What is he best known for?
The fields of study he is best known for:
Henry Weiner focuses on Biochemistry, Aldehyde dehydrogenase, ALDH2, Enzyme and Dehydrogenase.
Henry Weiner has researched Biochemistry in several fields, including Molecular biology and Stereochemistry.
His work carried out in the field of Aldehyde dehydrogenase brings together such families of science as Mitochondrial matrix, Cytosol, Chromatography, Allele and Branched-chain alpha-keto acid dehydrogenase complex.
The ALDH2 study combines topics in areas such as Isoelectric point, Dominance and Transfection.
When carried out as part of a general Enzyme research project, his work on Hemin, Enzyme assay and Heme is frequently linked to work in Apigenin, therefore connecting diverse disciplines of study.
His work deals with themes such as Benzaldehyde, Mutant, Aldehyde, Propionaldehyde and Esterase, which intersect with Dehydrogenase.
His most cited work include:
- Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. (272 citations)
- Mitochondrial Aldehyde Dehydrogenase Activity Is Required for Male Fertility in Maize (200 citations)
- Horse Liver Aldehyde Dehydrogenase I. PURIFICATION AND CHARACTERIZATION (171 citations)
What are the main themes of his work throughout his whole career to date?
His scientific interests lie mostly in Biochemistry, Aldehyde dehydrogenase, Enzyme, Stereochemistry and ALDH2.
Much of his study explores Biochemistry relationship to Molecular biology.
His Aldehyde dehydrogenase study combines topics from a wide range of disciplines, such as Aldehyde, Active site, Dehydrogenase, Isozyme and Metabolism.
The Enzyme study which covers Protein subunit that intersects with Dimer.
The concepts of his Stereochemistry study are interwoven with issues in Amino acid, Coenzyme binding, Mutant, Protein structure and Binding site.
Henry Weiner interconnects Cofactor and Nicotinamide in the investigation of issues within NAD+ kinase.
He most often published in these fields:
- Biochemistry (74.85%)
- Aldehyde dehydrogenase (58.28%)
- Enzyme (35.58%)
What were the highlights of his more recent work (between 2003-2021)?
- Biochemistry (74.85%)
- Aldehyde dehydrogenase (58.28%)
- Enzyme (35.58%)
In recent papers he was focusing on the following fields of study:
His main research concerns Biochemistry, Aldehyde dehydrogenase, Enzyme, Mitochondrion and Stereochemistry.
His study in Aldehyde dehydrogenase focuses on ALDH2 in particular.
His biological study spans a wide range of topics, including Ethanol metabolism, Acetaldehyde, Isozyme and Molecular biology.
His study in the field of Malate dehydrogenase, Alcohol dehydrogenase and Aldose reductase also crosses realms of Aldophosphamide.
His Mitochondrion research integrates issues from Mitochondrial DNA, Cytosol, Green fluorescent protein, N-terminus and Signal peptide.
His Stereochemistry research also works with subjects such as
- Coenzyme binding which is related to area like Active site, Oxidoreductase, NAD binding, Cofactor binding and Nicotinamide,
- Protein structure which is related to area like Serine, Binding site and Enzyme kinetics.
Between 2003 and 2021, his most popular works were:
- Role of reduced lipoic acid in the redox regulation of mitochondrial aldehyde dehydrogenase (ALDH-2) activity. Implications for mitochondrial oxidative stress and nitrate tolerance (132 citations)
- Structural and Functional Consequences of Coenzyme Binding to the Inactive Asian Variant of Mitochondrial Aldehyde Dehydrogenase ROLES OF RESIDUES 475 AND 487 (91 citations)
- Disruption of the coenzyme binding site and dimer interface revealed in the crystal structure of mitochondrial aldehyde dehydrogenase "Asian" variant. (81 citations)
In his most recent research, the most cited papers focused on:
Henry Weiner mostly deals with Biochemistry, Aldehyde dehydrogenase, Oxidoreductase, ALDH2 and Active site.
Enzyme, Mitochondrion, Dehydrogenase, Benzoic acid and Phenylalanine are the primary areas of interest in his Biochemistry study.
Henry Weiner combines subjects such as Reactive oxygen species and Ferritin with his study of Enzyme.
Henry Weiner focuses mostly in the field of Aldehyde dehydrogenase, narrowing it down to matters related to Branched-chain alpha-keto acid dehydrogenase complex and, in some cases, Malate dehydrogenase and Escherichia coli.
The study incorporates disciplines such as NAD+ kinase, Cofactor, Coenzyme binding, Stereochemistry and Protein structure in addition to Oxidoreductase.
His studies in ALDH2 integrate themes in fields like Molecular biology, Isozyme and Acetaldehyde.
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