Insights into the amyloid folding problem from solid-state NMR

被引：184
作者：
Tycko, R [1 ]
机构：
[1] NIDDK, Chem Phys Lab, NIH, Bethesda, MD 20892 USA
来源：
BIOCHEMISTRY | 2003年 / 42卷 / 11期
关键词：
D O I：
10.1021/bi027378p
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
[No abstract available]
引用
收藏
页码：3151 / 3159
页数：9
相关论文
共 99 条
[1]   Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils [J].
Antzutkin, ON ;
Balbach, JJ ;
Leapman, RD ;
Rizzo, NW ;
Reed, J ;
Tycko, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (24) :13045-13050
[2]   High-order multiple quantum excitation in 13C nuclear magnetic resonance spectroscopy of organic solids [J].
Antzutkin, ON ;
Tycko, R .
JOURNAL OF CHEMICAL PHYSICS, 1999, 110 (06) :2749-2752
[3]   Supramolecular structural constraints on Alzheimer's β-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance [J].
Antzutkin, ON ;
Leapman, RD ;
Balbach, JJ ;
Tycko, R .
BIOCHEMISTRY, 2002, 41 (51) :15436-15450
[4]  
ANTZUTKIN ON, 2003, UNPUB BIOPHYS J
[5]   Structure of alanine and glycine residues of Samia cynthia ricini silk fibers studied with solid-state 15N and 13C NMR [J].
Asakura, T ;
Ito, T ;
Okudaira, M ;
Kameda, T .
MACROMOLECULES, 1999, 32 (15) :4940-4946
[6]   Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR [J].
Balbach, JJ ;
Ishii, Y ;
Antzutkin, ON ;
Leapman, RD ;
Rizzo, NW ;
Dyda, F ;
Reed, J ;
Tycko, R .
BIOCHEMISTRY, 2000, 39 (45) :13748-13759
[7]   Supramolecular structure in full-length Alzheimer's β-amyloid fibrils:: Evidence for a parallel β-sheet organization from solid-state nuclear magnetic resonance [J].
Balbach, JJ ;
Petkova, AT ;
Oyler, NA ;
Antzutkin, ON ;
Gordon, DJ ;
Meredith, SC ;
Tycko, R .
BIOPHYSICAL JOURNAL, 2002, 83 (02) :1205-1216
[8]  
Baldus M, 1998, MOL PHYS, V95, P1197, DOI 10.1080/00268979809483251
[9]   SOLUTION STRUCTURES OF BETA PEPTIDE AND ITS CONSTITUENT FRAGMENTS - RELATION TO AMYLOID DEPOSITION [J].
BARROW, CJ ;
ZAGORSKI, MG .
SCIENCE, 1991, 253 (5016) :179-182
[10]   Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein [J].
Baxa, U ;
Speransky, V ;
Steven, AC ;
Wickner, RB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (08) :5253-5260
12345678910