The fibril_one on-line database: Mutations, experimental conditions, and trends associated with amyloid fibril formation

Protein Science

Volumn 11, Issue 7, 2002, Pages 1862-1866

  Siepen, Jennifer A ^a   Westhead, David R ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Amyloidosis; MySQL; Pathogenic mutations; Protein misfolding; Protein stability; Web interface

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID;

ARTICLE; HUMAN; INTERNET; METABOLISM; PROTEIN DATABASE; AMINO ACID SEQUENCE; AMYLOIDOSIS; COMPUTER INTERFACE; COMPUTER LANGUAGE; GENE MUTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN SYNTHESIS; SEQUENCE DATABASE;

AMYLOID BETA-PROTEIN; DATABASES, PROTEIN; HUMANS; INTERNET;

EID: 0036087114     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0204302     Document Type: Article

References (16)

1. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
2. GenBank
3. The Protein Data Bank
4. Designing conditions for in vitro formation of amyloid protofilaments and fibrils
5. Protein misfolding, evolution and disease
6. A role for destabilising amino acid replacements in light chain amyloidosis
7. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
8. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
9. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
10. Amyloid fibrillogenesis: Themes and variations
11. ID secondary structure prediction through evolutionary profiles
12. Common core structure of amyloid fibrils by synchrotron x-ray diffraction
13. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
14. Secondary structure predictions and medium range interactions