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- Publications
- Influence
Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils
- M. Ahmed, J. Davis, +6 authors S. Smith
- Chemistry, Medicine
- Nature Structural &Molecular Biology
- 11 April 2010
The amyloid-β1–42 (Aβ42) peptide rapidly aggregates to form oligomers, protofibils and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's disease. We show that… Expand
Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus
- Z. Chen, S. Yoshida, +7 authors H. Kiyama
- Biology, Medicine
- The Journal of neuroscience : the official…
- 1 July 1995
A novel murine cDNA which encodes a protein designated neuropsin was cloned. Northern and in situ hybridization analyses demonstrated that neuropsin mRNA is expressed specifically in the limbic… Expand
Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers.
- S. Smith, D. Song, S. Shekar, M. Groesbeek, M. Ziliox, S. Aimoto
- Chemistry, Medicine
- Biochemistry
- 10 May 2001
The hydrophobic transmembrane domain of glycophorin A contains a sequence motif that mediates dimerization in membrane environments. Long-range interhelical distance measurements using magic angle… Expand
Ribosome modulation factor: stationary growth phase-specific inhibitor of ribosome functions from Escherichia coli.
- A. Wada, K. Igarashi, S. Yoshimura, S. Aimoto, A. Ishihama
- Biology, Medicine
- Biochemical and biophysical research…
- 14 September 1995
Ribosome modulation factor (RMF) is an Escherichia coli protein associated with 100S ribosome dimers, which are formed at stationary growth phase or in slowly growing cells. RMF either purified from… Expand
Site‐Specific Phosphorylation of Neurofilament‐L Is Mediated by Calcium/Calmodulin‐Dependent Protein Kinase II in the Apical Dendrites During Long‐Term Potentiation
- R. Hashimoto, Y. Nakamura, +7 authors M. Takeda
- Biology, Medicine
- Journal of neurochemistry
- 1 July 2000
Abstract : Neurofilament‐L (NF‐L), one subunit of the neuronal intermediate filaments, is a major element of neuronal cytoskeletons. The dynamics of NF‐L are regulated by phosphorylation of its head… Expand
Comparison of the free and DNA-complexed forms of the DMA-binding domain from c-Myb
- K. Ogata, S. Morikawa, +9 authors Y. Nishimura
- Chemistry, Medicine
- Nature Structural Biology
- 1 April 1995
The DNA-binding domain of c-Myb consists of three imperfect tandem repeats (R1, R2 and R3). The three repeats have similar overall architectures, each containing a helix-turn-helix variation motif.… Expand
Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core.
- K. Ogata, H. Hojo, +5 authors Y. Nishimura
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 15 July 1992
The DNA-binding domain of the c-myb protooncogene product consists of three imperfect tandem repeats of 51 or 52 amino acids, each of which contains three conserved tryptophans, spaced 18 or 19 amino… Expand
Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.
- T. Sato, P. Kienlen-Campard, +7 authors S. Smith
- Chemistry, Medicine
- Biochemistry
- 2 May 2006
Amyloid fibrils associated with Alzheimer's disease and a wide range of other neurodegenerative diseases have a cross beta-sheet structure, where main chain hydrogen bonding occurs between… Expand
Hinge and chromoshadow of HP1α participate in recognition of K9 methylated histone H3 in nucleosomes.
- Yuichi Mishima, M. Watanabe, +9 authors I. Suetake
- Biology, Medicine
- Journal of molecular biology
- 9 January 2013
The majority of the genome in eukaryotes is packaged into transcriptionally inactive chromatin. Heterochromatin protein 1 (HP1) is a major player in the establishment and maintenance of… Expand
Transmembrane interactions in the activation of the Neu receptor tyrosine kinase.
- S. Smith, C. Smith, S. Shekar, O. Peersen, M. Ziliox, S. Aimoto
- Chemistry, Medicine
- Biochemistry
- 30 July 2002
The Neu receptor tyrosine kinase is constitutively activated by a single amino acid change in the transmembrane domain of the receptor. The mutation of Val664 to glutamate or glutamine induces… Expand