Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies(112 visite) Berisio R, Squeglia F, Ruggiero A, Petraccone L, Stellato MI, Del Vecchio P
BBA-MOL BASIS DIS (ISSN: 0925-4439), 2015 Feb 8; 1854(5): 402-409.
Tipo di articolo: Journal Article,
Impact factor: 5.158, Impact factor a 5 anni: 5.36
Parole chiave: Dsc, Eukaryotic-Type Serine Threonine Kinases, Thermal Unfolding Of Multi-Domain Proteins, Bacillus Subtilis, Posibacteria, Staphylococcus Aureus, Bacterial Enzyme, Protein Serine Threonine Kinase, Article, Calorimetry, Circular Dichroism, Differential Scanning Calorimetry, Enzyme Analysis, Extracellular Space, Melting Point, Nonhuman, Priority Journal, Protein Folding, Protein Unfolding, Thermodynamics, Protein Kinase C, Amino Acid Sequence, Chemistry, Enzymology, Models, Molecular, Molecular Sequence Data, Protein Stability, Protein Structure, Tertiary, Sequence Homology,
Affiliazioni:
*** IBB - CNR *** Institute of Biostructures and Bioimaging, CNR, via Mezzocannone 16Napoli, Italy Department of Chemical Sciences, University of Naples Federico II, via CintiaNapoli, Italy Consiglio Nazionale delle Ricerche Universita degli Studi di Napoli Federico II
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42 Records (40 escludendo Abstract e Conferenze). Impact factor totale: 169.726 (163.599 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 158.075 (151.729 escludendo Abstract e Conferenze).
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