Formation of amyloid fibers by monomeric light chain variable domains

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Formation of amyloid fibers by monomeric light chain variable domains is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M114.585638
P932PMC publication ID4183792
P698PubMed publication ID25138218

P50authorMeytal LandauQ28037100
Michael R SawayaQ37374572
Shannon R EssweinQ58237385
Julian P WhiteleggeQ88590279
P2093author name stringBoris Brumshtein
Duilio Cascio
Martin L Phillips
Christopher M Ryan
David S Eisenberg
P2860cites workStructure of the cross-beta spine of amyloid-like fibrilsQ24548308
Processing of X-ray diffraction data collected in oscillation modeQ26778468
Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7Q27620078
Molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolutionQ27637545
Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic propertiesQ27638904
Comparison of the three-dimensional structures of a human Bence-Jones dimer crystallized on Earth and aboard US Space Shuttle Mission STS-95Q27641099
Bence Jones KWR protein structures determined by X-ray crystallographyQ27646183
Altered Dimer Interface Decreases Stability in an Amyloidogenic ProteinQ27650295
A single mutation at the sheet switch region results in conformational changes favoring lambda6 light-chain fibrillogenesisQ27658345
A Single Mutation Promotes Amyloidogenicity through a Highly Promiscuous Dimer InterfaceQ27661519
β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkagesQ27666185
Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal formsQ27694809
Principles and pitfalls in designing site-directed peptide ligandsQ27731973
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesisQ27734827
XDSQ27860472
NMRPipe: a multidimensional spectral processing system based on UNIX pipesQ27860859
Refinement of macromolecular structures by the maximum-likelihood methodQ27861011
Review: history of the amyloid fibrilQ28143393
β-Sheet topology and the relatedness of proteinsQ28295058
Interconversion of conformational isomers of light chains in the Mcg immunoglobulinsQ28325499
Determination and analysis of urea and guanidine hydrochloride denaturation curvesQ29616644
Simultaneous optical recording of membrane potential and intracellular calcium from brain slicesQ30707340
Amyloidogenic and associated proteins in systemic amyloidosis proteome of adipose tissue.Q33334024
Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimensQ33508070
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitroQ34252457
The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloidQ34380911
Protein aggregation: folding aggregates, inclusion bodies and amyloidQ34460420
Aberrant immunoglobulin synthesis in light chain amyloidosis. Free light chain and light chain fragment production by human bone marrow cells in short-term tissue cultureQ34539341
Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I.Q34650054
Mcg in 2030: new techniques for atomic position determination of immune complexesQ35007312
An ABC of amyloidQ35144002
Domain swapping: entangling alliances between proteinsQ35156951
A role for destabilizing amino acid replacements in light-chain amyloidosisQ35458844
Mechanisms of disease: monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition diseaseQ36097644
Self-association of human immunoglobulin kappa I light chains: role of the third hypervariable regionQ36357713
Deposition diseases and 3D domain swappingQ36477837
Inhibiting transthyretin amyloid fibril formation via protein stabilizationQ37082709
Light chain amyloidosis - current findings and future prospectsQ37502618
The amyloid state of proteins in human diseasesQ37994283
Systemic amyloidosesQ38085664
Evolution of variable and constant domains and joining segments of rearranging immunoglobulins.Q38237042
Sequences at the somatic recombination sites of immunoglobulin light-chain genesQ39673181
Immunoglobulin and amyloid fibril proteinsQ39868822
Conformational isomerism, rotational allomerism, and divergent evolution in immunoglobulin light chainsQ41050005
The systemic amyloidosesQ41596634
Amyloid and myelomaQ42132877
AL-Base: a visual platform analysis tool for the study of amyloidogenic immunoglobulin light chain sequencesQ42772096
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 aggregationQ46656100
"Cross-beta" conformation in proteins.Q52502609
A Molecular Model for Self-Assembly of Amyloid Fibrils: Immunoglobulin Light ChainsQ53201393
Fragments of the constant region of immunoglobulin light chains are constituents of AL-amyloid proteins.Q53794637
IMGT, the international ImMunoGeneTics databaseQ57339950
Monomer – Dimer forms of Bence Jones ProteinsQ59071607
A Type k Bence Jones Protein Containing a Cysteinyl Residue in the Variable Region 1Q66957999
Crystal and molecular structure of the dimer of variable domains of the Bence-Jones protein ROYQ67044403
A crystallographic investigation of the Mcg myeloma protein. ANL-7635Q70138531
A search for site-filling ligands in the Mcg Bence-Jones dimer: crystal binding studies of fluorescent compoundsQ70490523
Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitroQ70610313
In vitro immunoglobulin light chain fibrillogenesisQ73043257
An amyloid protein: the amino-terminal variable fragment of an immunoglobulin light chainQ93694302
P433issue40
P407language of work or nameEnglishQ1860
P1104number of pages13
P304page(s)27513-27525
P577publication date2014-08-19
P1433published inJournal of Biological ChemistryQ867727
P1476titleFormation of amyloid fibers by monomeric light chain variable domains
P478volume289

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cites work (P2860)
Q38995080Amyloidosis: an unusual cause of upper gastrointestinal bleeding.
Q90642082Biochemical and biophysical characterisation of immunoglobulin free light chains derived from an initially unbiased population of patients with light chain disease
Q64071949Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis
Q42327795Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains
Q90164488Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation
Q38665447Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI.
Q57792069Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light chain amyloidosis
Q46507358Incomplete Refolding of Antibody Light Chains to Non-Native, Protease-Sensitive Conformations Leads to Aggregation: A Mechanism of Amyloidogenesis in Patients?
Q38549232Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain
Q40614534Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils
Q39164833Screening methods for identifying pharmacological chaperones.
Q91845290Site-Specific Interactions with Copper Promote Amyloid Fibril Formation for λ6aJL2-R24G
Q47292925Structure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients

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