Results 221 to 230 of about 49,644 (261)
Calmodulin binding is required for calcium mediated TRPA1 desensitization. [PDF]
Sanders JH +6 more
europepmc +1 more source
Oriented Surface Immobilization of Antibodies Using Enzyme-Mediated Site-Specific Biotinylation for Enhanced Antigen-Binding Capacity. [PDF]
Beitello E +5 more
europepmc +1 more source
The study of plasmodesmal biology using proximity labeling technologies. [PDF]
Li Z, Aung K.
europepmc +1 more source
Proximity Labeling and SILAC-Based Proteomic Approach Identifies Proteins at the Interface of Homotypic and Heterotypic Cancer Cell Interactions. [PDF]
Saner N +7 more
europepmc +1 more source
HCR-Proxy resolves site-specific proximal RNA proteomes at subcompartmental nanoscale resolution
Trupej A +14 more
europepmc +1 more source
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The Journal of Organic Chemistry, 2004
Inhibition of the 90 kDa heat shock proteins (Hsp90) represents a promising new chemotherapeutic approach for the treatment of several cancers. Hsp90 is essential to the survival of cancer cells and is inhibited by members of the ansamycin family of antibiotics.
Randell C, Clevenger +3 more
openaire +2 more sources
Inhibition of the 90 kDa heat shock proteins (Hsp90) represents a promising new chemotherapeutic approach for the treatment of several cancers. Hsp90 is essential to the survival of cancer cells and is inhibited by members of the ansamycin family of antibiotics.
Randell C, Clevenger +3 more
openaire +2 more sources
Molecular Immunology, 1982
Purified human C3 was biotinylated using the biotinyl-N-hydroxysuccinimide imidoester (BNHS). Depending on the input of BNHS, from three to six molecules of biotin were incorporated per C3 molecule. The biotinyl-C3 retained over 90% of its specific hemolytic activity and when bound to sheep erythrocytes maintained its ability to adhere to human C3b ...
M, Berger +5 more
openaire +3 more sources
Purified human C3 was biotinylated using the biotinyl-N-hydroxysuccinimide imidoester (BNHS). Depending on the input of BNHS, from three to six molecules of biotin were incorporated per C3 molecule. The biotinyl-C3 retained over 90% of its specific hemolytic activity and when bound to sheep erythrocytes maintained its ability to adhere to human C3b ...
M, Berger +5 more
openaire +3 more sources

