What is she best known for?
The fields of study she is best known for:
Her main research concerns Biochemistry, Stereochemistry, Enzyme, Chymotrypsin and Trypsin.
Biochemistry and IMP dehydrogenase are frequently intertwined in her study.
Her research integrates issues of Biosynthesis, Cryptosporidium parvum, Antimicrobial chemotherapy, Dehydrogenase and NAD+ kinase in her study of IMP dehydrogenase.
Her Stereochemistry study integrates concerns from other disciplines, such as Residue, Covalent bond, Arginine, Isothermal titration calorimetry and Binding site.
The Chymotrypsin study combines topics in areas such as Amino acid, Protease, Hydrolysis, Peptide sequence and Substrate.
Her Trypsin research incorporates themes from Protein structure, Enzyme catalysis and Benzamidine.
Her most cited work include:
- Serine protease mechanism and specificity. (1231 citations)
- A review of the global burden, novel diagnostics, therapeutics, and vaccine targets for cryptosporidium (427 citations)
- IMP dehydrogenase: structure, mechanism, and inhibition. (240 citations)
What are the main themes of her work throughout her whole career to date?
Lizbeth Hedstrom mostly deals with Biochemistry, IMP dehydrogenase, Enzyme, Stereochemistry and Inosine.
Her research combines Cryptosporidium parvum and Biochemistry.
Her study explores the link between IMP dehydrogenase and topics such as NAD+ kinase that cross with problems in Transition state analog, Oxidoreductase and Covalent bond.
Lizbeth Hedstrom has researched Enzyme in several fields, including Function, Penicillium and Antimicrobial chemotherapy.
Her Stereochemistry research incorporates elements of Cofactor, Substrate, Enzyme kinetics, Trypsin and Active site.
Her Inosine study incorporates themes from Xanthosine and Structure–activity relationship.
She most often published in these fields:
- Biochemistry (55.48%)
- IMP dehydrogenase (34.19%)
- Enzyme (33.55%)
What were the highlights of her more recent work (between 2015-2020)?
- Biochemistry (55.48%)
- Enzyme (33.55%)
- Cell biology (6.45%)
In recent papers she was focusing on the following fields of study:
Lizbeth Hedstrom focuses on Biochemistry, Enzyme, Cell biology, IMP dehydrogenase and Catalytic cycle.
Her study in Cryptosporidium parvum extends to Biochemistry with its themes.
Her study in Enzyme is interdisciplinary in nature, drawing from both Microbiology and Virulence.
Her studies deal with areas such as Metabolic pathway, Function and Drug discovery as well as IMP dehydrogenase.
She interconnects Substrate, Stereochemistry and Cofactor in the investigation of issues within Catalytic cycle.
Her Stereochemistry research includes themes of Xanthosine and Ternary complex.
Between 2015 and 2020, her most popular works were:
- Boc3Arg-Linked Ligands Induce Degradation by Localizing Target Proteins to the 20S Proteasome. (30 citations)
- Expanding Benzoxazole-Based Inosine 5'-Monophosphate Dehydrogenase (IMPDH) Inhibitor Structure-Activity As Potential Antituberculosis Agents. (18 citations)
- Ubiquilin-mediated Small Molecule Inhibition of Mammalian Target of Rapamycin Complex 1 (mTORC1) Signaling (17 citations)
In her most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Biochemistry, Cell biology, Mycobacterium tuberculosis, Virulence and Microbiology.
Her study ties her expertise on Cryptosporidium parvum together with the subject of Biochemistry.
In the subject of general Cell biology, her work in Proteasome, Protein degradation and mTORC1 is often linked to Ubiquilin-2, thereby combining diverse domains of study.
Her Mycobacterium tuberculosis research overlaps with Dehydrogenase, Benzoxazole, Inosine-5′-monophosphate dehydrogenase, Biosynthesis and Inosine.
Lizbeth Hedstrom interconnects IMP dehydrogenase, Tularemia, Mutant and Enzyme in the investigation of issues within Virulence.
Her Microbiology research is multidisciplinary, relying on both Francisella tularensis, Structure–activity relationship and DNA ligase.
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