The scientist’s investigation covers issues in Biochemistry, Stereochemistry, Amino acid, Somatostatin and Structure–activity relationship. Much of his study explores Biochemistry relationship to In vivo. He interconnects Protecting group, Methylation and Thiol in the investigation of issues within Stereochemistry.
His Amino acid research integrates issues from Tetrapeptide, Aqueous medium and Metabolism. His Somatostatin research includes themes of Protein structure, Insulin, Glucagon and Cyclic peptide. His research in Structure–activity relationship intersects with topics in Biological activity and Receptor.
The scientist’s investigation covers issues in Stereochemistry, Biochemistry, Cathepsin K, Pharmacology and Amino acid. His Stereochemistry study integrates concerns from other disciplines, such as Somatostatin, Biological activity, Enzyme inhibitor and Peptide, Peptide synthesis. Daniel F. Veber is investigating Somatostatin as part of his Endocrinology and Internal medicine and Somatostatin study.
His work on Protease, Receptor and Structure–activity relationship as part of general Biochemistry study is frequently connected to Composition, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. His Cathepsin K research is multidisciplinary, relying on both Cathepsin O, Cathepsin, Enzyme and Cysteine protease. His work carried out in the field of Osteoclast brings together such families of science as Bone resorption and Resorption.
His primary areas of study are Biochemistry, Cathepsin K, Protease, Cathepsin and Stereochemistry. In his research on the topic of Biochemistry, Enzyme inhibitor is strongly related with In vivo. His study in Cathepsin K is interdisciplinary in nature, drawing from both Cathepsin O, Bioavailability and Cysteine protease.
As a member of one scientific family, Daniel F. Veber mostly works in the field of Protease, focusing on Combinatorial chemistry and, on occasion, Scientific method. His Stereochemistry research incorporates elements of Biological activity, In vitro, Ring, Somatostatin and Enzyme. His work investigates the relationship between In vitro and topics such as Receptor that intersect with problems in Protein structure, Peptide sequence, Amino acid and Plasma protein binding.
Biochemistry, Stereochemistry, Cathepsin K, In vitro and Enzyme inhibitor are his primary areas of study. Daniel F. Veber works mostly in the field of Biochemistry, limiting it down to topics relating to In vivo and, in certain cases, Endothelial stem cell and Angiogenesis. His Stereochemistry study incorporates themes from Somatostatin, Rumen, Alanine, Sarcosine and Biological activity.
His Cathepsin K research is multidisciplinary, incorporating perspectives in Bone resorption, Cathepsin and Resorption. His In vitro study combines topics from a wide range of disciplines, such as Bioavailability, Pharmacology, Receptor, Combinatorial chemistry and Conformational isomerism. The concepts of his Enzyme inhibitor study are interwoven with issues in Matrigel and Small molecule.
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A potent cyclic hexapeptide analogue of somatostatin
Daniel F. Veber;Roger M. Freidinger;Debra Schwenk Perlow;William J. Paleveda.
Fibrinogen receptor antagonists
Ruth F. Nutt;Stephen F. Brady;Daniel F. Veber.
Transfusion Science (1993)
Compounds and methods
Joseph P. Marino;Scott K. Thompson;Daniel Frank Veber.
Benzodiazepine gastrin and brain cholecystokinin receptor ligands; L-365,260
Mark G. Bock;Robert M. DiPardo;Ben E. Evans;Kenneth E. Rittle.
Journal of Medicinal Chemistry (1989)
Design of potent, orally effective, nonpeptidal antagonists of the peptide hormone cholecystokinin
Ben E. Evans;Mark G. Bock;Kenneth E. Rittle;Robert M. Dipardo.
Proceedings of the National Academy of Sciences of the United States of America (1986)
Acetamidomethyl. A Novel Thiol Protecting Group for Cysteine
Daniel Veber;John Milkowski;Sandor Varga;Robert Denkewalter.
Journal of the American Chemical Society (1972)
HIV-1 protease specificity of peptide cleavage is sufficient for processing of gag and pol polyproteins.
Paul L. Darke;Ruth F. Nutt;Stephen F. Brady;Victor M. Garsky.
Biochemical and Biophysical Research Communications (1988)
Protected lactam-bridged dipeptides for use as conformational constraints in peptides
Roger M. Freidinger;Debra Schwenk Perlow;Daniel F. Veber.
Journal of Organic Chemistry (1982)
Peptide Aldehyde Inhibitors of Cathepsin K Inhibit Bone Resorption Both In Vitro and In Vivo
Bartholomew J. Votta;Mark A. Levy;Alison Badger;Jeremy Bradbeer.
Journal of Bone and Mineral Research (1997)
Novel renin inhibitors containing the amino acid statine
Joshua Boger;Nancy S. Lohr;Edgar H. Ulm;Martin Poe.
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