The structural basis of protein folding and its links with human disease.

By Christopher M. Dobson. Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2001

929 citations recorded by the source corpus.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c264230afa703a90192054215c51d1f26b81e24e

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Citations in the corpus

Principles of protein folding, misfolding and aggregation. (2004, background): “Indeed, it is becoming increasingly evident that a wide range of human diseases is associated with aberrations in the folding process ( Table 1) [46,47].”
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution (2003, background): “The potential cytotoxicity of many aggregated proteins suggests that, in addition to providing cells with mechanisms to clear unfolded and misfolded proteins and to minimise their ability to induce toxicity, evolution must also have operated to eliminate protein sequences with a high intrinsic prope”
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (2002, background): “jpg" NDATA ITEM> ]> An increasing body of evidence suggests that amyloid formation is the fundamental cause of protein deposition diseases”
REVIEW : Recent advances in developing web-servers for predicting protein attributes (2009, background): “…to fold into the intended 3D structure usually produces inactive proteins or misfolded proteins [202] that may cause cell death and tissue damage [203] and be implicated in prion diseases such as bovine spongiform encephalopathy (BSE, also known as “mad cow disease”) in cattle and…”
Protein folding and misfolding (2003, background): “Failure to fold correctly, or to remain correctly folded, will therefore give rise to the malfunctioning of living systems and hence to diseas”
Folding proteins in fatal ways (2003, result): “This finding supports the concept that aggregation into β-sheet-rich fibrils is a generic property of polypeptide chains regardless of sequenc”
Intrinsically disordered proteins in human diseases: introducing the D2 concept. (2008, background): “Therefore, it has been proposed that fibrillation of a globular protein requires the destabilization of its rigid native structure, leading to partial unfolding and the formation of a partially unfolded conformation (7, 30, 31, 50, 77, 83, 112, 138, 142, 143).”