The intrachain disulfide bond of β2-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH

Journal of Biochemistry

Volumn 131, Issue 1, 2002, Pages 45-52

  Ohhashi, Yumiko ^a   Hagihara, Yoshihisa ^a,b   Kozhukh, Gennady ^a   Hoshino, Masaru ^a   Hasegawa, Kazuhiro ^c   Yamaguchi, Itaru ^c   Naiki, Hironobu ^c   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^c UNIVERSITY OF FUKUI   (Japan)

Author keywords

Amyloid; Conformational disease; Disulfide; 2 Microglobulin

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; IMMUNOGLOBULIN; THIOL GROUP; TRYPTOPHAN;

ARTICLE; CIRCULAR DICHROISM; DENATURATION; DISULFIDE BOND; ELECTRON MICROSCOPY; FLUORESCENCE; MAJOR HISTOCOMPATIBILITY COMPLEX; NONHUMAN; PH; PICHIA PASTORIS; PROTEIN POLYMERIZATION; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE;

PICHIA; PICHIA PASTORIS;

EID: 0036172742     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003076     Document Type: Article

References (41)

1. A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin
2. Tumoral amyloidosis of bone of beta2-microglobulin origin in association with long-term hemodialysis
3. Dialysis-related amyloidosis
4. Dialysis amyloidosis: Current disease concepts and new perspectives for its treatment
5. First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
6. Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer's β-amyloid fibril formation in vitro
7. Fluorometric determination of amyliod fibrils in vitro using the fluorescent dye, thioflavine T
8. Kinetic analysis of amyloid fibril polymerization in vitro
9. Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro
10. Kinetic analysis of amyloid fibril formation
11. Structure of the human class I histocompatibility antigen, HLA-A2
12. 1H NMR assignments and secondary structure of human β2-microglobulin in solution
13. The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
14. Formation of the intrachain disulfide bond in the constant fragment of the immunoglobulin light chain
15. Unfolding and refolding of the reduced constant fragment of the immunoglobulin light chain
16. Identification of the phospholipid-binding site of human β2-glycoprotein I domain V by heteronuclear magnetic resonance
17. Calcium tartrate gel
18. Reassessment of Ellman's reagent
19. The structure and function of immunoglobulin domains: Studies with beta2-microglobulin on the role of the intrachain disulfide bond
20. β2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils
21. Partially unfolded states of β2-microglobulin and amyloid formation in vitro
22. Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin
23. Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation
24. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
25. Amyloid fibril formation by an SH3 domain
26. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy
27. Conformational diversity in a yeast prion dictates its seeding specificity
28. Solution conformation and amyloid-like fibril formation of a polar peptide derived from a β-hairpin in the OspA single-layer β-sheet
29. Mutational analysis of designed peptides that undergo structural transition from α helix to β sheet and amyloid fibril formation
30. A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils
31. Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR
32. Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin
33. Reexamination of the folding of BPTI: Predominance of native intermediate
34. Structural determinants of oxidative folding in proteins
35. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
36. The role of disulfide bridge in the folding and stability of the recombinant human prion protein
37. A role for intermolecular disulfide bonds in prion diseases?
38. Watching amyloid fibrils grow by time-lapse atomic force microscopy
39. Bidirectional amyloid fiber growth for a yeast prion determinant
40. Strong growth polarity of yeast prion fiber revealed by single fiber imaging
41. 2-microglobulin in amyloidosis in vitro