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Iskalni niz: "polno besedilo" AND "organizacija" (Kemijski inštitut) .

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1.
Cryo-EM structures of a protein pore reveal a cluster of cholesterol molecules and diverse roles of membrane lipids
Gašper Šolinc, Marija Srnko, Franci Merzel, Ana Crnković, Mirijam Kozorog, Marjetka Podobnik, Gregor Anderluh, 2025, izvirni znanstveni članek

Povzetek: The structure and function of membrane proteins depend on their interactions with lipids that constitute membranes. Actinoporins are α-pore-forming proteins that bind preferentially to sphingomyelin-containing membranes, where they oligomerize and form transmembrane pores. Through a comprehensive cryo-electron microscopic analysis of a pore formed by an actinoporin Fav from the coral Orbicella faveolata, we show that the octameric pore interacts with 112 lipids in the upper leaflet of the membrane, reveal the roles of lipids, and demonstrate that the actinoporin surface is suited for binding multiple receptor sphingomyelin molecules. When cholesterol is present in the membrane, it forms a cluster of four molecules associated with each protomer. Atomistic simulations support the structural data and reveal additional effects of the pore on the lipid membrane. These data reveal a complex network of protein-lipid and lipid-lipid interactions and an underrated role of lipids in the structure and function of transmembrane protein complexes.
Objavljeno v DiRROS: 12.05.2025; Ogledov: 66; Prenosov: 33
.pdf Celotno besedilo (2,01 MB)
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Bubble trouble : quantifying the effects of bubbles on the electrochemical interface
Anja Logar, Dževad Kozlica, Ožbej Vodeb, Miran Gaberšček, Nejc Hodnik, Dušan Strmčnik, 2025, izvirni znanstveni članek

Objavljeno v DiRROS: 06.05.2025; Ogledov: 132; Prenosov: 53
.pdf Celotno besedilo (3,09 MB)
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Oxidative events in a double helix system promote the formation of kinetically trapped G-quadruplexes
Simon Aleksič, Peter Podbevšek, Janez Plavec, 2025, izvirni znanstveni članek

Objavljeno v DiRROS: 05.05.2025; Ogledov: 132; Prenosov: 51
.pdf Celotno besedilo (1,42 MB)
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Efficient and selective biosynthesis of a precursor-directed FK506 analogue : paving the way for click chemistry
Dušan Goranovič, Branko Jenko, Barbara Ramšak, Ajda Podgoršek Berke, Leon Bedrač, Jaka Horvat, Martin Šala, Damjan Makuc, Guilhermina M. Carriche, Luana Silva, Aleksandra Lopez Krol, Alen Pšeničnik, Maria Beatriz Duran Alonso, Martina Avbelj, Stojan Stavber, Janez Plavec, Tim Sparwasser, Rolf Müller, Gregor Kosec, Štefan Fujs, Hrvoje Petković, 2025, izvirni znanstveni članek

Povzetek: The medically important immunosuppressant FK506 is a structurally complex macrolactone biosynthesized by a combined polyketide synthase and a nonribosomal peptide synthetase enzyme complex. Its acyltransferase domain 4 (AT4) selects an unusual extender unit, resulting in an allyl moiety on carbon 21 of the macrolactone backbone. Based on the AT4 domain, chemobiosynthetic processes have been developed that enable the introduction of diverse moieties at the carbon 21 position. However, the novel moieties that were introduced into the polyketide backbone are chemically inert. Reported here is a novel and efficient chemobiosynthetic approach that ensures high titer of an FK506 analogue containing a propargyl moiety. The novel FK506 analogue displays lower immunosuppression activity than FK506 with significantly reduced cytotoxicity. More importantly, the propargyl moiety contains a terminal alkyl group, which makes click chemistry reactions possible; this approach may potentially be translated to other medically important drugs of polyketide origin.
Objavljeno v DiRROS: 15.04.2025; Ogledov: 158; Prenosov: 44
.pdf Celotno besedilo (3,26 MB)

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