Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Taleh N. Yusifov"'
Publikováno v:
Biophysical Journal. 116:112a-113a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::563c9c96ab8ad97c63ebc4c7e649a3d7
https://doi.org/10.1016/j.bpj.2018.11.637
https://doi.org/10.1016/j.bpj.2018.11.637
Autor:
Riccardo Olcese, Giovanni Battista Luciani, Taleh N. Yusifov, Alan Neely, Nicoletta Savalli, Federica Steccanella
Publikováno v:
Biophysical Journal. 116:113a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4dfcabb9b0cd7f5354e143064bfc9a6f
https://doi.org/10.1016/j.bpj.2018.11.639
https://doi.org/10.1016/j.bpj.2018.11.639
Publikováno v:
Protein Science. 9:325-331
The lipocalin superfamily of proteins functions in the binding and transport of a variety of important hydrophobic molecules. Tear lipocalin is a promiscuous lipid binding member of the family and serves as a paradigm to study the molecular determina
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81ec06bd07c931a6f16063762cfcc3c0
https://doi.org/10.1110/ps.9.2.325
https://doi.org/10.1110/ps.9.2.325
Publikováno v:
Proceedings of the National Academy of Sciences. 105:376-381
Large conductance voltage and Ca 2+ -dependent K + channels (BK Ca ) are activated by both membrane depolarization and intracellular Ca 2+ . Recent studies on bacterial channels have proposed that a Ca 2+ -induced conformational change within special
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec33fb59a1b558ab08c3e1880c62efda
https://doi.org/10.1073/pnas.0705261105
https://doi.org/10.1073/pnas.0705261105
Publikováno v:
Biophysical Journal. 108(2)
Carbon monoxide (CO) is a recognized gasotransmitter that regulates BK channel activity, causing vasodilatory effects. It is thought that CO interacts with the intracellular portion of BK channels, which consists of the assembly of structural domains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55f7701a8731429e52b34b407d6b8a80
Publikováno v:
Biochemistry. 43:12894-12904
Tear lipocalin (TL), a major component of human tears, shows pH-dependent endogenous ligand binding. The structural and conformational changes associated with ligand release in the pH range of 7.5-3.0 are monitored by circular dichroism spectroscopy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::831b7947a089a76c67341e935d6d8d49
https://doi.org/10.1021/bi049076o
https://doi.org/10.1021/bi049076o
Publikováno v:
Biochemistry. 41:8837-8848
Previous studies suggest that the conserved Trp17 on strand A of TL has a role in lipocalin stability and interacts, directly or indirectly, with Ile98 and Phe99 on strand G to influence ligand binding. Here, we determined the proximity of Trp17 to I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b2c47c2bc035bd1ed6f281a1f75f554
https://doi.org/10.1021/bi0121003
https://doi.org/10.1021/bi0121003
Publikováno v:
Biochemistry. 40:14754-14762
The solution structure of human TL was deduced from the position of the emission peaks after site-directed tryptophan fluorescence (SDTF). The fluorescent amino acid tryptophan was sequentially substituted for each native amino acid in the sequence.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12d2b52b645e56f71b4ad73e5e7f7b67
https://doi.org/10.1021/bi0110342
https://doi.org/10.1021/bi0110342
Publikováno v:
Biochemical Journal. 347:815-819
Several lipocalins contain conserved amino acid sequences similar to the phosphodiester bond cleavage domain of sugar non-specific magnesium-dependent nucleases of the Serratia marcescens type. His-89 and Glu-127 of the S. marcescens endonuclease are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e8b92acafc10aff99c6d1d869537a1b6
https://doi.org/10.1042/bj3470815
https://doi.org/10.1042/bj3470815
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1433:307-320
The principal lipid binding protein in tears, tear lipocalin (TL), binds acid and the fluorescent fatty acid analogs, DAUDA and 16-AP at one site TL compete for this binding site. A fluorescent competitive binding assay revealed that apo-TL has a hig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e454b1536e9526532d3e33f1981223f9
https://doi.org/10.1016/s0167-4838(99)00133-8
https://doi.org/10.1016/s0167-4838(99)00133-8