Finding the right terms to bind is a difficult task but the effort to achieve terminology bindings may be reduced with the help of the described approach.
Finding the right terms to bind is a difficult task but the effort to achieve terminology bindings may be reduced with the help of our methods and tools.
Some of these studies have demonstrated that the PIP2-sequestering basic peptide (palpeptide) competes with the hDAT N-term to bind PIP2-enriched liposomes and that cell perfusion with palpeptide impairs AMPH-induced DA efflux but not the regular DA uptake.
The binding properties of MTR with histone proteins have been examined from the perspective of the current proposition from our laboratory to classify small DNA binding molecules in terms of their ability to bind chromosomal DNA alone (single binding mode) or both histones and chromosomal DNA (dual binding mode) [ 2, 3].
Unexpectedly, a C-terminus truncated form of EPRS, termed EPRSN1, was found to bind GAIT target mRNAs and prevent binding of the functional GAIT complex, thereby acting as a dominant-negative inhibitor of GAIT activity.
One compound, termed 3144, was found to bind to RAS proteins using microscale thermophoresis, nuclear magnetic resonance spectroscopy, and isothermal titration calorimetry and to exhibit lethality in cells partially dependent on expression of RAS proteins.
The relevance of this complex to MAL regulation, in terms of its competence to bind import factors or to recruit Crm1, remains unclear.
Connections to external terminology sources like SNOMED CT and UMLS were included so that the effort required to bind terms with the help of external terminology sources was reduced compared to manual lookup.
Viral structural proteins typically use one or more short peptide motifs, termed 'late assembly domains', to bind and recruit early-acting ESCRT factors or ESCRT-associated E3 ubiquitin ligases to sites of viral assembly and budding.
This water phase called structured water (term now preferred to "bound water", generally used for "dry" powders) corresponds to macromolecule-associated water [ 17].
Specialized proteins termed "nannies" have been shown to bind to and protect IDPs from ubiquitin-independent 20S proteasomal degradation.
