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One or more keywords matched the following properties of Zhao, Yingming
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keywords Proteomics, epigenetics, protein modifications, cancer, metabolism, Warburg effect
overview Post-translational modifications (PTMs) represent a major vehicle to diversify a cellular proteome, the inventory of all protein species in an organism. PTMs have critical roles in all the major cellular pathways and diseases. A protein can be potentially modified by more than 300 types of post-translational modifications, which are catalyzed by enzymes encoded by more than 5% of the genome in higher eukaryotes. A combination of a dozen PTM sites in a substrate protein could lead to more than a million possible protein structures with potentially different functions. Given the high abundance and diversities of PTMs, they are likely the most complex regulatory mechanisms in cells. Despite their critical roles in cells, little is known about their biology, except several most extensively studied PTMs. Functional characterizations of PTMs at the molecular level have been slow, largely due to a lack of suitable information infrastructure and technology infrastructure.
One or more keywords matched the following items that are connected to Zhao, Yingming
Item TypeName
Concept Protein Processing, Post-Translational
Concept Proteins
Concept Immediate-Early Proteins
Concept Protein Transport
Concept Mitochondrial Proteins
Concept Saccharomyces cerevisiae Proteins
Concept HMGB2 Protein
Concept Escherichia coli Proteins
Concept Protein Interaction Maps
Academic Article Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.
Academic Article The first identification of lysine malonylation substrates and its regulatory enzyme.
Academic Article SnapShot: histone modifications.
Academic Article Metabolic Regulation of Gene Expression by Histone Lysine ß-Hydroxybutyrylation.
Academic Article Metabolic regulation of gene expression through histone acylations.
Academic Article PTMap--a sequence alignment software for unrestricted, accurate, and full-spectrum identification of post-translational modification sites.
Academic Article Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway.
Academic Article ACSF3 and Mal(onate)-Adapted Mitochondria.
Academic Article Lysine glutarylation is a protein posttranslational modification regulated by SIRT5.
Academic Article SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.
Concept Protein Domains
Grant A Novel Proteomics Technology for Protein Farnesylation
Grant Systematic screening for new histone marks and studying their epigenetic function
Grant A Novel Proteomics Technology for Protein Farnesylation
Grant SIRT6 and lysine fatty acylation in macrophage inflammation
Grant Systems-wide analysis of histone lysine 2-hydroxyisobutyrylation pathway
Grant Systematic screening for new histone marks
Grant Biochemistry of lysine crotonylation pathway
Grant Histone lactylation pathway in hair cycle: deacylases and their protein targets
Grant IDENTIFICATION OF PROSTATE AND OVARIAN CANCER MARKERS
Grant MALDI/TOF MASS SPECTROMETER SHARED INSTRUMENT
Grant Global characterization of lysine acetylation in cancer by a proteomics approach
Grant Biochemistry of the lysine beta-hydroxybutyrylation pathway
Search Criteria
  • Protein
  • structures
  • functions