scholarly article | Q13442814 |
P50 | author | Meytal Landau | Q28037100 |
Michael R Sawaya | Q37374572 | ||
Shannon R Esswein | Q58237385 | ||
Julian P Whitelegge | Q88590279 | ||
P2093 | author name string | Boris Brumshtein | |
Duilio Cascio | |||
Martin L Phillips | |||
Christopher M Ryan | |||
David S Eisenberg | |||
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Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties | Q27638904 | ||
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β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages | Q27666185 | ||
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Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro | Q34252457 | ||
The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid | Q34380911 | ||
Protein aggregation: folding aggregates, inclusion bodies and amyloid | Q34460420 | ||
Aberrant immunoglobulin synthesis in light chain amyloidosis. Free light chain and light chain fragment production by human bone marrow cells in short-term tissue culture | Q34539341 | ||
Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. | Q34650054 | ||
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Mechanisms of disease: monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease | Q36097644 | ||
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Evolution of variable and constant domains and joining segments of rearranging immunoglobulins. | Q38237042 | ||
Sequences at the somatic recombination sites of immunoglobulin light-chain genes | Q39673181 | ||
Immunoglobulin and amyloid fibril proteins | Q39868822 | ||
Conformational isomerism, rotational allomerism, and divergent evolution in immunoglobulin light chains | Q41050005 | ||
The systemic amyloidoses | Q41596634 | ||
Amyloid and myeloma | Q42132877 | ||
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Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. | Q43571376 | ||
Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation | Q46656100 | ||
"Cross-beta" conformation in proteins. | Q52502609 | ||
A Molecular Model for Self-Assembly of Amyloid Fibrils: Immunoglobulin Light Chains | Q53201393 | ||
Fragments of the constant region of immunoglobulin light chains are constituents of AL-amyloid proteins. | Q53794637 | ||
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Crystal and molecular structure of the dimer of variable domains of the Bence-Jones protein ROY | Q67044403 | ||
A crystallographic investigation of the Mcg myeloma protein. ANL-7635 | Q70138531 | ||
A search for site-filling ligands in the Mcg Bence-Jones dimer: crystal binding studies of fluorescent compounds | Q70490523 | ||
Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro | Q70610313 | ||
In vitro immunoglobulin light chain fibrillogenesis | Q73043257 | ||
An amyloid protein: the amino-terminal variable fragment of an immunoglobulin light chain | Q93694302 | ||
P433 | issue | 40 | |
P407 | language of work or name | English | Q1860 |
P1104 | number of pages | 13 | |
P304 | page(s) | 27513-27525 | |
P577 | publication date | 2014-08-19 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Formation of amyloid fibers by monomeric light chain variable domains | |
P478 | volume | 289 |
Q38995080 | Amyloidosis: an unusual cause of upper gastrointestinal bleeding. |
Q90642082 | Biochemical and biophysical characterisation of immunoglobulin free light chains derived from an initially unbiased population of patients with light chain disease |
Q64071949 | Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis |
Q42327795 | Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains |
Q90164488 | Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation |
Q38665447 | Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI. |
Q57792069 | Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light chain amyloidosis |
Q46507358 | Incomplete Refolding of Antibody Light Chains to Non-Native, Protease-Sensitive Conformations Leads to Aggregation: A Mechanism of Amyloidogenesis in Patients? |
Q38549232 | Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain |
Q40614534 | Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils |
Q39164833 | Screening methods for identifying pharmacological chaperones. |
Q91845290 | Site-Specific Interactions with Copper Promote Amyloid Fibril Formation for λ6aJL2-R24G |
Q47292925 | Structure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients |
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