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Critical Reviews™ in Eukaryotic Gene Expression

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ISSN Druckformat: 1045-4403

ISSN Online: 2162-6502

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 1.6 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.2 The Immediacy Index is the average number of times an article is cited in the year it is published. The journal Immediacy Index indicates how quickly articles in a journal are cited. Immediacy Index: 0.3 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00058 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.33 SJR: 0.345 SNIP: 0.46 CiteScore™:: 2.5 H-Index: 67

Indexed in

Protein Flexibility as a Biosignal

Volumen 20, Ausgabe 2, 2010, pp. 157-170
DOI: 10.1615/CritRevEukarGeneExpr.v20.i2.60
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ABSTRAKT

Dynamic properties of a protein are crucial for all protein functions, and those of signaling proteins are closely related to the biological function of living beings. The protein flexibility signal concept can be used to analyze this relationship. Protein flexibility controls the rate of protein conformational change and influences protein function. The modification of protein flexibility results in a change of protein activity. The logical nature of protein flexibility cannot be explained by applying the principles of protein three-dimensional structure theory or conformation concept. Signaling proteins show high protein flexibility. Many properties of signaling can be traced back to the dynamic natures of signaling protein. The action mechanism of volatile anesthetics and universal cellular reactions are related to flexibility in the change of signaling proteins. We conclude that protein dynamics is an enzyme-enhanced process, called dynamicase.

REFERENZIERT VON
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  2. Gupta Akshita, Singh Anamika, Ahmad Nabeel, Singh Tej P., Sharma Sujata, Sharma Pradeep, Experimental techniques to study protein dynamics and conformations, in Advances in Protein Molecular and Structural Biology Methods, 2022. Crossref

  3. Bhunia Shome S., Saxena Anil K., Efficiency of Homology Modeling Assisted Molecular Docking in G-protein Coupled Receptors, Current Topics in Medicinal Chemistry, 21, 4, 2021. Crossref

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