What is she best known for?
The fields of study she is best known for:
Her primary areas of study are Endocrinology, Internal medicine, Phosphodiesterase, Biochemistry and Phosphodiesterase 3.
Her research in Endocrinology intersects with topics in Phosphatidylinositol and Cyclin-dependent kinase 9.
Her studies in Internal medicine integrate themes in fields like MAPK14, cGMP-dependent protein kinase, Cyclin-dependent kinase 2, Mitogen-activated protein kinase kinase and MAP2K7.
In her study, Adrenergic agonist is inextricably linked to Cell biology, which falls within the broad field of Phosphodiesterase.
Eva Degerman focuses mostly in the field of Biochemistry, narrowing it down to matters related to Molecular biology and, in some cases, Protein kinase A, Enzyme activator, Protein domain, Endoplasmic reticulum and Open reading frame.
Her Phosphodiesterase 3 study typically links adjacent topics like Cyclic nucleotide phosphodiesterase.
Her most cited work include:
- Structure, localization, and regulation of cGMP-inhibited phosphodiesterase (PDE3). (380 citations)
- Identification of Novel Phosphorylation Sites in Hormone-sensitive Lipase That Are Phosphorylated in Response to Isoproterenol and Govern Activation Properties in Vitro (374 citations)
- Diversity in cyclic nucleotide phosphodiesterase isoenzyme families (207 citations)
What are the main themes of her work throughout her whole career to date?
Eva Degerman focuses on Internal medicine, Endocrinology, Biochemistry, Insulin and Phosphodiesterase.
Her research integrates issues of Protein kinase A and Phosphorylation in her study of Internal medicine.
Her Endocrinology study often links to related topics such as AMPK.
The Biochemistry study which covers Molecular biology that intersects with cDNA library and Recombinant DNA.
Phosphodiesterase 3 and Cilostamide are the primary areas of interest in her Phosphodiesterase study.
Her Phosphodiesterase 3 research incorporates themes from Rolipram, PDE10A, Signal transduction and Cyclic adenosine monophosphate.
She most often published in these fields:
- Internal medicine (47.52%)
- Endocrinology (47.52%)
- Biochemistry (34.04%)
What were the highlights of her more recent work (between 2010-2021)?
- Internal medicine (47.52%)
- Endocrinology (47.52%)
- Adipose tissue (14.18%)
In recent papers she was focusing on the following fields of study:
Eva Degerman mainly focuses on Internal medicine, Endocrinology, Adipose tissue, Phosphodiesterase 3 and Insulin.
Eva Degerman combines subjects such as Protein kinase A and Phosphorylation with her study of Internal medicine.
The various areas that Eva Degerman examines in her Endocrinology study include AMP-activated protein kinase, AMPK and Protein kinase B.
Her Phosphodiesterase 3 study focuses on Phosphodiesterase and Cell biology.
Her Insulin research focuses on Brown adipose tissue and how it connects with Cholic acid, CYP8B1 and TFAM.
Her Cyclic nucleotide phosphodiesterase study is concerned with the field of Biochemistry as a whole.
Between 2010 and 2021, her most popular works were:
- Reduced insulin secretion correlates with decreased expression of exocytotic genes in pancreatic islets from patients with type 2 diabetes. (85 citations)
- Cyclic Nucleotide Phosphodiesterases: important signaling modulators and therapeutic targets (76 citations)
- From PDE3B to the regulation of energy homeostasis. (76 citations)
In her most recent research, the most cited papers focused on:
Her primary scientific interests are in Internal medicine, Endocrinology, Phosphodiesterase 3, Biochemistry and Lipolysis.
Her Internal medicine study frequently draws connections to adjacent fields such as Protein kinase A.
Her Endocrinology research integrates issues from PDE1 and Receptor.
Her Phosphodiesterase 3 study is related to the wider topic of Phosphodiesterase.
She works mostly in the field of Phosphodiesterase, limiting it down to concerns involving ATPase and, occasionally, Phosphorylation.
Her Lipolysis study combines topics in areas such as Lipid metabolism, Mediator and Energy homeostasis.
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