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Current Issues in Molecular Biology is published by MDPI from Volume 43 Issue 1 (2021). Previous articles were published by another publisher in Open Access under a CC-BY (or CC-BY-NC-ND) licence, and they are hosted by MDPI on mdpi.com as a courtesy and upon agreement with Caister Press.

Curr. Issues Mol. Biol., Volume 3, Issue 3 (July 2001) – 3 articles

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887 KiB  
Review
DNA Measurement and Cell Cycle Analysis by Flow Cytometry
by Rafael Nunez
Curr. Issues Mol. Biol. 2001, 3(3), 67-70; https://doi.org/10.21775/cimb.003.067 - 1 Jul 2001
Cited by 5 | Viewed by 3782
Abstract
Measurement of cellular DNA content and the analysis of the cell cycle can be performed by flow cytometry. Protocols for DNA measurement have been developed including Bivariate cytokeratin/DNA analysis, Bivariate BrdU/DNA analysis, and multiparameter flow cytometry measurement of cellular DNA content. This review [...] Read more.
Measurement of cellular DNA content and the analysis of the cell cycle can be performed by flow cytometry. Protocols for DNA measurement have been developed including Bivariate cytokeratin/DNA analysis, Bivariate BrdU/DNA analysis, and multiparameter flow cytometry measurement of cellular DNA content. This review summarises the methods for measurement of cellular DNA and analysis of the cell cycle and discusses the commercial software available for these purposes. Full article
1062 KiB  
Review
Degradation of Mutant Proteins, Underlying "Loss of Function" Phenotypes, Plays a Major Role in Genetic Disease
by Paula J. Waters
Curr. Issues Mol. Biol. 2001, 3(3), 57-65; https://doi.org/10.21775/cimb.003.057 - 1 Jul 2001
Cited by 2 | Viewed by 496
Abstract
Many Mendelian monogenic disorders are caused by loss of the function of a single protein. This can result from rapid degradation of the mutant protein by cellular proteases, which reduces the steady-state concentration of the protein within the cell. The susceptibility of a [...] Read more.
Many Mendelian monogenic disorders are caused by loss of the function of a single protein. This can result from rapid degradation of the mutant protein by cellular proteases, which reduces the steady-state concentration of the protein within the cell. The susceptibility of a protein to such proteolytic breakdown depends upon its kinetics of monomer folding and oligomer assembly and upon the intrinsic (thermodynamic) stability of its functional native-state conformation. Other cellular proteins, notably molecular chaperones, promote correct protein folding and assembly and thus provide some protection against degradation. An accumulation of recent evidence indicates that premature or accelerated degradation of mutant proteins, provoked by aberrations in their conformation, occurs in various subcellular compartments and represents a significant and prevalent pathogenic mechanism underlying genetic diseases. Inter-individual variability in proteolytic and folding systems can in part explain why "simple monogenic diseases" often display inconsistent genotype-phenotype correlations which show these disorders to be in reality quite complex. Protein folding and degradation may also be modulated artificially using exogenous small molecules. The identification or design of compounds which can interact specifically with particular target proteins, and which in so doing can exert beneficial effects on protein folding, assembly and/or stability, is beginning to open up a new and remarkably promising avenue for the treatment of diverse genetic disorders. Full article
976 KiB  
Review
SWISS-PROT: Connecting Biomolecular Knowledge Via a Protein Database
by Elisabeth Gasteiger, Eva Jung and Amos Bairoch
Curr. Issues Mol. Biol. 2001, 3(3), 47-55; https://doi.org/10.21775/cimb.003.047 - 1 Jul 2001
Cited by 8 | Viewed by 953
Abstract
With the explosive growth of biological data, the development of new means of data storage was needed. More and more often biological information is no longer published in the conventional way via a publication in a scientific journal, but only deposited into a [...] Read more.
With the explosive growth of biological data, the development of new means of data storage was needed. More and more often biological information is no longer published in the conventional way via a publication in a scientific journal, but only deposited into a database. In the last two decades these databases have become essential tools for researchers in biological sciences. Biological databases can be classified according to the type of information they contain. There are basically three types of sequence-related databases (nucleic acid sequences, protein sequences and protein tertiary structures) as well as various specialized data collections. It is important to provide the users of biomolecular databases with a degree of integration between these databases as by nature all of these databases are connected in a scientific sense and each one of them is an important piece to biological complexity. In this review we will highlight our effort in connecting biological information as demonstrated in the SWISS-PROT protein database. Full article
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