What is he best known for?
The fields of study he is best known for:
- Enzyme
- Amino acid
- Organic chemistry
His primary scientific interests are in Stereochemistry, Crystal structure, Binding site, Active site and Protein structure.
His research in Stereochemistry intersects with topics in Hirudin, Crystallography, Catalytic triad, DNA and Hydrogen bond.
His Crystallography study integrates concerns from other disciplines, such as Hydroquinone, Gla domain and Oxidation state.
His Crystal structure research incorporates elements of Solution structure and Sodium dithionite.
His work deals with themes such as A-site and Allosteric regulation, which intersect with Active site.
His research investigates the connection between Protein structure and topics such as Antiparallel that intersect with issues in Tetrapeptide and Stacking.
His most cited work include:
- The structure of a complex of recombinant hirudin and human alpha-thrombin (619 citations)
- The structure of alpha-thrombin inhibited by a 15-mer single-stranded DNA aptamer. (428 citations)
- Structure of human des(1-45) factor Xa at 2.2 A resolution. (335 citations)
What are the main themes of his work throughout his whole career to date?
Stereochemistry, Crystallography, Crystal structure, Binding site and Molecule are his primary areas of study.
His research integrates issues of Hirudin, Active site, Hydrogen bond, Protein structure and Peptide in his study of Stereochemistry.
His Crystallography research is multidisciplinary, incorporating elements of Aldolase A and Multiple isomorphous replacement.
His study in Crystal structure is interdisciplinary in nature, drawing from both Ion and Antiparallel.
Alexander Tulinsky usually deals with Binding site and limits it to topics linked to Lysine and Ligand.
His work carried out in the field of Molecule brings together such families of science as Diffractometer, Crystallization and Crystal.
He most often published in these fields:
- Stereochemistry (69.72%)
- Crystallography (35.78%)
- Crystal structure (30.28%)
What were the highlights of his more recent work (between 1997-2008)?
- Stereochemistry (69.72%)
- Biochemistry (12.84%)
- Crystal structure (30.28%)
In recent papers he was focusing on the following fields of study:
His main research concerns Stereochemistry, Biochemistry, Crystal structure, Active site and Crystallography.
His Stereochemistry research incorporates themes from Hydrolase, Binding site, Molecule, Molecular replacement and Peptide.
His work on Trypsin and Peptide mimetic as part of general Biochemistry study is frequently linked to Tissue factor and Ancylostoma caninum, therefore connecting diverse disciplines of science.
His Crystal structure study combines topics in areas such as Bovine Pancreatic Trypsin Inhibitor and Biophysics.
His Active site study incorporates themes from Cleavage, Lyase and Enzyme inhibitor.
His study looks at the relationship between Crystallography and fields such as Protein structure, as well as how they intersect with chemical problems.
Between 1997 and 2008, his most popular works were:
- Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant. (93 citations)
- Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. (79 citations)
- Structure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A Streptococcal surface protein. (53 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Amino acid
- Organic chemistry
His primary areas of investigation include Stereochemistry, Biochemistry, Enzyme inhibitor, Molecular replacement and Active site.
The concepts of his Stereochemistry study are interwoven with issues in Aeruginosin 298-A, Aldehyde and Binding site.
The Binding site study combines topics in areas such as Serine Proteinase Inhibitors and Scissile bond.
The study incorporates disciplines such as Discovery and development of direct thrombin inhibitors and Crystal structure in addition to Biochemistry.
A significant part of his Molecular replacement research incorporates Protein structure and Crystallography studies.
His Active site research is multidisciplinary, incorporating perspectives in Molecular model and Small molecule.
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