What is she best known for?
The fields of study she is best known for:
Her primary areas of study are Stereochemistry, Active site, Protein structure, Enzyme and Biochemistry.
Her research integrates issues of Isomerase, Hydrolase, Molecule and Binding site in her study of Stereochemistry.
Her Active site study also includes fields such as
- Carbamoyl phosphate synthetase which connect with Tryptophan synthase, Asparagine synthetase and Glutamine amidotransferase,
- Dictyostelium discoideum that connect with fields like Protein tertiary structure.
She combines subjects such as Propionyl-CoA carboxylase, Crystallography, Biotin carboxylase, Dehalogenase and Multiple isomorphous replacement with her study of Protein structure.
Her work in the fields of Enzyme, such as Substrate, GTP' and Galactose Metabolism, intersects with other areas such as Structure and function.
Her work in Biochemistry addresses subjects such as Molecular motor, which are connected to disciplines such as Smooth Muscle Myosins and MYL2.
Her most cited work include:
- Three-dimensional structure of myosin subfragment-1: a molecular motor (1744 citations)
- Structure of the actin-myosin complex and its implications for muscle contraction. (1444 citations)
- X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. (550 citations)
What are the main themes of her work throughout her whole career to date?
Her primary scientific interests are in Stereochemistry, Biochemistry, Enzyme, Active site and Protein structure.
The concepts of her Stereochemistry study are interwoven with issues in Crystallography, Protein subunit, Isomerase, Substrate and Binding site.
Her Crystallography research incorporates themes from Ferredoxin, Molecule, Hydrogen bond and Crystallization.
Hazel M. Holden interconnects Hydrolysis and Campylobacter jejuni in the investigation of issues within Enzyme.
Her Active site research includes themes of Amino acid, Mutant protein, Protein quaternary structure and Dehydratase.
Her Protein structure study combines topics from a wide range of disciplines, such as Peptide sequence and Multiple isomorphous replacement.
She most often published in these fields:
- Stereochemistry (58.67%)
- Biochemistry (50.55%)
- Enzyme (33.58%)
What were the highlights of her more recent work (between 2013-2021)?
- Biochemistry (50.55%)
- Enzyme (33.58%)
- Campylobacter jejuni (6.27%)
In recent papers she was focusing on the following fields of study:
Hazel M. Holden mainly focuses on Biochemistry, Enzyme, Campylobacter jejuni, Stereochemistry and Transferase.
Her study in Biosynthesis, Active site, NAD+ kinase, Dehydratase and Acyltransferase falls under the purview of Biochemistry.
Her studies in Active site integrate themes in fields like Protein structure, Protein subunit, Giant Virus and Mimivirus.
Her Enzyme study integrates concerns from other disciplines, such as Escherichia coli, Protein quaternary structure and Bacteria.
She integrates many fields in her works, including Stereochemistry and N-acetyltransferase.
She has included themes like Pyridoxal, Streptomyces fradiae, Protein domain, Function and Streptomyces in her Transferase study.
Between 2013 and 2021, her most popular works were:
- Computational Redesign of Acyl-ACP Thioesterase with Improved Selectivity toward Medium-Chain-Length Fatty Acids (39 citations)
- New role for the ankyrin repeat revealed by a study of the N-formyltransferase from Providencia alcalifaciens. (16 citations)
- Three-dimensional structure of a sugar N-formyltransferase from Francisella tularensis. (15 citations)
In her most recent research, the most cited papers focused on:
Her main research concerns Biochemistry, Enzyme, Campylobacter jejuni, Transferase and Biosynthesis.
Her Enzyme research integrates issues from Escherichia coli and Bacteria.
Her Campylobacter jejuni research incorporates elements of Francisella tularensis, Reductase and NAD+ kinase.
Her Transferase study incorporates themes from Lipid A, Protein domain, Protein subunit, Stereochemistry and Ankyrin repeat.
The study incorporates disciplines such as Protein structure and Active site in addition to Protein subunit.
Her work carried out in the field of Stereochemistry brings together such families of science as L-serine dehydratase, Dehydratase and Substrate.
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