Ubiquitinization noun interpretation: a guide paper for the systematic identification of ubiquitin interaction protein research methods.

Ubiquitinization noun salutation: Ubiquitin (a class of low molecular weight protein) molecules under a series of special enzymes, the protein in the cell classification, from which to select the target protein molecules, target protein specific modification process.
ubiquitin plays an important role in protein positioning, metabolism, function, regulation and degradation, and participates in the regulation of cell cycle, proliferation, apoptosis, differentiation, transfer and almost all life activities.
ubiquitination is closely related to the incidence of cancer, cardiovascular and other diseases. As one of the major achievements of biochemical research in recent years,
ubiquitin has become a new target for research and development of new drugs.
recently, at the invitation of Nature Protocols, Zhang Xiaofei Research Group of the Guangzhou Institute of Biomedicine and Health of the Chinese Academy of Sciences and the University of Nemegen in the Netherlands jointly published a guide paper on the systematic identification of ubiquitin interaction protein research methods. According to the number of protein molecules and topology connected to the protein substrate, the
is divided into monophey, multi-point single ubiquitinization and polypolypnophon, in which the homogenous polyphiminization may be subtyped into 8 subtypes.
at this stage, people are still in case studies and lack of systematic system at which cells are identified by which ubiquitins, proteins, identify different types of polypheronization.
in recent years, Zhang Xiaofei's research team has developed a pro-uclin-rich-mass spectrometry ("UbIA-MS") method with the University of Nemegen in the Netherlands and Leiden University in the Netherlands.
the method can fully and quickly identify the interaction proteins from all ubiquitin chains in the cell lysis.
research published in the journal Molecular Cell and highly rated in same-time journal reviews. "This article establishes a new technique for studying the ubiquitinization signaling pathway and provides a specific set of dichlorophenoprotein chains of interaction proteins,"
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they are now demonstrating that mass spectrometry techniques can be used to systematically identify specific interaction proteins for ubiquitin signals.
this new technology and the newly discovered ubiquitin interaction protein will promote the development of ubiquitin signaling research."
Zhang Xiaofei's research team, together with the University of Nemegen in the Netherlands, published a guide detailing the method, which describes the UbIA-MS approach in five steps.
first, click on the gupliate chain of chemical synthesis that is not hydrolyzed by ubiquitin asesome; second, in vitro affinity and purification of proteins that interact with ubiquitin; second, the proteins that interact with the columns are digested as peptides; then, the liquid chromatography (LC)-mass spectrometry MS/MS is used for analysis; and finally, the differences in enriched proteins are identified through data analysis.
the advantage of this method is that they are rich in a wide range of interacting proteins from primitive cell lysates, which contain biologically relevant post-translation modifications and exist in the form of protein complexes.
, using this method, the chemically synthesized dichlorochlorophyllin, which simulates natural dichlorophyllines, is not cut by endogenous line ubiquitase (DUB).
the application of this technique will help in an in-depth analysis of how cells distinguish between different types of ubiquitin modification.
the data analysis software provided by the guide paper, which can be used to quickly analyze other protein spectrum-related data and give different types of data charts.
research work has been supported by the "100-person Plan" of the Chinese Academy of Sciences and the Guangdong Provincial Science and Technology Department.
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