|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1994-9-27
|
|
pubmed:abstractText |
Surface plasmon resonance is emerging as the method of choice to study biomolecular interactions between macromolecules because it allows the observation of real-time kinetics for these processes. The method is currently being applied to the study of antigen-antibody interactions, protein-DNA interactions, receptor SH2 domain-phosphotyrosine peptide interactions and receptor-ligand interactions.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
B
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0958-1669
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
5
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
389-95
|
|
pubmed:dateRevised |
2000-12-18
|
|
pubmed:meshHeading |
pubmed-meshheading:7765171-Antigen-Antibody Reactions,
pubmed-meshheading:7765171-Biosensing Techniques,
pubmed-meshheading:7765171-DNA-Binding Proteins,
pubmed-meshheading:7765171-Kinetics,
pubmed-meshheading:7765171-Ligands,
pubmed-meshheading:7765171-Models, Chemical,
pubmed-meshheading:7765171-Nucleic Acids,
pubmed-meshheading:7765171-Protein Binding,
pubmed-meshheading:7765171-Proteins,
pubmed-meshheading:7765171-Receptors, Cytoplasmic and Nuclear
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions.
|
|
pubmed:affiliation |
Laboratory of Cellular Biochemistry, PRI/DynCorp, NCI-Frederick Cancer Research and Development Center, Maryland 21702-1201.
|
|
pubmed:publicationType |
Journal Article
|
