Characterization of multimetric variants of ubiquitin carboxyl-terminal hydrolase L1 in water by small-angle neutron scattering

Here, we illustrated that the morphological structures of ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) variants and Parkinson’s disease (PD) exhibit good pathological correlation by a small-angle neutron scattering (SANS). UCH-L1 is a neuro-specific multiple functional enzyme, deubiquitinating,...

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Veröffentlicht in:	Biochemical and biophysical research communications 2006-01, Vol.339 (2), p.717-725
Hauptverfasser:	Naito, Sachio, Mochizuki, Hideki, Yasuda, Toru, Mizuno, Yoshikuni, Furusaka, Michihiro, Ikeda, Susumu, Adachi, Tomohiro, Shimizu, Hirohiko M., Suzuki, Junichi, Fujiwara, Satoru, Okada, Tomoko, Nishikawa, Kaori, Aoki, Shunsuke, Wada, Keiji
Format:	Artikel
Sprache:	eng
Schlagworte:	60 APPLIED LIFE SCIENCES Circular Dichroism DIMERS DISEASES HAZARDS Humans LIGASES Models, Molecular MONOMERS MUTATIONS NEUTRON DIFFRACTION Parkinsonism Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism SMALL ANGLE SCATTERING Small-angle neutron scattering STABILIZATION Structure in water Ubiquitin carboxyl-terminal hydrolase L1 Ubiquitin Thiolesterase - chemistry Ubiquitin Thiolesterase - genetics Ubiquitin Thiolesterase - isolation & purification Ubiquitin Thiolesterase - metabolism Water - chemistry
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