What is she best known for?
The fields of study she is best known for:
Her primary scientific interests are in Biochemistry, Cell biology, Cancer research, Molecular biology and Exome.
Her research related to Secretory pathway, Protein phosphorylation, Sterol transport, Transmembrane domain and ATP-binding domain of ABC transporters might be considered part of Biochemistry.
Her Cell biology research includes elements of Peptide sequence, In vitro, Membrane protein and Peptide.
Lisa N. Kinch regularly links together related areas like Germline mutation in her Cancer research studies.
Her study explores the link between Molecular biology and topics such as RNA that cross with problems in Gene silencing.
Her Exome research incorporates elements of PTEN and Ectopic expression.
Her most cited work include:
- BAP1 loss defines a new class of renal cell carcinoma (588 citations)
- Identification of a candidate therapeutic autophagy-inducing peptide (511 citations)
- Identification of a candidate therapeutic autophagy-inducing peptide (511 citations)
What are the main themes of her work throughout her whole career to date?
Lisa N. Kinch focuses on Biochemistry, Cell biology, Protein structure, Computational biology and Genetics.
Her Cell biology research is multidisciplinary, relying on both Regulator and Membrane protein.
The study incorporates disciplines such as Biophysics, Peptide sequence, Plasma protein binding and Database in addition to Protein structure.
Lisa N. Kinch combines subjects such as Binding site and Virulence with her study of Peptide sequence.
Her Computational biology research includes themes of Protein domain, Protein family, Protein Data Bank, Homology and Structural genomics.
Her studies deal with areas such as Cancer research and Allele as well as Mutation.
She most often published in these fields:
- Biochemistry (25.00%)
- Cell biology (19.74%)
- Protein structure (17.11%)
What were the highlights of her more recent work (between 2018-2021)?
- Computational biology (16.45%)
- Protein domain (10.53%)
- Cell biology (19.74%)
In recent papers she was focusing on the following fields of study:
The scientist’s investigation covers issues in Computational biology, Protein domain, Cell biology, Mutation and Mutant.
Her work in Computational biology addresses subjects such as Homology, which are connected to disciplines such as Protein structure, A protein and Protein superfamily.
Her Protein domain study incorporates themes from Manual curation, Human proteome project, Protein multimerization and ATP-binding cassette transporter.
Her Cell biology study incorporates themes from Mutant protein and Protein AMPylation.
Lisa N. Kinch has included themes like Wild type, Cancer research and Kidney in her Mutation study.
Her research integrates issues of Cryptococcosis, Cryptococcus neoformans and Virulence in her study of Mutant.
Between 2018 and 2021, her most popular works were:
- Structure, lipid scrambling activity and role in autophagosome formation of ATG9A (23 citations)
- Combined blockade of activating ERBB2 mutations and ER results in synthetic lethality of ER+/HER2 mutant breast cancer (21 citations)
- A lytic polysaccharide monooxygenase-like protein functions in fungal copper import and meningitis (17 citations)
In her most recent research, the most cited papers focused on:
Her primary scientific interests are in Cancer research, Gene, Protein structure, Neratinib and Tyrosine-kinase inhibitor.
In most of her Cancer research studies, her work intersects topics such as Cancer cell.
Her research in Cancer cell intersects with topics in Phenotype, RUVBL2, Multiprotein complex and ATPase.
Her Protein structure course of study focuses on Computational biology and Protein domain.
Her Protein domain study integrates concerns from other disciplines, such as Last universal ancestor, Sequence, Enzyme Commission number and Artificial intelligence.
Her Tyrosine-kinase inhibitor research is multidisciplinary, incorporating elements of Protein kinase B, Synthetic lethality, MEK inhibitor and Estrogen receptor, Fulvestrant.
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