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The importin-beta P446L dominant-negative mutant protein loses RanGTP binding ability and blocks the formation of intact nuclear envelope.
The P446L mutant importin-beta does not exert its dominant-negative effect on nuclear protein import and has no effect on mitotic spindle-related functions and chromosome segregation, however, it interferes with nuclear envelope formation during mitosis-to-interphase transition, revealing a novel function of import in-beta.
Decreased serum and red blood cell kynurenic acid levels in Alzheimer's disease
Cell-penetrating peptide exploited syndecans.
Genetic Polymorphisms of NOD1 and IL‐8, but not Polymorphisms of TLR4 Genes, Are Associated with Helicobacter pylori‐Induced Duodenal Ulcer and Gastritis
The relationship between NOD1 and IL‐8 genetic polymorphisms and the development of H. pylori‐induced gastritis and duodenal ulcer (DU) as compared with TLR4 polymorphisms was evaluated.
Clinical associations of autoantibodies to human muscarinic acetylcholine receptor 3(213-228) in primary Sjogren's syndrome.
Although it is significantly more common in pSS than in the comparison groups, anti-m3AChR(213-228) positivity is not exclusive to pSS.
A peptide of human muscarinic acetylcholine receptor 3 is antigenic in primary Sjogren's syndrome.
A hemagglutinin-based multipeptide construct elicits enhanced protective immune response in mice against influenza A virus infection.
Conformational effect of phosphorylation on T cell receptor/CD3 zeta-chain sequences.
- I. Laczkó, M. Hollósi, E. Vass, Z. Hegedüs, Ė. Monostori, G. Tóth
- Biology, ChemistryBiochemical and biophysical research…
- 26 January 1998
Evidence that phosphorylation can alter the secondary structure of the peptides is given and the most significant--alpha-helix to beta-sheet--conformational change was observed in the case of the zeta(138-155) peptide sequence which may be relevant to recognition by Src homology 2 (SH2) domains of signaling proteins.
Cooperation between a salt bridge and the hydrophobic core triggers fold stabilization in a Trp-cage miniprotein.
- P. Hudáky, Pál Stráner, V. Farkas, G. Váradi, G. Tóth, A. Perczel
- Biology, ChemistryBiochemistry
- 22 January 2008
A systematic investigation of structural factors influencing the stability of Tc5b by solving its solution structure in different environments, varying temperature, and pH results in a new variant, Tc6b, differing only by a methylene group from T c5b, in which both key interactions are optimized simultaneously.