Literature DB >> 15627377

Antibodies as specific chaperones.

D N Ermolenko1, A V Zherdev, B B Dzantiev.   

Abstract

Protein folding is often accompanied by formation of non-native conformations leading to protein aggregation. A number of reports indicate that antibodies can facilitate folding and prevent aggregation of protein antigens. The influence of antibodies on folding is strictly antigen specific. Chaperone-like antibody activity may be due to the stabilization of native antigen conformations or folding transition states, or screening of aggregating hydrophobic surfaces. Taking advantage of chaperone-like activity of antibodies for immunotherapy may prove to be a promising approach to the treatment of Alzheimer's and prion-related diseases. Antibody-assisted folding may enhance renaturation of recombinant proteins from inclusion bodies.

Entities:  

Mesh:

Substances:

Year:  2004        PMID: 15627377     DOI: 10.1007/s10541-005-0069-4

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  8 in total

Review 1.  Chaperone-like antibodies in neurodegenerative tauopathies: implication for immunotherapy.

Authors:  Eva Kontsekova; Natalia Ivanovova; Martina Handzusova; Michal Novak
Journal:  Cell Mol Neurobiol       Date:  2009-02-13       Impact factor: 5.046

2.  Protease-stable DARPins as promising oral therapeutics.

Authors:  Rudo A Simeon; Yu Zeng; Vikas Chonira; Andrea Martinez Aguirre; Mauricio Lasagna; Marko Baloh; Joseph A Sorg; Cecilia Tommos; Zhilei Chen
Journal:  Protein Eng Des Sel       Date:  2021-02-15       Impact factor: 1.952

3.  Angiotensin I-converting enzyme Gln1069Arg mutation impairs trafficking to the cell surface resulting in selective denaturation of the C-domain.

Authors:  Sergei M Danilov; Sergey Kalinin; Zhenlong Chen; Elena I Vinokour; Andrew B Nesterovitch; David E Schwartz; Olivier Gribouval; Marie-Claire Gubler; Richard D Minshall
Journal:  PLoS One       Date:  2010-05-03       Impact factor: 3.240

4.  A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.

Authors:  Erwin De Genst; Pak-Ho Chan; Els Pardon; Shang-Te D Hsu; Janet R Kumita; John Christodoulou; Linda Menzer; Dimitri Y Chirgadze; Carol V Robinson; Serge Muyldermans; André Matagne; Lode Wyns; Christopher M Dobson; Mireille Dumoulin
Journal:  J Phys Chem B       Date:  2013-09-24       Impact factor: 2.991

Review 5.  Biotechnological applications of recombinant single-domain antibody fragments.

Authors:  Ario de Marco
Journal:  Microb Cell Fact       Date:  2011-06-09       Impact factor: 5.328

6.  Amyloid oligomer conformation in a group of natively folded proteins.

Authors:  Yuji Yoshiike; Ryoichi Minai; Yo Matsuo; Yun-Ru Chen; Tetsuya Kimura; Akihiko Takashima
Journal:  PLoS One       Date:  2008-09-18       Impact factor: 3.240

7.  A study of the mechanism of the chaperone-like function of an scFv of human creatine kinase by computer simulation.

Authors:  Jianyu Feng; Hong Guo; Sen Li; Tun Lu
Journal:  PLoS One       Date:  2013-04-24       Impact factor: 3.240

8.  IgG Conformer's Binding to Amyloidogenic Aggregates.

Authors:  Monichan Phay; Alfred T Welzel; Angela D Williams; Helen P McWilliams-Koeppen; Veronika Blinder; Tiernan T O'Malley; Alan Solomon; Dominic M Walsh; Brian O'Nuallain
Journal:  PLoS One       Date:  2015-09-14       Impact factor: 3.240

  8 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.