ArticleBiophysical journal2003
Protein aggregation/folding: the role of deterministic singularities of sequence hydrophobicity as determined by nonlinear signal analysis of acylphosphatase and Abeta(1-40).
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 42 citations in OpenAlex.
- Antimicrobial resistance in Klebsiella pneumoniae: identification of bacterial DNA adenine methyltransferase as a novel drug target from hypothetical proteins using subtractive genomics.Genomics & informatics · 2022Article
- Detecting transitions in protein dynamics using a recurrence quantification analysis based bootstrap method.BMC bioinformatics · 2017Article
- Classification model of amino acid sequences prone to aggregation of therapeutic proteins.In silico pharmacology · 2016Article
- Fluorescence spectroscopy of protein oligomerization in membranes.Journal of fluorescence · 2011Review
- Sequence signatures of allosteric proteins towards rational design.Systems and synthetic biology · 2010Article
- Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress.Biophysical journal · 2007Article
- Conformation of a peptide encompassing the proton translocation channel of vacuolar H(+)-ATPase.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The problem of protein folding vs. aggregation was investigated in acylphosphatase and the amyloid protein Abeta(1-40) by means of nonlinear signal analysis of their chain hydrophobicity. Numerical descriptors of recurrence patterns provided the basis for statistical evaluation of folding/aggregation distinctive features. Static and dynamic approaches were used to elucidate conditions coincident with folding vs. aggregation using comparisons with known protein secondary structure classifications, site-directed mutagenesis studies of acylphosphatase, and molecular dynamics simulations of amyloid protein, Abeta(1-40). The results suggest that a feature derived from principal component space characterized by the smoothness of singular, deterministic hydrophobicity patches plays a significant role in the conditions governing protein aggregation.
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Registered trials
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