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Kanały jonowe aktywowane przez cykliczne nukleotydy

100%
Sobierajska K., Fabczak S.
Kosmos
|
2003
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vol. 52
|
issue 2-3
185-201
EN
Summary Cyclic nucleotide-gated (CNG) channels are a novel class of cation channels first identified in retinal photoreceptor cells and subsequently found also in other sensory and nonsensory cells. CNG channels form heterotetrameric complexes consisting of two or three different types of channel subunits. Six different genes encoding CNG channels, four A subunits (A1 to A4) and two B subunits (B1and B3), give rise to three different channel types. Functionally,CNGchannels belong to the class of ligand-gated channels, which are activated by binding of ligand (cGMP) to a domain in the carboxyl terminal region, but structurally they are similar to voltage-dependent K+ channels. All channel subunits include six transmembrane segments (S1 to S6), a voltage-sensor motif (S4), a pore region (P) and a cGMP-binding domain. These channels are nonselective cation channels that do not discriminate well between monovalent and divalent ions and even pass divalent cations, in particular Ca2+. Activity of CNG channel is modulated by Ca2+/ calmodulin and by phosphorylation. Other factors may also be involved in channel regulation.
2
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Białka opiekuńcze - "molekularne przyzwoitki" w fałdowaniu białek

81%
Bregier C., Fabczak H., Fabczak S.
Kosmos
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2007
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vol. 56
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issue 3-4
409-419
EN
Proteins must be folded into their correct three-dimensional conformation in order to attain biological function. Conversely, protein aggregation and misfolding are primary contributors to many devastating "conformational" diseases. Proteins are synthesized and folded continuously. The last of these processes is greatly assisted by molecular chaperones. They are a group of structurally diverse and mechanistically distinct proteins that either promote folding or prevent the aggregation of other proteins. Proteins that can be classified as molecular chaperones can be divided into two groups: (a) ribosome-associated chaperons responsible for co-traslational folding of polypetides and (b) cytoplasmic molecular chaperones including Hsp90, Hsp70/Hsp40 and chaperonin CCT in eukaryotic cells. Prokaryotic cells posses DnaK/DnaJ system and GroEL/GroES, respectively. This review focuses on the emerging role of molecular chaperones in protein quality control in eukaryotic and prokaryotic cells.
3
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Dimer αγ białka G - cząsteczka sygnałowa

81%
Fabczak H., Sobierajska K., Fabczak S.
Kosmos
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2004
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vol. 53
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issue 3-4
355-372
EN
Summary The extracellular signals received by receptors with seven membrane-spanning regions that activate the G proteins, are routed to several distinct intracellular pathways. The G proteins consist of two functional units, Gα subunit, that binds guanine nucleotides and Gβγ dimer that functions as a single unit. The regulation of signal transduction by the Gβγ complex at different protein interfaces: subunit - subunit, receptor - G protein, and Gβγ - effector, are reviewed. Gβγ dimer regulates over twelve cellular effectors including phospholipase-β, adenyl cyclases, ion channels and G-protein coupled receptor kinases, which control a broad range of cellular processes.
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