Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 A molecular model for self-assembly of amyloid fibrils: immunoglobulin light chains.

× No keyword cloud information.

15 in total

1. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains.

Authors: R Raffen; L J Dieckman; M Szpunar; C Wunschl; P R Pokkuluri; P Dave; P Wilkins Stevens; X Cai; M Schiffer; F J Stevens
Journal: Protein Sci Date: 1999-03 Impact factor: 6.725

2. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy.

Authors: C Ionescu-Zanetti; R Khurana; J R Gillespie; J S Petrick; L C Trabachino; L J Minert; S A Carter; A L Fink
Journal: Proc Natl Acad Sci U S A Date: 1999-11-09 Impact factor: 11.205

3. Heterogeneity in primary structure, post-translational modifications, and germline gene usage of nine full-length amyloidogenic kappa1 immunoglobulin light chains.

Authors: Lawreen H Connors; Yan Jiang; Marianna Budnik; Roger Théberge; Tatiana Prokaeva; Kip L Bodi; David C Seldin; Catherine E Costello; Martha Skinner
Journal: Biochemistry Date: 2007-11-16 Impact factor: 3.162

Review 4. Molecular anatomy and the pathological expression of antibody light chains.

Authors: M Schiffer
Journal: Am J Pathol Date: 1996-05 Impact factor: 4.307

5. Single amino acid substitution in LC-CDR1 induces Russell body phenotype that attenuates cellular protein synthesis through eIF2α phosphorylation and thereby downregulates IgG secretion despite operational secretory pathway traffic.

Authors: Haruki Hasegawa; Ann Hsu; Christine E Tinberg; Karen E Siegler; Aaron A Nazarian; Mei-Mei Tsai
Journal: MAbs Date: 2017-04-05 Impact factor: 5.857

A molecular model for self-assembly of amyloid fibrils: immunoglobulin light chains.

1. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains.

2. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy.

3. Heterogeneity in primary structure, post-translational modifications, and germline gene usage of nine full-length amyloidogenic kappa1 immunoglobulin light chains.

Review 4. Molecular anatomy and the pathological expression of antibody light chains.

5. Single amino acid substitution in LC-CDR1 induces Russell body phenotype that attenuates cellular protein synthesis through eIF2α phosphorylation and thereby downregulates IgG secretion despite operational secretory pathway traffic.

6. Formation of amyloid fibers by monomeric light chain variable domains.

Review 7. Kidney disease associated with plasma cell dyscrasias.

8. Structural analysis of a therapeutic monoclonal antibody dimer by hydroxyl radical footprinting.

9. Light chain-associated amyloid deposits comprised of a novel kappa constant domain.

10. Light chain cardiomyopathy. Structural analysis of the light chain tissue deposits.