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Protein Engineering Design and Selection is a peer-reviewed journal published by Oxford University Press, covering Protein Structure and Dynamics, Monoclonal and Polyclonal Antibodies Research, Enzyme Structure and Function.
| Publisher | Oxford University Press |
|---|---|
| Reference style | Author–year (OUP) Author–year — (Smith, 2023) in the text Smith, A., Jones, B. and Lee, C. (2023) 'A representative article title', Protein Engineering Design and Selection, 12(3), pp. 45–58.
Formats any DOI in the closest standard style — Protein Engineering Design and Selection has no published style definition, so this is an approximation. No sign-up. |
| Publishes research in | Protein Structure and Dynamics Monoclonal and Polyclonal Antibodies Research Enzyme Structure and Function Glycosylation and Glycoproteins Research RNA and protein synthesis mechanisms |
| ISSN | 1741-0126 |
| Citation impact (2-yr) | 2.98 |
| h-index | 159 |
| i10-index | 2,774 |
| Total citations | 181,345 |
| Top institutions publishing here | Centre National de la Recherche Scientifique |
| Journal website | academic.oup.com |
| You get | A submission-ready PDF and the editable LaTeX source — ready to submit. |
Citations each year’s papers have accumulated so far — the most recent years are still building up.
The LIGPLOT program automatically generates schematic 2-D representations of protein-ligand complexes from standard Protein Data Bank file input. The output is a colour, or black-and-white, PostScript file giving a simple and informative representation of the intermolecular interactions and their strengths, including hydrogen bonds, hydrophobic interactions and atom accessibilities. The program is completely general for any…
We have developed a new method for the identification of signal peptides and their cleavage sites based on neural networks trained on separate sets of prokaryotic and eukaryotic sequence. The method performs significantly better than previous prediction schemes and can easily be applied on genome-wide data sets. Discrimination between cleaved signal peptides and uncleaved N-terminal…
We have identified a new protein fold--the alpha/beta hydrolase fold--that is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is similar: an alpha/beta sheet, not barrel, of eight beta-sheets connected by alpha-helices. These enzymes have diverged from a common ancestor so as to preserve the…
A new algorithm is reported which builds an alignment between two protein structures. The algorithm involves a combinatorial extension (CE) of an alignment path defined by aligned fragment pairs (AFPs) rather than the more conventional techniques using dynamic programming and Monte Carlo optimization. AFPs, as the name suggests, are pairs of fragments, one from each…
Sequence alignments unambiguously distinguish between protein pairs of similar and non-similar structure when the pairwise sequence identity is high (>40% for long alignments). The signal gets blurred in the twilight zone of 20-35% sequence identity. Here, more than a million sequence alignments were analysed between protein pairs of known structures to re-define a line distinguishing…
