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The MUC1 SEA module is a self-cleaving domain
Fiana Levitin
, Omer Stern
, Mordechai Weiss
, Chava Gil-Henn
, Ravit Ziv
, Zofnat Prokocimer
, Nechama I. Smorodinsky
, Daniel B. Rubinstein
, Daniel H. Wreschner
Tel Aviv University
Assaf Harofeh Medical Center
United States Food and Drug Administration
Research output
:
Contribution to journal
›
Article
›
peer-review
183
Scopus citations
Overview
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Keyphrases
Mucin 1 (MUC1)
100%
Self-cleavage
100%
Amino Acids
12%
Extracellular Domain
12%
Glycoprotein
12%
Proteolysis
12%
Cleavage Site
12%
Proteolytic Cleavage
12%
Cysteine
6%
Threonine
6%
Nucleophile
6%
Noncovalent Interactions
6%
Transmembrane
6%
In Vitro Incubation
6%
Esters
6%
Transmembrane Protein
6%
Alternative Splicing
6%
Hydroxylamine
6%
Human Adenocarcinoma
6%
Serine Residues
6%
Acyl Rearrangement
6%
Autoproteolysis
6%
Mucin Proteins
6%
Hydrolytic Resolution
6%
Post-translational Cleavage
6%
MUC3
6%
X Protein
6%
N-terminal Amino Acids
6%
Biochemistry, Genetics and Molecular Biology
MUC1
100%
Amino Acids
18%
Isoform
12%
Protein Catabolism
12%
Glycoprotein
12%
N-Terminus
6%
Serine
6%
Cysteine
6%
Threonine
6%
C-Terminus
6%
Precursor
6%
Alternative Splicing
6%
Transmembrane Protein
6%
Membrane Protein
6%
Mucin
6%
Immunology and Microbiology
MUC1
100%
Glycoprotein
12%
Protein Degradation
12%
Carboxy Terminal Sequence
6%
Precursor
6%
Amino Terminal Sequence
6%
Alternative RNA Splicing
6%
Mucin
6%