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Immunoglobulin binding protein (BiP) forms two types of dimers
Karina New
, Miguel I.A. Lagos-Espinoza
,
Nathalie Casanova-Morales
, Roi Asor
, John William Young
, Zahra Alavi
, Christian A.M. Wilson
Faculty of Liberal Arts
Research output
:
Contribution to journal
›
Article
›
peer-review
1
Scopus citations
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Keyphrases
Immunoglobulin-binding Protein
100%
Binding Protein
100%
Proteins Form
100%
Single Molecule
28%
Nucleotide-binding Domain
28%
Substrate-binding Domain
28%
Protein Concentration
28%
Protein Dimerization
28%
Adenosine Triphosphate
28%
High Concentration
14%
Unfolded Protein Response
14%
Oligomerization
14%
High Affinity
14%
Occupancy
14%
Polypeptide
14%
Binding Site
14%
Dissociation Constant
14%
Peptide Substrate
14%
Protein Function
14%
Protein Transport
14%
Binding Affinity
14%
Protein Folding
14%
Adenosine
14%
Concentration-dependent
14%
Enzymatic Assay
14%
Protein Monomer
14%
Affinity Kinetics
14%
Mechanical Activity
14%
Low Affinity
14%
Protomers
14%
Molecular Chaperone
14%
Dimer Dissociation
14%
Protein Regulation
14%
Thio
14%
Biphasic Behavior
14%
Triphosphate
14%
INIS
proteins
100%
dimers
100%
immunoglobulins
100%
concentration
30%
nucleotides
30%
peptides
23%
substrates
23%
affinity
23%
interactions
15%
molecules
15%
transport
7%
stability
7%
regulations
7%
dissociation
7%
kinetics
7%
monomers
7%
ozone
7%
adp
7%
polypeptides
7%
adenosine
7%
Biochemistry, Genetics and Molecular Biology
Binding Immunoglobulin Protein
100%
Binding Protein
100%
Binding Domain
50%
Nucleotide
50%
Peptide
37%
Adenosine Triphosphate
25%
Protein Dimer
25%
Oligomerization
12%
Binding Site
12%
Enzyme Activity
12%
Protein Function
12%
Dissociation Constant
12%
Binding Affinity
12%
Protein Folding
12%
Transport Protein
12%
Adenosine Diphosphate
12%
Protomer
12%
Adenosine
12%
Chaperone
12%