| review article | Q7318358 |
| scholarly article | Q13442814 |
| P50 | author | Sheena Radford | Q17011933 |
| P2093 | author name string | Geoffrey W Platt | |
| P2860 | cites work | Beta2-Microglobulin dialysis amyloid and its formation: role of 3-deoxyglucosone and advanced glycation end products | Q73634931 |
| Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis | Q80093135 | ||
| Mechanism by which the amyloid-like fibrils of a beta 2-microglobulin fragment are induced by fluorine-substituted alcohols | Q80227832 | ||
| A native to amyloidogenic transition regulated by a backbone trigger | Q46954596 | ||
| Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. | Q52855180 | ||
| Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. | Q52856652 | ||
| A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH. | Q52856687 | ||
| Dynamics in the unfolded state of beta2-microglobulin studied by NMR. | Q52858320 | ||
| Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro. | Q52860845 | ||
| Early stages of misfolding and association of beta2-microglobulin: insights from infrared spectroscopy and dynamic light scattering. | Q52917886 | ||
| Collagen plays an active role in the aggregation of beta2-microglobulin under physiopathological conditions of dialysis-related amyloidosis | Q57187511 | ||
| Variants of β2-microglobulin cleaved at lysine-58 retain the main conformational features of the native protein but are more conformationally heterogeneous and unstable at physiological temperature | Q57819631 | ||
| Role of the C-Terminal 28 Residues of β2-Microglobulin in Amyloid Fibril Formation | Q64360618 | ||
| Fast-folding and slow-folding forms of unfolded proteins | Q69647574 | ||
| A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin | Q69899045 | ||
| Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation | Q24530946 | ||
| Crystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic properties | Q27639361 | ||
| The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties | Q27650266 | ||
| DE loop mutations affect beta2-microglobulin stability and amyloid aggregation | Q27652402 | ||
| Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution | Q27660465 | ||
| Review: history of the amyloid fibril | Q28143393 | ||
| Protein folding and misfolding | Q28235199 | ||
| A primer of amyloid nomenclature | Q28241008 | ||
| A possible role for pi-stacking in the self-assembly of amyloid fibrils | Q34107552 | ||
| Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases | Q34422461 | ||
| A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments | Q34572928 | ||
| Towards an understanding of the structural molecular mechanism of beta(2)-microglobulin amyloid formation in vitro | Q36228856 | ||
| From chance to frequent encounters: origins of beta2-microglobulin fibrillogenesis | Q36286710 | ||
| A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils | Q36719294 | ||
| Anti-A beta 1-11 antibody binds to different beta-amyloid species, inhibits fibril formation, and disaggregates preformed fibrils but not the most toxic oligomers. | Q36731538 | ||
| Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly | Q36736931 | ||
| An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril | Q36986109 | ||
| Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils | Q37305282 | ||
| Competition between intramolecular and intermolecular interactions in an amyloid-forming protein | Q43076154 | ||
| Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation | Q43197716 | ||
| A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis | Q43759053 | ||
| Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro | Q43776859 | ||
| Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I. | Q43785536 | ||
| Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence | Q44368597 | ||
| Amyloidogenic synthetic peptides of β2-microglobulin—a role of the disulfide bond | Q44410252 | ||
| Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH. | Q44512589 | ||
| A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation | Q44512592 | ||
| Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of beta2-microglobulin | Q44575256 | ||
| Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH. | Q45026374 | ||
| Prediction of aggregation-prone regions in structured proteins | Q45335883 | ||
| A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch. | Q46006165 | ||
| A beta2-microglobulin cleavage variant fibrillates at near-physiological pH. | Q46114848 | ||
| Nuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond | Q46422967 | ||
| Ultrasonication-induced amyloid fibril formation of beta2-microglobulin | Q46620766 | ||
| Amyloid nucleation triggered by agitation of beta2-microglobulin under acidic and neutral pH conditions | Q46797402 | ||
| P275 | copyright license | Creative Commons Attribution 3.0 Unported | Q14947546 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 16 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | globulins | Q321710 |
| energy landscape | Q5377166 | ||
| membrane protein | Q423042 | ||
| blood proteins | Q425056 | ||
| macromolecular substance | Q75174158 | ||
| P304 | page(s) | 2623-2629 | |
| P577 | publication date | 2009-05-09 | |
| 2009-08-20 | |||
| P1433 | published in | FEBS Letters | Q1388051 |
| P1476 | title | Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape | |
| P478 | volume | 583 |
| Q42532927 | A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity |
| Q40484665 | A covalent homodimer probing early oligomers along amyloid aggregation |
| Q35165212 | A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior |
| Q40117218 | A systematic molecular dynamics approach to the structural characterization of amyloid aggregation propensity of β2-microglobulin mutant D76N. |
| Q26824195 | Assessing the causes and consequences of co-polymerization in amyloid formation |
| Q48058836 | Assessing the effect of D59P mutation in the DE loop region in amyloid aggregation propensity of β2-microglobulin: A molecular dynamics simulation study. |
| Q42663683 | Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations |
| Q40826378 | Capillary electrophoresis analysis of different variants of the amyloidogenic protein β2 -microglobulin as a simple tool for misfolding and stability studies |
| Q92241558 | Collagen I Weakly Interacts with the β-Sheets of β2-Microglobulin and Enhances Conformational Exchange To Induce Amyloid Formation |
| Q27666683 | Conformational Conversion during Amyloid Formation at Atomic Resolution |
| Q37395119 | Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry. |
| Q24302181 | D-strand perturbation and amyloid propensity in beta-2 microglobulin |
| Q42379486 | DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form |
| Q38305183 | Distinguishing closely related amyloid precursors using an RNA aptamer |
| Q38950497 | Double-stranded DNA stereoselectively promotes aggregation of amyloid-like fibrils and generates peptide/DNA matrices |
| Q64892260 | Extracellular matrix components modulate different stages in β2-microglobulin amyloid formation. |
| Q42152268 | How one bad protein spoils the barrel: structural details of β2-microglobulin amyloidogenicity |
| Q41283573 | Intermolecular alignment in β2-microglobulin amyloid fibrils |
| Q42550081 | Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies |
| Q52847877 | Mass spectrometry and the amyloid problem--how far can we go in the gas phase? |
| Q47625995 | Molecular dynamics simulations of β2-microglobulin interaction with hydrophobic surfaces. |
| Q42136608 | Population of nonnative states of lysozyme variants drives amyloid fibril formation |
| Q35597175 | Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level |
| Q42105214 | Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation |
| Q33883237 | Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling |
| Q39736236 | Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH. |
| Q43127628 | Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin |
| Q83227865 | Structural mapping of oligomeric intermediates in an amyloid assembly pathway |
| Q38093118 | The role of amyloidogenic protein oligomerization in neurodegenerative disease |
| Q43233916 | The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH. |
| Q41774231 | Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers |
| Q36806901 | Understanding protein aggregation from the view of monomer dynamics |
| Q27666185 | β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages |
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