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Literature DB >> 6811753

Unfolding and refolding of the constant fragment of the immunoglobulin light chain.

Y Goto, K Hamaguchi.

Abstract

Mesh：

Substances：

Year: 1982 PMID： 6811753 DOI： 10.1016/0022-2836(82)90146-2

Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469

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11 in total

1. The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity.

Authors: Matthias J Feige; Sandra Groscurth; Moritz Marcinowski; Zu Thur Yew; Vincent Truffault; Emanuele Paci; Horst Kessler; Johannes Buchner
Journal: Proc Natl Acad Sci U S A Date: 2008-09-03 Impact factor: 11.205

2. Enhanced secretory production of a single-chain antibody fragment from Bacillus subtilis by coproduction of molecular chaperones.

Authors: S C Wu; R Ye; X C Wu; S C Ng; S L Wong
Journal: J Bacteriol Date: 1998-06 Impact factor: 3.490

3. The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins.

Authors: Matthias J Feige; Melissa A Gräwert; Moritz Marcinowski; Janosch Hennig; Julia Behnke; David Ausländer; Eva M Herold; Jirka Peschek; Caitlin D Castro; Martin Flajnik; Linda M Hendershot; Michael Sattler; Michael Groll; Johannes Buchner
Journal: Proc Natl Acad Sci U S A Date: 2014-05-15 Impact factor: 11.205

4. Kinetic stability and sequence/structure studies of urine-derived Bence-Jones proteins from multiple myeloma and light chain amyloidosis patients.

Authors: Luis M Blancas-Mejía; Emily B Martin; Angela Williams; Jonathan S Wall; Marina Ramirez-Alvarado
Journal: Biophys Chem Date: 2017-09-01 Impact factor: 2.352

Review 5. How antibodies fold.

Authors: Matthias J Feige; Linda M Hendershot; Johannes Buchner
Journal: Trends Biochem Sci Date: 2009-12-21 Impact factor: 13.807

10. Effect of Heat-treatment on Accuracy of Infrared Spectroscopy and Digital and Optical Brix Refractometers for Measuring Immunoglobulin G Concentration in Bovine Colostrum.

Authors: I Elsohaby; J T McClure; N Dow; G P Keefe
Journal: J Vet Intern Med Date: 2017-12-27 Impact factor: 3.333

Unfolding and refolding of the constant fragment of the immunoglobulin light chain.

1. The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity.

2. Enhanced secretory production of a single-chain antibody fragment from Bacillus subtilis by coproduction of molecular chaperones.

3. The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins.

4. Kinetic stability and sequence/structure studies of urine-derived Bence-Jones proteins from multiple myeloma and light chain amyloidosis patients.

Review 5. How antibodies fold.

6. A remote prolyl isomerization controls domain assembly via a hydrogen bonding network.

7. An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.

8. Denaturant-induced expansion and compaction of a multi-domain protein: IgG.

Review 9. Understanding the complex mechanisms of β2-microglobulin amyloid assembly.

10. Effect of Heat-treatment on Accuracy of Infrared Spectroscopy and Digital and Optical Brix Refractometers for Measuring Immunoglobulin G Concentration in Bovine Colostrum.