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UnknownK-Carrageenan Stimulates Pre-Osteoblast Proliferation and Osteogenic Differentiation: A Potential Factor for the Promotion of Bone Regeneration?
Not available
S-EPMC8541607 | biostudies-literature
UnknownMolecular dynamics investigation of the ω-current in the Kv1.2 voltage sensor domains.
Not available
S-EPMC3260662 | biostudies-literature
UnknownThe FMO complex in a glycerol-water mixture.
Not available
S-EPMC3714603 | biostudies-literature
UnknownCytoplasmic domain filter function in the mechanosensitive channel of small conductance.
Not available
S-EPMC3127185 | biostudies-literature
UnknownMolecular dynamics study of gating in the mechanosensitive channel of small conductance MscS.
Not available
S-EPMC1304777 | biostudies-literature
UnknownConformational model of the Holliday junction transition deduced from molecular dynamics simulations.
Not available
S-EPMC545448 | biostudies-literature
UnknownExploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase.
Not available
S-EPMC3081669 | biostudies-literature
UnknownEnd-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation.
Not available
S-EPMC1567890 | biostudies-literature
ProteomicsAnalysis of reconstituted tripartite complex supports avidity-based recruitment of Hsp70 by substrate bound J-domain protein
Hsp70 are ubiquitous, versatile molecular chaperones that cyclically interact with substrate protein(s). The initial step requires synergistic interaction of a substrate and a J-domain protein (JDP) cochaperone, via its J-domain, with Hsp70 to stimulate hydrolysis of its bound ATP. This hydrolysis d...
ORGANISM(S): Escherichia coli Saccharomyces cerevisiae (Baker's yeast) 
2024-02-19 | PXD044739 | Pride
Hsc20 Hsp70 atpase cycle Substrate delivery Ssq1 Molecular chaperones 
ProteomicsCharacterization of the diphthamide modification of eEF2 in Arabidopsis thaliana
Diphthamide, a post-translationally modified histidine residue of eukaryotic TRANSLATION ELONGATION FACTOR2 (eEF2), is the human host cell-sensitizing target of diphtheria toxin. Diphthamide biosynthesis depends on the 4Fe-4S-cluster protein Dph1 catalyzing the first committed step, as well as Dph2 ...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2022-08-11 | PXD034873 | Pride
Diphthamide translation elongation factor 2 (eef2) arabidopsis thaliana growth development 
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