Zobrazeno 1 - 10
of 27
pro vyhledávání: '"V M, Tischenko"'
Publikováno v:
Molecular Immunology. 92:199-210
Human IgG4 (hIgG4) has weak pro-inflammatory activity. The structural basis for this is still unclear. Here a 3D model of myeloma hIgG4 was created at ∼3nm resolution using electron microscopy (EM) with negative staining and single-particle 3D reco
Autor:
V. M. Tischenko
Publikováno v:
Biochemistry (Moscow). 80:21-30
A long-lived metastable minor fraction has been detected and characterized in myeloma protein IgG4 MAM by hydro- and thermodynamic methods. The sedimentation constants of the minor and the major protein fractions are different. The stability of the t
Autor:
D. A. Prohorov, V. M. Tischenko
Publikováno v:
Biophysics. 58:460-464
Several experimental methods (circular dichroism, viscosity, intrinsic fluorescence, and fluorescence labeling) were used to study the conformational folding/unfolding transitions in a compact monomeric form of the Caf113-149 subunit under the action
Autor:
M. A. Timchenko, V. M. Tischenko
Publikováno v:
Biochemistry (Moscow). 78:667-673
Fc fragments (hFc) of human myeloma IgG2 proteins LOM and SIN having core hinge (Cys-Cys-Val-Glu-Cys-Pro-Pro-Cys) were first obtained by a modified proteolytic procedure. The thermostability of CH2 domains inside of standard Fc, hFc fragments, and in
Autor:
Xiaodi Yu, Stefan D. Knight, V. M. Tischenko, Anton V. Zavialov, Sheila MacIntyre, Elham Moslehi-Mohebi, L.J. Fooks, G. Askarieh
Publikováno v:
Journal of Molecular Biology. 417:294-308
The chaperone/usher pathway assembles surface virulence organelles of Gram-negative bacteria, consisting of fibers of linearly polymerized protein subunits. Fiber subunits are connected through 'donor strand complementation': each subunit completes t
Autor:
V. M. Tischenko
Publikováno v:
Molecular Biology. 45:967-975
Isolated constant domains of two Bence Jones proteins, VAD and BIR, are able to form amyloid fibrils, but only the first one retains this feature within the intact protein. The conformation and stability of these proteins were studied using scanning
Autor:
V. M. Tischenko
Publikováno v:
Biophysics. 56:602-605
It is shown by several methods (circular dichroism, viscometry, intrinsic fluorescence, and fluorescence of labels) that, as in the case of small globular proteins, the folding-unfolding transition in the Caf113–149 subunit under the action of two
Autor:
V M, Tischenko
Publikováno v:
Molekuliarnaia biologiia. 48(3)
Human myeloma immunoglobulin second subclass LOM and SIN, their Fc fragment and firstly obtained hFc fragment in which there is not only low portion of the hinge region, but also its core portion (Cys-Cys-Val-Glu-Cys-Pro-Pro-Cys), have been studied b
Autor:
Sheila MacIntyre, Bjørn Olav Brandsdal, Johan Åqvist, Vladimir P. Zav'yalov, Stefan D. Knight, L.J. Fooks, V. M. Tischenko, Anton V. Zavialov
Publikováno v:
Biochemical Journal. 389:685-694
Periplasmic chaperone/usher machineries are used for assembly of filamentous adhesion organelles of Gram-negative pathogens in a process that has been suggested to be driven by folding energy. Structures of mutant chaperone–subunit complexes reveal
Publikováno v:
Immunology Letters. 90:43-47
Earlier, the electron microscopy and hydrodynamic studies revealed the transformation of the globule-like form of the human (h) IgG3 Kus hinge into a rod-like shape under non-denaturing perturbations [Eur. J. Biochem. 190 (1990) 393]. In this work, i