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Chemical chaperones assist intracellular folding to buffer mutational variations.

• Authors : Bandyopadhyay A; Institute of Genomics and Integrative Biology, Council of Scientific and Industrial Research, Delhi, India.; Saxena K

Subjects: Maltose-Binding Proteins/Maltose-Binding Proteins/Maltose-Binding Proteins/*chemistry ; Maltose-Binding Proteins/Maltose-Binding Proteins/Maltose-Binding Proteins/*genetics ; Methylamines/Methylamines/Methylamines/*pharmacology

• Source: Nature chemical biology [Nat Chem Biol] 2012 Jan 15; Vol. 8 (3), pp. 238-45. Date of Electronic Publication: 2012 Jan 15.Publisher: Nature Pub. Group Country of Publication: United States NLM ID: 101231976 Publication Model: Electronic Cited Medium: Internet ISSN:

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Protein folding: Chaperoning protein evolution.

• Authors : De Los Rios P; Goloubinoff P

Subjects: Maltose-Binding Proteins/Maltose-Binding Proteins/Maltose-Binding Proteins/*chemistry ; Maltose-Binding Proteins/Maltose-Binding Proteins/Maltose-Binding Proteins/*genetics ; Methylamines/Methylamines/Methylamines/*pharmacology

• Source: Nature chemical biology [Nat Chem Biol] 2012 Feb 15; Vol. 8 (3), pp. 226-8. Date of Electronic Publication: 2012 Feb 15.Publisher: Nature Pub. Group Country of Publication: United States NLM ID: 101231976 Publication Model: Electronic Cited Medium: Internet ISSN:

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Agricola

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Phenylketonuria as a protein misfolding disease: The mutation pG46S in phenylalanine hydroxylase promotes self-association and fibril formation.

• Authors : Leandro J; Department of Biomedicine, University of Bergen, Jonas Lies vei 91, N-5009 Bergen, Norway.; Simonsen N

Subjects: Mutation* ; Protein Folding*; Phenylalanine Hydroxylase/Phenylalanine Hydroxylase/Phenylalanine Hydroxylase/*chemistry

• Source: Biochimica et biophysica acta [Biochim Biophys Acta] 2011 Jan; Vol. 1812 (1), pp. 106-20. Date of Electronic Publication: 2010 Oct 16.Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print-Electronic Cited Medium: Print ISSN:

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Functional analysis of MUTYH mutated proteins associated with familial adenomatous polyposis.

• Authors : D'Agostino VG; Department of Genetics and Microbiology, University of Pavia, Pavia, Italy.; Minoprio A

Subjects: Mutation*; Adenomatous Polyposis Coli/Adenomatous Polyposis Coli/Adenomatous Polyposis Coli/*genetics ; DNA Glycosylases/DNA Glycosylases/DNA Glycosylases/*genetics

• Source: DNA repair [DNA Repair (Amst)] 2010 Jun 04; Vol. 9 (6), pp. 700-7. Date of Electronic Publication: 2010 Apr 24.Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101139138 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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