J.F. Kuo

What is he best known for?

The fields of study he is best known for:

• Enzyme
• Biochemistry
• Phosphorylation

J.F. Kuo mainly investigates Protein kinase A, Biochemistry, Protein kinase C, Molecular biology and Kinase. His study on Protein kinase A is mostly dedicated to connecting different topics, such as Calmodulin. Ca2+/calmodulin-dependent protein kinase, Phospholipid and Phosphorylation are the core of his Biochemistry study.

J.F. Kuo combines subjects such as Ouabain and Nucleus with his study of Protein kinase C. His work deals with themes such as Chlorprothixene, Endocrinology, Chlorpromazine and Non-competitive inhibition, which intersect with Kinase. His Protein phosphorylation research includes themes of Cyclin-dependent kinase 2 and MAP2K7.

His most cited work include:

• Phospholipid-sensitive Ca2+-dependent protein kinase from heart. II. Substrate specificity and inhibition by various agents. (251 citations)
• Phospholipid-sensitive calcium-dependent protein kinase: inhibition by antipsychotic drugs. (220 citations)
• Phospholipid-sensitive Ca2+-dependent protein phosphorylation system in various types of leukemic cells from human patients and in human leukemic cell lines HL60 and K562, and its inhibition by alkyl-lysophospholipid. (199 citations)

What are the main themes of his work throughout his whole career to date?

Biochemistry, Protein kinase A, Protein kinase C, Phosphorylation and Molecular biology are his primary areas of study. His study in Biochemistry focuses on Protein phosphorylation, Ca2+/calmodulin-dependent protein kinase, Kinase, Phospholipid and Enzyme. His Protein kinase A research integrates issues from Myosin light-chain kinase and Calmodulin.

The various areas that J.F. Kuo examines in his Protein kinase C study include Phosphatidylserine and Nucleus. His Phosphorylation research is multidisciplinary, incorporating perspectives in Cytoplasm, Myelin basic protein and Myeloid leukemia. The Molecular biology study combines topics in areas such as K562 cells and PRKCB1.

He most often published in these fields:

• Biochemistry (70.73%)
• Protein kinase A (63.41%)
• Protein kinase C (62.20%)

What were the highlights of his more recent work (between 1989-1996)?

• Protein kinase C (62.20%)
• Biochemistry (70.73%)
• Phosphorylation (36.59%)

In recent papers he was focusing on the following fields of study:

His primary areas of study are Protein kinase C, Biochemistry, Phosphorylation, Molecular biology and Protein kinase A. Protein kinase C is a subfield of Cell biology that J.F. Kuo investigates. In general Phosphorylation study, his work on Myosin light-chain kinase often relates to the realm of Ca Mg-ATPase, thereby connecting several areas of interest.

J.F. Kuo has researched Molecular biology in several fields, including Protein phosphorylation and Serine. A large part of his Protein kinase A studies is devoted to PRKCE. His Mechanism of action research includes elements of Na+/K+-ATPase and Phospholipid.

Between 1989 and 1996, his most popular works were:

• Cardiac Troponin I Mutants PHOSPHORYLATION BY PROTEIN KINASES C AND A AND REGULATION OF Ca2+-STIMULATED MgATPase OF RECONSTITUTED ACTOMYOSIN S-1 (155 citations)
• Inhibition of Protein Kinase C, (Sodium plus Potassium)-activated Adenosine Triphosphatase, and Sodium Pump by Synthetic Phospholipid Analogues (108 citations)
• Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2. (83 citations)

In his most recent research, the most cited papers focused on:

• Enzyme
• Biochemistry
• Phosphorylation

J.F. Kuo mostly deals with Protein kinase C, Biochemistry, PRKCE, Protein kinase A and Phosphorylation. His Protein kinase C study combines topics in areas such as Molecular biology, Troponin complex, Enzyme inhibitor and Adenosine triphosphate. His Molecular biology research is multidisciplinary, incorporating elements of Akt/PKB signaling pathway, cGMP-dependent protein kinase, Kinase and Ca2+/calmodulin-dependent protein kinase.

His Troponin complex study incorporates themes from Substrate-level phosphorylation and Isozyme. His work carried out in the field of Enzyme inhibitor brings together such families of science as Ouabain, Phospholipid, Mechanism of action, Intracellular and Na+/K+-ATPase. His Adenosine triphosphate research includes elements of Myosin light-chain kinase, Calphostin C and Chelerythrine.