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S-Adenosylmethionine Decarboxylase Degradation by the 26 S Proteasome Is Accelerated by Substrate-mediated Transamination
Azmi Yerlikaya
, Bruce A. Stanley
Penn State College of Medicine
Research output
:
Contribution to journal
›
Article
›
peer-review
30
Scopus citations
Overview
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Dive into the research topics of 'S-Adenosylmethionine Decarboxylase Degradation by the 26 S Proteasome Is Accelerated by Substrate-mediated Transamination'. Together they form a unique fingerprint.
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Keyphrases
Substrate-mediated
100%
S-adenosylmethionine Decarboxylase
100%
Transamination
100%
S-adenosylmethionine
16%
Degradation Rate
16%
COS-7 Cells
16%
Proteasome Inhibition
16%
Decarboxylase Activity
8%
Amino
8%
Covalently Bound
8%
Ubiquitin
8%
Polyamine Biosynthesis
8%
Ubiquitination
8%
Hemagglutinin
8%
Substrate Analog
8%
Enzyme Substrates
8%
5′-deoxyadenosine
8%
His-tag
8%
Anti-S
8%
Biochemistry, Genetics and Molecular Biology
Proteasome
100%
Adenosylmethionine Decarboxylase
100%
Transamination
100%
Enzyme
33%
S-Adenosyl Methionine
16%
Hemagglutinin
16%
Ubiquitin
8%
Anabolism
8%
Ubiquitination
8%
Carboxy-Lyases
8%
Substrate Analog
8%
Enzyme Substrate
8%
Deoxyadenosine
8%
Methionine
8%