Literature DB >> 15556268

Probing the origins, diagnosis and treatment of amyloid diseases using antibodies.

Mireille Dumoulin1, Christopher M Dobson.   

Abstract

The deposition of proteins in the form of amyloid fibrils is the characteristic feature of more than 20 medical conditions affecting the central nervous system or a variety of peripheral tissues. These disorders, which include Alzheimer's disease, the prion diseases and type II diabetes, are of enormous importance in the context of present-day human health and welfare. Extensive research is therefore being carried out to define the molecular details of the mechanism of the pathological conversion of amyloidogenic proteins from their soluble forms into fibrillar structures. This review focuses on recent studies that demonstrate the power of using antibodies or antibody fragments to probe the process of fibril formation, and discusses the emerging potential of these species as diagnostic and therapeutic agents.

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Year:  2004        PMID: 15556268     DOI: 10.1016/j.biochi.2004.09.012

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  13 in total

1.  Structural determination of Abeta25-35 micelles by molecular dynamics simulations.

Authors:  Xiang Yu; Qiuming Wang; Jie Zheng
Journal:  Biophys J       Date:  2010-07-21       Impact factor: 4.033

2.  Molecular basis of β-amyloid oligomer recognition with a conformational antibody fragment.

Authors:  Isabel Morgado; Karin Wieligmann; Magdalena Bereza; Raik Rönicke; Katrin Meinhardt; Karthikeyan Annamalai; Monika Baumann; Jessica Wacker; Peter Hortschansky; Miroslav Malešević; Christoph Parthier; Christian Mawrin; Cordelia Schiene-Fischer; Klaus G Reymann; Milton T Stubbs; Jochen Balbach; Matthias Görlach; Uwe Horn; Marcus Fändrich
Journal:  Proc Natl Acad Sci U S A       Date:  2012-07-18       Impact factor: 11.205

3.  Amphiphilic copolymers reduce aggregation of unfolded lysozyme more effectively than polyethylene glycol.

Authors:  Jaemin Chin; Devkumar Mustafi; Michael J Poellmann; Raphael C Lee
Journal:  Phys Biol       Date:  2017-02-08       Impact factor: 2.583

4.  Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant.

Authors:  Katarzyna Domanska; Saskia Vanderhaegen; Vasundara Srinivasan; Els Pardon; Florine Dupeux; Jose A Marquez; Sofia Giorgetti; Monica Stoppini; Lode Wyns; Vittorio Bellotti; Jan Steyaert
Journal:  Proc Natl Acad Sci U S A       Date:  2011-01-10       Impact factor: 11.205

5.  Structure of an early native-like intermediate of β2-microglobulin amyloidogenesis.

Authors:  Saskia Vanderhaegen; Marcus Fislage; Katarzyna Domanska; Wim Versées; Els Pardon; Vittorio Bellotti; Jan Steyaert
Journal:  Protein Sci       Date:  2013-08-20       Impact factor: 6.725

6.  Localization of a conformational epitope common to non-native and fibrillar immunoglobulin light chains.

Authors:  Brian O'Nuallain; Amy Allen; Stephen J Kennel; Deborah T Weiss; Alan Solomon; Jonathan S Wall
Journal:  Biochemistry       Date:  2007-02-06       Impact factor: 3.162

7.  A camelid anti-PrP antibody abrogates PrP replication in prion-permissive neuroblastoma cell lines.

Authors:  Daryl Rhys Jones; William Alexander Taylor; Clive Bate; Monique David; Mourad Tayebi
Journal:  PLoS One       Date:  2010-03-22       Impact factor: 3.240

8.  Phage display and peptide mapping of an immunoglobulin light chain fibril-related conformational epitope.

Authors:  Brian O'Nuallain; Amy Allen; Demet Ataman; Deborah T Weiss; Alan Solomon; Jonathan S Wall
Journal:  Biochemistry       Date:  2007-10-18       Impact factor: 3.162

9.  Unfolding, aggregation, and amyloid formation by the tetramerization domain from mutant p53 associated with lung cancer.

Authors:  Yuichiro Higashimoto; Yuya Asanomi; Satoru Takakusagi; Marc S Lewis; Kohei Uosaki; Stewart R Durell; Carl W Anderson; Ettore Appella; Kazuyasu Sakaguchi
Journal:  Biochemistry       Date:  2006-02-14       Impact factor: 3.162

Review 10.  The amyloid state and its association with protein misfolding diseases.

Authors:  Tuomas P J Knowles; Michele Vendruscolo; Christopher M Dobson
Journal:  Nat Rev Mol Cell Biol       Date:  2014-06       Impact factor: 94.444

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