상위피인용논문
- 조회1,459
Abstract
Sun-Joo Lee‡, So Jung Kim§, In-Kwon Kim¶, Junsang Ko∥, Chang-Sook Jeong‡, Gyung-Hwa Kim‡, Chankyu Park∥, Sa-Ouk Kang¶, Pann-Ghill Suh§, Heung-Soo Lee‡ and Sun-Shin Cha‡,**
‡Beamline Division, Pohang Accelerator Laboratory, Pohang, 790-784, §Department of Life Science, Pohang University of Science and Technology, Pohang, 790-784, ¶Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul, 151-742, and ∥National Creative Research Initiative Center for Behavioral Genetics, Department of Biological Science, Korea Advanced Institute of Science and Technology, Taejon, 305-710, Republic of Korea
** To whom correspondence should be addressed: Beamline Division, Pohang Accelerator Laboratory, Pohang, 790-784, Kyungbuk, Republic of Korea.
Abstract
Human DJ-1 and Escherichia coli Hsp31 belong to ThiJ/PfpI family, whose members contain a conserved domain. DJ-1 is associated with autosomal recessive early onset parkinsonism and Hsp31 is a molecular chaperone. Structural comparisons between DJ-1, Hsp31, and an Archaea protease, a member of ThiJ/PfpI family, lead to the identification of the chaperone activity of DJ-1 and the proteolytic activity of Hsp31. Moreover, the comparisons provide insights into how the functional diversity is realized in proteins that share an evolutionarily conserved domain. On the basis of the chaperone activity the possible role of DJ-1 in the pathogenesis of Parkinson's disease is discussed.
논문정보
- Research article
- 2003년 11월 (BRIC 등록일 2013-06-20)
- 국내 연구진
- 120회 이상 인용된 논문
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