Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Hsiang-Kai Lin"'
Autor:
Hsiang-Kai Lin, Jennifer C. Boatz, Inge E. Krabbendam, Ravindra Kodali, Zhipeng Hou, Ronald Wetzel, Amalia M. Dolga, Michelle A. Poirier, Patrick C. A. van der Wel
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Huntington's disease is caused by a polyglutamine stretch expansion in the first exon of huntingtin. Here, the authors use infrared spectroscopy and solid-state NMR and show that polymorphic huntingtin exon1 fibres differ in their flanking regions bu
Externí odkaz:
https://doaj.org/article/6d1f8de6f3eb481d8704dc203117b49c
Mechanistic Study of Apatite Formation on Bioactive Glass Surface Using Solid-State NMR Spectroscopy
Autor:
Hsiang-Kai Lin, 林祥凱
93
The molecular mechanism of apatite formation on bioactive glass surface is studied using the techniques of XRD, EDX, SEM, FT-IR, and solid-state NMR. Using the sol-gel method a bioactive glass system containing glass beads of 2 to 3 microns i
The molecular mechanism of apatite formation on bioactive glass surface is studied using the techniques of XRD, EDX, SEM, FT-IR, and solid-state NMR. Using the sol-gel method a bioactive glass system containing glass beads of 2 to 3 microns i
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/93613631291419817094
Autor:
Józef R. Lewandowski, Jonathan M. Lamley, Jennifer C. Boatz, Abhishek Mandal, Gábor Magyarfalvi, Karunakar Kar, Hsiang Kai Lin, Ronald Wetzel, Patrick C.A. van der Wel, Cody L. Hoop
Publikováno v:
Proceedings of the National Academy of Sciences. 113:1546-1551
Polyglutamine expansion within the exon1 of huntingtin leads to protein misfolding, aggregation, and cytotoxicity in Huntington's disease. This incurable neurodegenerative disease is the most prevalent member of a family of CAG repeat expansion disor
Autor:
Michelle A. Poirier, Patrick C.A. van der Wel, Ravindra Kodali, Zhipeng Hou, Jennifer C. Boatz, Amalia M. Dolga, Inge Krabbendam, Ronald Wetzel, Hsiang Kai Lin
Publikováno v:
Nature Communications, 8:15462. Nature Publishing Group
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Nature Communications
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Nature Communications
Polyglutamine expansion in the huntingtin protein is the primary genetic cause of Huntington's disease (HD). Fragments coinciding with mutant huntingtin exon1 aggregate in vivo and induce HD-like pathology in mouse models. The resulting aggregates ca
Publikováno v:
Biochemistry. 51:7367-7382
Differentiation of binding accurate DNA replication polymerases over error prone DNA lesion bypass polymerases is essential for the proper maintenance of the genome. The hyperthermophilic archaeal organism Sulfolobus solfataricus (Sso) contains both
Publikováno v:
Biochemistry. 50:5379-5390
DNA replication polymerases have the inherent ability to faithfully and rapidly copy a DNA template according to precise Watson-Crick base pairing. The primary B-family DNA replication polymerase (Dpo1) in the hyperthermophilic archaeon, Sulfolobus s
Publikováno v:
Nucleic Acids Research
DNA polymerases are essential enzymes in all domains of life for both DNA replication and repair. The primary DNA replication polymerase from Sulfolobus solfataricus (SsoDpo1) has been shown previously to provide the necessary polymerization speed an
Autor:
Michelle A. Poirier, Karunakar Kar, Patrick C.A. van der Wel, Cody L. Hoop, Ronald Wetzel, Zhipeng Hou, Hsiang Kai Lin
Publikováno v:
Biochemistry
In Huntington's disease, expansion of a polyglutamine (polyQ) domain in the huntingtin (htt) protein leads to misfolding and aggregation. There is much interest in the molecular features that distinguish monomeric, oligomeric, and fibrillar species t
Publikováno v:
Biophysical Journal. 106(2)
Most organisms encode for multiple DNA polymerases with similar substrate affinities, but vastly different fidelities. Proper genomic maintenance by the high fidelity (PolB1) and lesion bypass polymerases (PolY) from Sulfolobus solfataricus involves
Publikováno v:
Journal of molecular biology. 425(23)
The assembly and enzymatic ability of the replication DNA polymerase holoenzyme from Sulfolobus solfataricus (Sso) was investigated using presteady-state fluorescence resonance energy transfer assays coupled with functional and structural studies. Ki