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1 fibrils in patients overproducing monoclonal immunoglobulin light chains.
2  free kappa (kappa) and free lambda (lambda) immunoglobulin light chains.
3 nd trafficking of other glycoproteins, or of immunoglobulin light chains.
4 n of amyloid fibrils derived from monoclonal immunoglobulin light chains.
5 minating between benign and pathologic human immunoglobulin light chains.
6 idosis is characterized by the misfolding of immunoglobulin light chains, accumulating as amyloid fib
7 ile systemic amyloidosis, SSA) or monoclonal immunoglobulin light chain (AL amyloidosis).
8 outcome were determined for 80 patients with immunoglobulin light chain (AL) amyloidosis treated with
9                                           In immunoglobulin light chain (AL) amyloidosis, amyloid fib
10                          Among patients with immunoglobulin light chain (AL) amyloidosis, there is li
11                In light of major advances in immunoglobulin light chain (AL) amyloidosis, we evaluate
12 xazomib in patients with relapsed/refractory immunoglobulin light chain (AL) amyloidosis.
13 developed for the treatment of patients with immunoglobulin light chain (AL) amyloidosis.
14  of the 2 main types of cardiac amyloidosis, immunoglobulin light chain (AL) and transthyretin (ATTR)
15                                              Immunoglobulin light-chain (AL) amyloidosis is a rare, i
16 and limited therapeutic options characterize immunoglobulin light-chain (AL) amyloidosis with major h
17 e kidney is involved in 70% of patients with immunoglobulin light-chain (AL) amyloidosis, but little
18                              Differentiating immunoglobulin light-chain (AL) from transthyretin-relat
19 uding heart involvement of either monoclonal immunoglobulin light-chain (AL) or transthyretin (ATTR)
20                   Progeny mice carrying this immunoglobulin light chain allele produced mature B cell
21           This donor cell had two rearranged immunoglobulin light chain alleles, both directing the s
22 ntransformed plants and those that expressed immunoglobulin light chain alone.
23                                Patients with immunoglobulin light chain amyloidosis (AL amyloidosis)
24                The majority of patients with immunoglobulin light chain amyloidosis (AL) fail to achi
25                                              Immunoglobulin light chain amyloidosis (AL) is character
26 me the treatment of choice for patients with immunoglobulin light chain amyloidosis (AL).
27                                           In immunoglobulin light chain amyloidosis a small, indolent
28                                              Immunoglobulin light chain amyloidosis is a protein misf
29                      Evolution into systemic immunoglobulin light chain amyloidosis is very rare.
30                   Although we confirmed that immunoglobulin light chain amyloidosis was the most freq
31                                   Except for immunoglobulin light chain amyloidosis with heart involv
32 is study, we address the structural basis of immunoglobulin light chain amyloidosis, which results fr
33  for MGRS-related kidney diseases, except in immunoglobulin light chain amyloidosis.
34                                              Immunoglobulin light-chain amyloidosis (AL) and multiple
35                                    Localised immunoglobulin light-chain amyloidosis has an excellent
36 mparisons were made with other patients with immunoglobulin light-chain amyloidosis who did not have
37                                    Localised immunoglobulin light-chain amyloidosis, involving one ty
38 al lymphoplasmacytic malignancies, including immunoglobulin light-chain amyloidosis, multiple myeloma
39 rvival in patients with liver involvement in immunoglobulin light-chain amyloidosis.
40 ing used for the management of patients with immunoglobulin light-chain amyloidosis.
41  transcribed double-stranded (ds) DNA during immunoglobulin light chain and heavy chain class switch
42                                              Immunoglobulin light chain and heavy chain genes were am
43  is a lethal disease characterized by excess immunoglobulin light chains and light chain fragments co
44 ment of B cells that coexpress two different immunoglobulin light chains and, therefore, two antibody
45 nal B-cell disorders producing amyloidogenic immunoglobulin light chains, and the hereditary and "sen
46                                 Primary (AL; immunoglobulin light-chain associated) amyloidosis is ch
47 y probabilities of selected positions of the immunoglobulin light chain-binding domain of protein L,
48 l surface and did not efficiently bind kappa immunoglobulin light chains, but did associate with Ig a
49            This study emphasizes the complex immunoglobulin light chain-cell interactions that result
50 rimary (light chain-associated) amyloidosis, immunoglobulin light chains deposit as amyloid fibrils i
51                                              Immunoglobulin light chain deposition diseases involve v
52 lls expressing CRBN, causing accumulation of immunoglobulin light-chain dimers, significantly increas
53 ional stability, and aggregation behavior of immunoglobulin light chain domain LEN.
54 ta consist of 209 proteins of human antibody immunoglobulin light chains, each represented by aligned
55 BCR knock-in mice lacking self-Thy-1 ligand, immunoglobulin light chain editing occurred, generating
56      These results indicate that the 3'kappa immunoglobulin light chain enhancer can effectively targ
57 L transgene under the control of the 3'kappa immunoglobulin light chain enhancer, which is most activ
58 unction as transcriptional activators of the immunoglobulin light-chain enhancer E lambda 2.4 when co
59 Serum amyloid P component, apolipoprotein E, immunoglobulin light chains, Factor X, and complement pr
60 n amyloidosis is a devastating disease where immunoglobulin light chains form amyloid fibrils, result
61         In light chain amyloidosis (AL), the immunoglobulin light chain forms amyloid fibrils that de
62 hological deposition of insoluble fibrils of immunoglobulin light chain fragments in various tissues,
63 hological deposition of insoluble fibrils of immunoglobulin light-chain fragments in various organs a
64 ain gene segments as substrate for secondary immunoglobulin light chain gene rearrangement and is ind
65 eexpressed in small, resting pre-B cells for immunoglobulin light chain gene rearrangement.
66 for the ability of BCR ligation to stimulate immunoglobulin light chain gene rearrangements in immatu
67 the Fraction C'-D transition is critical for immunoglobulin light chain gene recombination and to pre
68 at is recruited to composite elements within immunoglobulin light-chain gene enhancers through a spec
69 hocyte developmental checkpoints inasmuch as immunoglobulin light-chain gene rearrangement occurred i
70                    To approach these issues, immunoglobulin light-chain gene rearrangements were indu
71 e kappaB DNA of the intronic enhancer of the immunoglobulin light-chain gene.
72 d as preB since they failed to rearrange the immunoglobulin light chain genes.
73                                              Immunoglobulin light chains have two similar domains, ea
74 ing the immunoglobulin heavy chain (Igh) and immunoglobulin light chain (Igk) takes place sequentiall
75                                              Immunoglobulin light chain (IgL) rearrangements occur mo
76    Mass spectrometric analysis identified an immunoglobulin light chain in the band but found no PrP
77 verproduction and abnormal deposition of the immunoglobulin light chain in various organs.
78  presence of monoclonal free kappa or lambda immunoglobulin light chains in monoclonal gammopathy of
79 at increased monoclonal free kappa or lambda immunoglobulin light chains in smoldering multiple myelo
80 characterized by the deposition of monotypic immunoglobulin light chains in the kidney, resulting in
81 that facilitates the detection of editing of immunoglobulin light chains in vivo.
82 lization and cellular trafficking of urinary immunoglobulin light chains into cardiac fibroblasts.
83         The sample used was an amyloidogenic immunoglobulin light chain, involved in AL or light chai
84 w BiP interacts with a particular substrate, immunoglobulin light chain (lambda LC), during its foldi
85                     Deposition of monoclonal immunoglobulin light chain (LC) aggregates in tissues is
86                                     Systemic immunoglobulin light chain (LC) amyloidosis (AL) is a po
87                                              Immunoglobulin light chain (LC) normally is a soluble, s
88 e clonal production and tissue deposition of immunoglobulin light chain (LC) proteins.
89 used by the clonal production of an unstable immunoglobulin light chain (LC), which affects organ fun
90 n both AL and multiple myeloma (MM), soluble immunoglobulin light chains (LC) are produced by clonal
91 crasia characterized by clonal production of immunoglobulin light chains (LC) resulting in the subseq
92 d systemic deposition of amyloid composed of immunoglobulin light chains (LC).
93 s from overproduction of unstable monoclonal immunoglobulin light chains (LCs) and the deposition of
94                            Overproduction of immunoglobulin light chains leads to systemic amyloidosi
95 idosis and familial amyloid polyneuropathy), immunoglobulin light chains (light-chain amyloid), beta2
96       We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a str
97 e, can also lead to allelic inclusion at the immunoglobulin light chain loci and the development of B
98                                              Immunoglobulin light-chain loci normally undergo recombi
99 center B cells, demonstrating that the kappa immunoglobulin light-chain locus becomes a substrate for
100 ens and cytokines in regulation of the kappa immunoglobulin light-chain locus, we have characterized
101  protein misfolding disease where monoclonal immunoglobulin light chains misfold and deposit as amylo
102          The cellular response to 11 urinary immunoglobulin light chains of kappa1, lambda6, and lamb
103 arge membrane pores and high permeability to immunoglobulin light chains) or a conventional high-flux
104             LEN is the variable domain of an immunoglobulin light chain originally isolated from the
105 izing and destabilizing mutations is key for immunoglobulin light-chains populating unfolded intermed
106 idosis, amyloid fibril deposits derived from immunoglobulin light chains produced by a clonal plasma
107 in conformation disorder in which monoclonal immunoglobulin light chains produced by clonal plasma ce
108 s element has considerable homology to mouse immunoglobulin light chain promoter sequences to which t
109 ed that the dimer interface of amyloidogenic immunoglobulin light chain protein AL-09 is twisted 90 d
110 ated with the overproduction of a monoclonal immunoglobulin light chain protein by a B-lymphocyte clo
111 egulatory factor 4 (IRF-4) and IRF-8 promote immunoglobulin light-chain rearrangement and transcripti
112  via the signaling molecule Syk and promoted immunoglobulin light-chain rearrangement.
113 t with aberrant VJ recombination between the immunoglobulin light chain region (Ig kappa) on chromoso
114            Monoclonality was demonstrated by immunoglobulin light-chain restriction in all cases with
115 t remains tightly bound to newly synthesized immunoglobulin light chains, resulting in retention of l
116 idosis is a protein misfolding disease where immunoglobulin light chains sample partially folded stat
117 ted with amyloid fibril formation, including immunoglobulin light chain, serum amyloid A protein, and
118  631 substitutions present in 90 nurse shark immunoglobulin light chain somatic mutants, 338 constitu
119 rget the type of amyloid that is formed from immunoglobulin light chains, that is, AL.
120 e B cells within the HL cell lines expressed immunoglobulin light chain, the memory B-cell antigen CD
121 st possible mechanisms for the propensity of immunoglobulin light chains to amyloid formation.
122  exchange rates) and the propensity of human immunoglobulin light chains to form amyloid fibrils in v
123 ted an FcgammaRIIB-independent difference in immunoglobulin light-chain usage, consistent with an alt
124 y studying the effects of mutations of human immunoglobulin light chain variable domain (V(L)).
125 re we identify the monomeric form of the Mcg immunoglobulin light chain variable domain as the quater
126                             LEN is a kappaIV immunoglobulin light chain variable domain from a patien
127 loid fibrils were investigated for a dimeric immunoglobulin light chain variable domain, employing pr
128  as a model amyloidogenic protein, a dimeric immunoglobulin light chain variable domain.
129 temic extracellular deposition of monoclonal immunoglobulin light chain variable domains in the form
130   This study characterizes the repertoire of immunoglobulin light chain variable genes used by the cl
131 tional dynamics of a pathogenic kappa4 human immunoglobulin light-chain variable domain, SMA, associa
132 model for the assembly of amyloid fibrils of immunoglobulin light-chain variable domains is proposed
133 s the free light-chain assay and the role of immunoglobulin light-chain variable region germline gene
134     The structure of a multisubunit protein (immunoglobulin light chain) was solved in three crystal
135 ubiquitylation sites on the NS-1 nonsecreted immunoglobulin light chain, which is an ERAD substrate.

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