Preferencje help
Polish version English version Język
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 6

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych:  oligomerization
help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
1

Heat and SDS insensitive NDK dimers are largely stabilised by hydrophobic interaction to form functional hexamer in Mycobacterium smegmatis

100%
Arumugam M., Ajitkumar P.
Acta Biochimica Polonica
|
2013
|
tom 60
|
nr 2
 The primary structure and function of nucleoside diphosphate kinase (NDK), a substrate non-specific enzyme involved in the maintenance of nucleotide pools is also implicated to play pivotal roles in many other cellular processes. NDK is conserved from bacteria to human and forms a homotetramer or hexamer to exhibit its biological activity. However, the nature of the functional oligomeric form of the enzyme differs among different organisms. The functional form of NDKs from many bacterial systems, including that of the human pathogen, Mycobacterium tuberculosis (MtuNDK), is a hexamer, although some bacterial NDKs are tetrameric in nature. The present study addresses the oligomeric property of MsmNDK and how a dimer, the basic subunit of a functional hexamer, is stabilized by hydrogen bonds and hydrophobic interactions. Homology modeling was generated using the three-dimensional structure of MtuNDK as a template; the residues interacting at the monomer-monomer interface of MsmNDK were mapped. Using recombinant enzymes of wild type, catalytically inactive mutant, and monomer-monomer interactive mutants of MsmNDK, the stability of the dimer was verified under heat, SDS, low pH, and methanol. The predicted residues (Gln17, Ser24 and Glu27) were engaged in dimer formation, however the mutated proteins retained the ATPase and GTPase activity even after introducing single (MsmNDK- Q17A, MsmNDK-E27A, and MsmNDK-E27Q) and double (MsmNDK-E27A/Q17A) mutation. However, the monomer-monomer interaction could be abolished using methanol, indicating the stabilization of the monomer-monomer interaction by hydrophobic interaction.
2
Content available remote

Melatonin influences the expression and oligomerization of amylin in rat INS-1E cells

84%
Jung E.-M., Yoo Y.-M., Jeung E.-B.
Journal of Physiology and Pharmacology
|
2019
|
tom 70
|
nr 5
3

Camptothecin induces the transit of FasL trimers to the cell surface in apoptosis HEp-2 cells

84%
Meza-Lamas E., Bollain-Y-Goytia J.J., Ramirez-Sandoval R., Sanchez-Rodriguez S. H., Lopez-Robles E., Avaloz-Diaz E., Herrera-Esparza R.
Cellular and Molecular Biology Letters
|
2006
|
tom 11
|
nr 3
Fas ligand (L) is a membrane protein from the tumor necrosis factor (TNF) family. It induces apoptosis upon contact with its Fas/CD95/APO1 receptor. Trimerization of FasL on the surface of effector cells is essential in the binding of the Fas trimer of the target cells. The receptor then recruits an adaptor and caspase-like proteins which lead apoptosis. This paper reports on the fate of FasL in HEp-2 cells committed to apoptosis by induction with campthotecin. Our main results demonstrated that in non-apoptotic cells, FasL aggregates in the cytoplasm forming trimers of 120 kDa. Apoptosis increases the trimeric FasL species, but also induces its dissociation into monomers of 35 kDa. In conclusion, camptothecin appears to perturb the Fas and FasL segregation in the cytoplasm by promoting the transit of FasL to the cell surface, thus fostering a process of autocrine or paracrine apoptosis. FasL is trimerized prior to Fas/FasL complex formation, and after apoptosis, FasL undergoes an intense turnover.
4

Congo red interaction with alpha-proteins

84%
Sereikaite J., Bumelis V. A.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr 1
The ability of Congo red to form complexes with α-proteins, human growth hormone and human interferon-α2b, was found by absorption difference spectroscopy. A human growth hormone-Congo red complex was isolated by gel-permeation chromatography, and its visible absorption spectrum was registered in comparison to free dye. The ability of Congo red to induce dimerization of human growth hormone was demonstrated using chemical cross-linking agents 1,3,5-triacryloyl-hexahydro-s-triazine and ethylene glycol bis(succinimidylsuccinate).
5
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

3D domain swapping – implications for conformational disorders and ways of control

67%
Jaskolski M.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
|
2011
|
tom 92
|
nr 1
6

Redox potential influences oligomerization state of annexin 1 [AnnAt1] from Arabidopsis thaliana

67%
Gorecka K. M., Konopka-Postupolska D., Henning J., Pikula S.
Biological Letters
|
2005
|
tom 42
|
nr 2 Spec.Vol.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.