Current Opinion in Structural Biology (CURR OPIN STRUC BIOL)

Publisher: Elsevier

Journal description

Current Opinion in Structural Biology contains: Over 90 reviews from leading international contributors Web alerts of hot sites Paper alert service - the latest exciting papers Evaluated reference lists for all articles Annual author and subject index Online Fully searchable Access back issues Numerous links Search and read all issues published since 1984, giving you access to your own reference library without leaving your desk. Save valuable time by exploring our links to MEDLINE and numerous websites. Check out contents and abstracts FREE

Current impact factor: 7.20

Impact Factor Rankings

2016 Impact Factor Available summer 2017
2014 / 2015 Impact Factor 7.201
2013 Impact Factor 8.747
2012 Impact Factor 8.738
2011 Impact Factor 9.424
2010 Impact Factor 9.903
2009 Impact Factor 9.344
2008 Impact Factor 9.06
2007 Impact Factor 10.15
2006 Impact Factor 11.215
2005 Impact Factor 9.559
2004 Impact Factor 9.821
2003 Impact Factor 8.686
2002 Impact Factor 9.63
2001 Impact Factor 10.893
2000 Impact Factor 10.427
1999 Impact Factor 8.633
1998 Impact Factor 8.69
1997 Impact Factor 7.509

Impact factor over time

Impact factor
Year

Additional details

5-year impact 8.08
Cited half-life 8.10
Immediacy index 1.24
Eigenfactor 0.03
Article influence 4.05
Website Current Opinion in Structural Biology website
Other titles Bibliography of the current world literature., Current opinion in structural biology, Structural biology
ISSN 1879-033X
OCLC 23812553
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details

Elsevier

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Authors pre-print on any website, including arXiv and RePEC
    • Author's post-print on author's personal website immediately
    • Author's post-print on open access repository after an embargo period of between 12 months and 48 months
    • Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months
    • Author's post-print may be used to update arXiv and RepEC
    • Publisher's version/PDF cannot be used
    • Must link to publisher version with DOI
    • Author's post-print must be released with a Creative Commons Attribution Non-Commercial No Derivatives License
    • Publisher last reviewed on 03/06/2015
  • Classification
    green

Publications in this journal

  • [Show abstract] [Hide abstract] ABSTRACT: The N-formyltransferases, also known as transformylases, play key roles in de novo purine biosynthesis where they catalyze the transfer of formyl groups to primary amine acceptors. These enzymes require N10-formyltetrahydrofolate for activity. Due to their biological importance they have been extensively investigated for many years, and they are still serving as targets for antifolate drug design. Most of our understanding of the N-formyltransferases has been derived from these previous studies. It is now becoming increasingly apparent, however, that N-formylation also occurs on some amino sugars found on the O-antigens of pathogenic bacteria. This review focuses on recent developments in the biochemical and structural characterization of the sugar N-formyltransferases.
    No preview · Article · Dec 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Computational structure-based protein design programs are becoming an increasingly important tool in molecular biology. These programs compute protein sequences that are predicted to fold to a target structure and perform a desired function. The success of a program's predictions largely relies on two components: first, the input biophysical model, and second, the algorithm that computes the best sequence(s) and structure(s) according to the biophysical model. Improving both the model and the algorithm in tandem is essential to improving the success rate of current programs, and here we review recent developments in algorithms for protein design, emphasizing how novel algorithms enable the use of more accurate biophysical models. We conclude with a list of algorithmic challenges in computational protein design that we believe will be especially important for the design of therapeutic proteins and protein assemblies.
    No preview · Article · Aug 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Biological membranes form barriers that are essential for cellular integrity and compartmentalisation. Proteins in the membrane have co-evolved with their hydrophobic lipid environment, which serves as a solvent for proteins with very diverse requirements. As a result, their interactions range from non-selective to highly discriminating. Mass spectrometry enables us to monitor how lipids interact with membrane proteins and assess their effects on structure and dynamics. Recent studies illustrate the ability to differentiate specific lipid binding, preferential interactions with lipid subsets, and nonselective annular contacts. Here, we consider the biological implications of different lipid-binding scenarios and propose that binding occurs on a sliding selectivity scale, in line with the view of biological membranes as facilitators of dynamic protein and lipid organization.
    No preview · Article · Aug 2016 · Current Opinion in Structural Biology
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    [Show abstract] [Hide abstract] ABSTRACT: Protein self-assembly is extensively used in nature to build functional biomolecules and provides a general approach to design molecular complexes with many intriguing applications. Although computational design of protein-protein interfaces remains difficult, much progress has recently been made in de novo design of protein assemblies with cyclic, helical, cubic, internal and lattice symmetries. Here, we discuss some of the underlying biophysical principles of self-assembly that influence the design problem and highlight methodological advances that have made self-assembly design a fruitful area of protein design.
    Preview · Article · Aug 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Photosystem I (PSI) is one of the two photosystems in oxygenic photosynthesis, and absorbs light energy to generate reducing power for the reduction of NADP(+) to NADPH with a quantum efficiency close to 100%. The plant PSI core forms a supercomplex with light-harvesting complex I (LHCI) with a total molecular weight of over 600kDa. Recent X-ray structure analysis of the PSI-LHCI membrane-protein supercomplex has revealed detailed arrangement of the light-harvesting pigments and other cofactors especially within LHCI. Here we introduce the overall structure of the PSI-LHCI supercomplex, and then focus on the excited energy transfer (EET) pathways from LHCI to the PSI core and photoprotection mechanisms based on the structure obtained.
    No preview · Article · Aug 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: The availability of vast amounts of protein sequence data facilitates detection of subtle statistical correlations due to imposed structural and functional constraints. Recent breakthroughs using Direct Coupling Analysis (DCA) and related approaches have tapped into correlations believed to be due to compensatory mutations. This has yielded some remarkable results, including substantially improved prediction of protein intra- and inter-domain 3D contacts, of membrane and globular protein structures, of substrate binding sites, and of protein conformational heterogeneity. A complementary approach is Bayesian Partitioning with Pattern Selection (BPPS), which partitions related proteins into hierarchically-arranged subgroups based on correlated residue patterns. These correlated patterns are presumably due to structural and functional constraints associated with evolutionary divergence rather than to compensatory mutations. Hence joint application of DCA- and BPPS-based approaches should help sort out the structural and functional constraints contributing to sequence correlations.
    No preview · Article · Jun 2016 · Current Opinion in Structural Biology
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    [Show abstract] [Hide abstract] ABSTRACT: In this formula, dm is the resolution limit of an image where the particles within it have moved in random directions, but on average by a distance r [23]. S is the signal to noise ratio required to distinguish a particular feature in the image. Here we make the simplifying assumption that the particle velocity can be approximated as being constant during image acquisition. For a signal to noise ratio of ln S = 2 and using previous measurements of average particle movement r [20• and 21••], we use Equation (1) to calculate the resolution limits plotted in Figure 1b (dashed lines). Compared to other limits on resolution, it is clear that movement is more limiting than either the wavelength of the electron or the optics of the microscope. This illustrates another important improvement in cryo-EM due to the development of direct-electron detectors. By splitting the micrographs in time into movies, tracking the movement of the particles and then compensating for the movement using image correction algorithms, the effective particle movement, r, can be reduced [17•, 18, 19 and 32]. This lowers the resolution limit, dm, imposed by that movement and accounts for the improved resolution with direct electron detectors versus film which cannot be explained by increased detector efficiency alone.
    Full-text · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Short helical peptides combine characteristics of small molecules and large proteins and provide an exciting area of opportunity in protein design. A growing number of studies report novel helical peptide inhibitors of protein-protein interactions. New techniques have been developed for peptide design and for chemically stabilizing peptides in a helical conformation, which frequently improves protease resistance and cell permeability. We summarize advances in peptide crosslinking chemistry and give examples of peptide design studies targeting coiled-coil transcription factors, Bcl-2 family proteins, MDM2/MDMX, and HIV gp41, among other targets.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Intramembrane proteases catalyze hydrolysis of peptide bond within the lipid bilayer and play a key role in a variety of cellular processes. These membrane-embedded enzymes comprise four major classes: rhomboid serine proteases, site-2 metalloproteases, Rce1-type glutamyl proteases, and aspartyl proteases exemplified by signal peptide peptidase and γ-secretase. In the past several years, three-dimensional structures of representative members of these four classes of intramembrane protease have been reported at atomic resolutions, which reveal distinct protein folds and active site configurations. These structures, together with structure-guided biochemical analyses, shed light on the working mechanisms of water access and substrate entry. In this review, we discuss the shared as well as unique features of these intramembrane proteases, with a focus on presenilin — the catalytic component of γ-secretase.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Dynamic expression of the genome requires coordinated binding of chromatin factors and enzymes that carry out genome-templated processes. Until recently, the molecular mechanisms governing how these factors and enzymes recognize and act on the fundamental unit of chromatin, the nucleosome core particle, have remained a mystery. A small, yet growing set of structures of the nucleosome in complex with chromatin factors and enzymes highlights the importance of multivalency in defining nucleosome binding and specificity. Many such interactions include an arginine anchor motif, which targets a unique acidic patch on the nucleosome surface. These emerging paradigms for chromatin recognition will be discussed, focusing on several recent structural breakthroughs.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Regulatory protein–protein interactions are ubiquitous in biology, and small molecule protein–protein interaction inhibitors are an important focus in drug discovery. Remarkably little attention has been given to the opposite strategy — stabilization of protein–protein interactions, despite the fact that several well-known therapeutics act through this mechanism. From a structural perspective, we consider representative examples of small molecules that induce or stabilize the association of protein domains to inhibit, or alter, signaling for nuclear hormone, GTPase, kinase, phosphatase, and ubiquitin ligase pathways. These SPLINTS (small-molecule protein ligand interface stabilizers) drive interactions that are in some cases physiologically relevant, and in others entirely adventitious. The diverse structural mechanisms employed suggest approaches for a broader and systematic search for such compounds in drug discovery.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Helical filamentous assembly is ubiquitous in biology, but was only recently realized to be broadly employed in the innate immune system of vertebrates. Accumulating evidence suggests that the filamentous assemblies and helical oligomerization play important roles in detection of foreign nucleic acids and activation of the signaling pathways to produce antiviral and inflammatory mediators. In this review, we focus on the helical assemblies observed in the signaling pathways of RIG-I-like receptors (RLRs) and AIM2-like receptors (ALRs). We describe ligand-dependent oligomerization of receptor, receptor-dependent oligomerization of signaling adaptor molecules, and their functional implications and regulations.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Discrete Molecular Dynamics (DMD) is a physics-based simulation method using discrete energetic potentials rather than traditional continuous potentials, allowing microsecond time scale simulations of biomolecular systems to be performed on personal computers rather than supercomputers or specialized hardware. With the ongoing explosion in processing power even in personal computers, applications of DMD have similarly multiplied. In the past two years, researchers have used DMD to model structures of disease-implicated protein folding intermediates, study assembly of protein complexes, predict protein-protein binding conformations, engineer rescue mutations in disease-causative protein mutants, design a protein conformational switch to control cell signaling, and describe the behavior of polymeric dispersants for environmental cleanup of oil spills, among other innovative applications.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: The intrinsic flexibility of proteins and nucleic acids can be grasped from remarkably simple mechanical models of particles connected by springs. In recent decades, Elastic Network Models (ENMs) combined with Normal Model Analysis widely confirmed their ability to predict biologically relevant motions of biomolecules and soon became a popular methodology to reveal large-scale dynamics in multiple structural biology scenarios. The simplicity, robustness, low computational cost, and relatively high accuracy are the reasons behind the success of ENMs. This review focuses on recent advances in the development and application of ENMs, paying particular attention to combinations with experimental data. Successful application scenarios include large macromolecular machines, structural refinement, docking, and evolutionary conservation.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Design of proteins has far-reaching potentials in diverse areas that span repurposing of the protein scaffold for reactions and substrates that they were not naturally meant for, to catching a glimpse of the ephemeral proteins that nature might have sampled during evolution. These non-natural proteins, either in synthesized or virtual form have opened the scope for the design of entities that not only rival their natural counterparts but also offer a chance to visualize the protein space continuum that might help to relate proteins and understand their associations. Here, we review the recent advances in protein engineering and design, in multiple areas, with a view to drawing attention to their future potential.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology
  • [Show abstract] [Hide abstract] ABSTRACT: Microtubules (MTs) have been the subject of cryo-electron microscopy (cryo-EM) studies since the birth of this technique. Although MTs pose some unique challenges, having to do with the presence of a MT seam, lattice variability and disorder, MT cryo-EM reconstructions are steadily improving in resolution and providing exciting new insights into MT structure and function. Recent work has lead to the atomic-detail visualization of lateral contacts between tubulin subunits and the conformational changes that give rise to strain in the MT lattice accompanying GTP hydrolysis. Cryo-EM has also been invaluable in describing the interactions between MTs and MT associated proteins (MAPs), which function to regulate MT dynamic instability, move cargoes, or contribute to other MT cellular processes.
    No preview · Article · Apr 2016 · Current Opinion in Structural Biology