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María Gabriela Álvarez-Rodríguez,Matías Estaras,Felipe Hornos et al. María Gabriela Álvarez-Rodríguez et al.
Our model compound can hamper the pathological state (SG formation) triggered by this IDP, and indicates that the search for potential inhibitors of disordered proteins could be further extended to bioactive natural compounds.
David De Sancho,Xabier Lopez David De Sancho
Biomolecular condensates often form through the self-assembly of disordered proteins with low-complexity sequences. In these polypeptides, the aromatic amino acids phenylalanine and tyrosine act as key 'sticker' residues, driving the cohesion of dense phases.
Zhitao Cui,Cong Lin,Huiying Zhao et al. Zhitao Cui et al.
In striking contrast, tardigrades (phylum Tardigrada) routinely endure exposures beyond 5 kGy by deploying a multifaceted defense repertoire that includes genome-shielding proteins such as damage suppressor (Dsup) and Tardigrade DNA-Repair protein 1 (TDR1), families of intrinsically disordered proteins
Uroš Zavrtanik,Jurij Lah,San Hadži Uroš Zavrtanik
This has important implications for understanding the net energetic balance in protein folding and the interactions of intrinsically disordered proteins that undergo α-helix folding upon binding.
Lenette F Kjaer,Francesco S Ielasi,Thomas Winbolt et al. Lenette F Kjaer et al.
Intrinsically disordered proteins (IDPs) often undergo folding-upon-binding to their partners via short linear motifs, typically 5-15 amino acids in length.
Michael Phillips,Andrea Holla,Magdalena Wojtas et al. Michael Phillips et al.
Intrinsically disordered proteins (IDPs) are often rich in charged residues, and electrostatic interactions have a pronounced effect on their conformational distributions, interactions and functions.
Pablo L Garcia,Jerelle A Joseph Pablo L Garcia
However, how condensate viscoelastic responses are encoded in the chemistries of their constituents-such as intrinsically disordered proteins (IDPs)-are not well understood.
Thomas R Sisk,Simon Olsson,Paul Robustelli Thomas R Sisk
The biological functions of intrinsically disordered proteins (IDPs) are governed by the conformational states they adopt in solution and the kinetics of transitions between these states.
Fatima Tu Zahra,Hooreen Kayani,Samra Noreen et al. Fatima Tu Zahra et al.
Synucleins α, β, and γ are inherently disordered proteins that play essential roles in neuronal physiology and are increasingly recognized as key players in neurodegenerative disease mechanisms.
Jules Marien,Chantal Prévost,Sophie Sacquin-Mora Jules Marien
The biological importance of intrinsically disordered proteins (IDPs) has been established for over two decades, yet these systems remain difficult to characterize, as they are better described by conformational ensembles instead of a single reference structure for their folded counterparts.
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