Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Victor I. Emelyanenko"'
Autor:
Alisa A. Vologzhannikova, Polina A. Khorn, Marina P. Shevelyova, Alexei S. Kazakov, Victor I. Emelyanenko, Eugene A. Permyakov, Sergei E. Permyakov
Publikováno v:
Biomolecules, Vol 11, Iss 1, p 66 (2021)
Oncomodulin (Ocm), or parvalbumin β, is an 11–12 kDa Ca2+-binding protein found inside and outside of vertebrate cells, which regulates numerous processes via poorly understood mechanisms. Ocm consists of two active Ca2+-specific domains of the EF
Externí odkaz:
https://doaj.org/article/f7cfefda04854669a8f755de7705d82a
Autor:
Alisa A. Vologzhannikova, Victor I. Emelyanenko, Alexey S. Kazakov, Nadezhda I. Borisova, Eugene A. Permyakov
Publikováno v:
Protein & Peptide Letters. 30:108-115
Background: Small Ca2+-binding protein parvalbumin possesses two strong Ca2+/Mg2+- binding sites located within two EF-hand domains. Most parvalbumins have no tryptophan residues, while cod protein contains a single tryptophan residue, which fluoresc
Autor:
Alisa A. Vologzhannikova, Marina P. Shevelyova, Konstantin Denessiouk, Vladimir N. Uversky, Sergei E. Permyakov, Alexander I. Denesyuk, Victor I. Emelyanenko, Alexei S. Kazakov, Polina Khorn, Eugene A. Permyakov
Publikováno v:
Cell calcium. 75
Recently we found two highly conserved structural motifs in the proteins of the EF-hand calcium binding protein family. These motifs provide a supporting scaffold for the Ca2+ binding loops and contribute to the hydrophobic core of the EF-hand domain
Autor:
Andrei P. Zhadan, Yulia S. Lapteva, Alisa A. Vologzhannikova, Alexei S. Kazakov, Sergei E. Permyakov, Victor I. Emelyanenko, Maria E. Permyakova, Eugene A. Permyakov, Ekaterina L. Knyazeva
Publikováno v:
Cell Calcium. 52:366-376
The effect of alpha-N-acetylation (Nt-acetylation) on the properties of parvalbumin (PA), a Ca2+-binding relaxing factor of skeletal muscles and major food allergen, has been explored. Intact PA contains an N-terminal acetyl group which is absent in
Publikováno v:
Photochemistry and Photobiology. 64:316-320
The smooth fluorescence bands of various organic fluorophores of different classes (e. g. indole, tryptophan, tyrosine, phthalimides, quinine sulfate, aminopyridines, acetylanthracenes) in different ionization states of their substituents and dissolv
Publikováno v:
Biophysical Chemistry. 40:181-188
Analysis of the tryptophan fluorescence emission spectra of caldesmon and its 34 kDa C-terminal fragment indicates that all tryptophan residues are located on the surface of the molecule, accessible to solvent. All three tryptophan residues of the 34
Autor:
Edward A. Burstein, Victor I. Emelyanenko, Eugene A. Permyakov, Jean-François Pechere, T.L. Bushueva
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 400:1-16
The influence of pH, temperature and Ca2+-release on the phenylalanyl and tyrosyl fluorescence of muscular parvalbumins from white muscles of hake and carp has been investigated. Within the pH range from 7 to 8, Ca2+-saturated parvalbumins show a con
Autor:
Alexander V. Ostrovsky, Victor I. Emelyanenko, Alexander V. Klimanov, Lina P. Kalinichenko, Eugene A. Permyakov
Publikováno v:
Biophysical chemistry. 30(2)
Decay curves for tryptophan fluorescence of bovine and human α-lactalbumin in different states (metal-free and Ca 2+ or Mg 2+ -loaded states of the native and thermally denatured proteins) have been measured at different wavelengths. The curves are