What is he best known for?
The fields of study he is best known for:
Howard Zalkin spends much of his time researching Biochemistry, Binding site, Molecular biology, Glutamine amidotransferase and Glutamine.
Howard Zalkin regularly ties together related areas like Bacillus subtilis in his Biochemistry studies.
The various areas that Howard Zalkin examines in his Binding site study include Repressor and Purr.
Howard Zalkin combines subjects such as RNA, Messenger RNA and Transcription with his study of Molecular biology.
His biological study spans a wide range of topics, including Stereochemistry and Active site.
His Stereochemistry research is multidisciplinary, incorporating perspectives in Asparagine synthetase and Enzyme.
His most cited work include:
- Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices (335 citations)
- Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis. (222 citations)
- Enzymes Utilizing Glutamine as an Amide Donor (218 citations)
What are the main themes of his work throughout his whole career to date?
Howard Zalkin mainly investigates Biochemistry, Enzyme, Glutamine, Purr and Repressor.
His Biochemistry study integrates concerns from other disciplines, such as Molecular biology, Stereochemistry and Bacillus subtilis.
His work in the fields of Enzyme, such as Substrate, intersects with other areas such as Phosphoribosyltransferase.
Howard Zalkin works mostly in the field of Glutamine, limiting it down to concerns involving Cysteine and, occasionally, Histidine.
His Purr study incorporates themes from Mutant, Regulon, DNA, Operator and Lac repressor.
The Repressor study combines topics in areas such as Purine, Operon, Binding site and Hypoxanthine.
He most often published in these fields:
- Biochemistry (71.54%)
- Enzyme (27.64%)
- Glutamine (26.83%)
What were the highlights of his more recent work (between 1994-2011)?
- Biochemistry (71.54%)
- Purr (23.58%)
- Repressor (23.58%)
In recent papers he was focusing on the following fields of study:
Biochemistry, Purr, Repressor, Glutamine and Bacillus subtilis are his primary areas of study.
His Purr research is multidisciplinary, incorporating elements of Lac repressor, Guanine, Mutant and DNA.
The concepts of his Repressor study are interwoven with issues in Binding domain, Binding site and Hypoxanthine.
Within one scientific family, he focuses on topics pertaining to Operon under Bacillus subtilis, and may sometimes address concerns connected to DNA footprinting.
Howard Zalkin works mostly in the field of Transcription, limiting it down to topics relating to Molecular biology and, in certain cases, Gene.
His work carried out in the field of Glutamine amidotransferase brings together such families of science as Enzyme, Active site, Asparagine synthetase and Stereochemistry.
Between 1994 and 2011, his most popular works were:
- Enzymes Utilizing Glutamine as an Amide Donor (218 citations)
- Coupled Formation of an Amidotransferase Interdomain Ammonia Channel and a Phosphoribosyltransferase Active Site (156 citations)
- Mechanism of corepressor-mediated specific DNA binding by the purine repressor (88 citations)
In his most recent research, the most cited papers focused on:
Howard Zalkin mostly deals with Biochemistry, Glutamine amidotransferase, Glutamine, Purine and Binding site.
His research in Biochemistry is mostly focused on Allosteric regulation.
His study explores the link between Glutamine amidotransferase and topics such as Stereochemistry that cross with problems in Asparagine synthetase and Enzyme.
His study focuses on the intersection of Purine and fields such as Psychological repression with connections in the field of Open reading frame, Mutant and Guanosine.
Howard Zalkin has researched Binding site in several fields, including Biophysics, Active site, Lac repressor, Repressor and Bacillus subtilis.
Howard Zalkin interconnects Regulation of gene expression, Transcription and Gene in the investigation of issues within Bacillus subtilis.
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