Results 281 to 290 of about 248,637 (315)

ImmunoMatch learns and predicts cognate pairing of heavy and light immunoglobulin chains

Guo D, Dunn-Walters DK, Fraternali F, Ng JCF.   +3 more
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Immunoglobulin light chain amyloidosis

Expert Review of Hematology, 2013
Primary light chain amyloidosis is the most common form of systemic amyloidosis and is caused by misfolded light chains that cause proteotoxicity and rapid decline of vital organ function. Early diagnosis is essential in order to deliver effective therapy and prevent irreversible organ damage.
MERLINI, GIAMPAOLO, Comenzo RL, Seldin DC, Wechalekar A, Gertz MA   +4 more
openaire   +4 more sources

Light chain immunoglobulins as substrates for collagenase

Immunochemistry, 1975
Abstract The proteolytic action of collagenase on immunoglobulin light chains has been studied by mean of quantitative determination of N-terminal amino acid residues. L (λ) and L (κ) appear to be susceptible to the enzymatic action and this characteristics is a highly specific and general one.
J.-C Cavadore, M.-A Coletti-Previero, C Tonnelle   +2 more
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Light chains of immunoglobulins in human secretions

Clinica Chimica Acta, 1994
Immunoglobulin kappa light chains are predominant in normal human serum and a kappa/lambda ratio of 1.7 to 2 has been reported. However, little is known of the partition of light chains in secretions. The levels of IgA, kappa and lambda were assayed by nephelometry in a series of secretions and in normal human serum.
Marie C. Béné, Estelle Seilles, Claire Molé, Gilbert C. Faure, Paul M. Montagne   +4 more
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Treatment of immunoglobulin light chain amyloidosis

Current Hematologic Malignancy Reports, 2009
No therapy is uniformly effective in the management of immunoglobulin light chain amyloidosis (AL amyloidosis). Despite the common generalization, therapy is highly effective. Options available to patients with AL amyloidosis include high-dose therapy, but this is applicable to only about one fourth of patients.
Steven R. Zeldenrust, Morie A. Gertz
openaire   +3 more sources

Immunoglobulin light chain toxicity in a mouse model of monoclonal immunoglobulin light-chain deposition disease

Blood, 2020
Light chain deposition disease (LCDD) is a rare disorder characterized by glomerular and peritubular amorphous deposits of a monoclonal immunoglobulin (Ig) light chain (LC), leading to nodular glomerulosclerosis and nephrotic syndrome. We developed a transgenic model using site-directed insertion of the variable domain of a pathogenic human LC gene ...
Christophe Sirac, Guy Touchard, Vincent Javaugue, Maria Victoria Ayala, Frank Bridoux, Nicolas Pons, François Boyer, Michel Cogné, Michel Cogné, Mohamad Omar Ashi, Arnaud Jaccard, Amélie Bonaud, Zeliha Oruc, Agnès Paquet, Laurent Delpy, Bastien Hervé, Sébastien Bender, Claire Carrion, Alexia Rinsant, Sihem Kaaki, Christelle Oblet   +20 more
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The mysterious immunoglobulin light chain

Developmental & Comparative Immunology, 2002
The immunoglobulin light chain is mysterious from different points of view. In an evolutionary perspective there seems to be at least three major pathways but it is today impossible to say which of them is the most ancient one and which isotype belongs to which branch.
openaire   +3 more sources

A Possible Precursor of Immunoglobulin Light Chains

Nature New Biology, 1972
IMMUNOGLOBULIN light chains are synthesized in heterologous cell-free systems from reticulocytes1 and Krebs II ascites cells2 and in reconstituted homologous systems from lymph nodes3,4 and myeloma tumours5,6. Although the synthesis appeared to be essentially faithful, absolute identity with authentic light chains was not demonstrated and some small ...
Michael B. Mathews, Michael B. Mathews, C. Milstein, George G. Brownlee, T. M. Harrison   +4 more
openaire   +3 more sources

Refolding of the Immunoglobulin Light Chain1

The Journal of Biochemistry, 1979
The kinetics of the refolding reactions of type lambda Bence Jones proteins from 4 M GuHCl were studied by CD, ultraviolet absorption, and fluorescence spectrophotometry. The kinetics were complex and consisted of at least three phases, an undetectable fast phase, a detectable fast phase, and a slow phase.
Kozo Hamaguchi, Yuji Goto, Takachika Azuma   +2 more
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Immunoglobulin light chains, glycosaminoglycans, and amyloid

Cellular and Molecular Life Sciences, 2000
Immunoglobulin light chains are the precursor proteins for fibrils that are formed during primary amyloidosis and in amyloidosis associated with multiple myeloma. As found for the approximately 20 currently described forms of focal, localized, or systemic amyloidoses, light chain-related fibrils extracted from physiological deposits are invariably ...
R. Kisilevsky, F. J. Stevens
openaire   +3 more sources