoprotein Metabolism*

N. Walker, J. Delaney, R. Gunawardane, 2015, The Journal of Biological Chemistry.

Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern.

E. Komives, M. Hunter, D. Meininger, 1997, Journal of molecular biology.

Systems-based design of bi-ligand inhibitors of oxidoreductases: filling the chemical proteomic toolbox.

Maurizio Pellecchia, Daniel S Sem, H. Villar, 2004, Chemistry & biology.

Developability studies before initiation of process development

W. Xu, A. Ambrogelly, Jason K. Cheung, 2013, mAbs.

Characterization of the binding interface between the E-domain of Staphylococcal protein A and an antibody Fv-fragment.

M. Rance, N. Skelton, M. Starovasnik, 2000, Biochemistry.

Synthesis, activity, and preliminary structure of the fourth EGF‐like domain of thrombomodulin

E. Komives, M. Hunter, D. Meininger, 1995, Protein science : a publication of the Protein Society.

Thrombin inhibition by cyclic peptides from thrombomodulin

E. Komives, D. Meininger, J. Lougheed, 1995, Protein science : a publication of the Protein Society.

Structure/function of the fourth and fifth EGF domains of thrombomodulin

E. Komives, M. Hunter, D. Meininger, 1996 .

SEA-TROSY (solvent exposed amides with TROSY): a method to resolve the problem of spectral overlap in very large proteins.

D. Sem, C. Kasper, M. Pellecchia, 2001, Journal of the American Chemical Society.