Current Opinion in Structural Biology Journal Impact Factor & Information

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: 8.75

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 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

Additional details

5-year impact 9.02
Cited half-life 7.20
Immediacy index 1.45
Eigenfactor 0.04
Article influence 4.60
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


  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Pre-print allowed on any website or open access repository
    • Voluntary deposit by author of authors post-print allowed on authors' personal website, or institutions open scholarly website including Institutional Repository, without embargo, where there is not a policy or mandate
    • Deposit due to Funding Body, Institutional and Governmental policy or mandate only allowed where separate agreement between repository and the publisher exists.
    • 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 .
    • Set statement to accompany deposit
    • Published source must be acknowledged
    • Must link to journal home page or articles' DOI
    • Publisher's version/PDF cannot be used
    • Articles in some journals can be made Open Access on payment of additional charge
    • NIH Authors articles will be submitted to PubMed Central after 12 months
    • Publisher last contacted on 18/10/2013
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: We discuss recent approaches for structure-based protein function annotation. We focus on template-based methods where the function of a query protein is deduced from that of a template for which both the structure and function are known. We describe the different ways of identifying a template. These are typically based on sequence analysis but new methods based on purely structural similarity are also being developed that allow function annotation based on structural relationships that cannot be recognized by sequence. The growing number of available structures of known function, improved homology modeling techniques and new developments in the use of structure allow template-based methods to be applied on a proteome-wide scale and in many different biological contexts. This progress significantly expands the range of applicability of structural information in function annotation to a level that previously was only achievable by sequence comparison. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 06/2015; 32. DOI:10.1016/
  • Current Opinion in Structural Biology 05/2015; 32:S0959-440. DOI:10.1016/
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    ABSTRACT: Native mass spectrometry (MS) and ion mobility MS provide a way to discriminate between various allosteric mechanisms that cannot be distinguished using ensemble measurements of ligand binding in bulk protein solutions. Native MS, which yields mass measurements of intact assemblies, can be used to determine the values of ligand binding constants of multimeric allosteric proteins, thereby providing a way to distinguish, for example, between concerted and sequential allosteric models. Native MS can also be employed to study cooperativity owing to ligand-modulated protein oligomerization. The rotationally averaged cross-section areas of complexes obtained by ion mobility MS can be used to distinguish between induced fit and conformational selection. Native MS and its allied techniques are, therefore, becoming increasingly powerful tools for dissecting allosteric mechanisms. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 05/2015; 34:7-16. DOI:10.1016/
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    ABSTRACT: During its contraction cycle, the myosin motor catalyzes the hydrolysis of ATP. Several combined quantum/classical mechanics (QM/MM) studies of this step have been published, which substantially contributed to our thinking about the catalytic mechanism. The methodological difficulties encountered over the years in the simulation of this complex reaction are now understood: (a) Polarization of the protein peptide groups surrounding the highly charged ATP(4-) cannot be neglected. (b) Some unsuspected protein groups need to be treated QM. (c) Interactions with the γ-phosphate versus the β-phosphate favor a concurrent versus a sequential mechanism, respectively. Thus, these practical aspects strongly influence the computed mechanism, and should be considered when studying other catalyzed phosphor-ester hydrolysis reactions, such as in ATPases or GTPases. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 05/2015; 31:115-123. DOI:10.1016/
  • Current Opinion in Structural Biology 05/2015; DOI:10.1016/
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    ABSTRACT: Polyproteins are chains of covalently conjoined smaller proteins that occur in nature as versatile means to organize the proteome of viruses including HIV. During maturation, viral polyproteins are typically cleaved into the constituent proteins with different biological functions by highly specific proteases, and structural analyses at defined stages of this maturation process can provide clues for antiviral intervention strategies. Recombinant polyproteins that use similar mechanisms are emerging as powerful tools for producing hitherto inaccessible protein targets such as the influenza polymerase, for high-resolution structure determination by X-ray crystallography. Conversely, covalent linking of individual protein subunits into single polypeptide chains are exploited to overcome sample preparation bottlenecks. Moreover, synthetic polyproteins provide a promising tool to dissect dynamic folding of polypeptide chains into three-dimensional architectures in single-molecule structure analysis by atomic force microscopy (AFM). The recent use of natural and synthetic polyproteins in structural biology and major achievements are highlighted in this contribution. Crown Copyright © 2015. Published by Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 05/2015; 32:139-146. DOI:10.1016/
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    ABSTRACT: Currently, membrane proteins only comprise 1.5% of the protein data bank and, thus, still remain a challenge for structural biologists. Expression, stabilization in membrane mimics (e.g. detergent), heterogeneity (conformational and chemical), and crystallization in the presence of a membrane mimic are four major bottlenecks encountered. In response, several post-expression protein modifications have been utilized to facilitate structure determination of membrane proteins. This review highlights four approaches: limited proteolysis, deglycosylation, cysteine alkylation, and lysine methylation. Combined these approaches have facilitated the structure determination of more than 40 membrane proteins and, therefore, are a useful addition to the membrane protein structural biologist's toolkit. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 05/2015; 32:131-138. DOI:10.1016/
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    ABSTRACT: Antiviral restriction factors are an integral part of the host innate immune system that protects cells from viral pathogens, such as human immunodeficiency virus (HIV). Studies of the interactions between restriction factors and HIV have greatly advanced our understanding of both the viral life cycle and basic cell biology, as well as provided new opportunities for therapeutic intervention of viral infection. Here we review the recent developments towards establishing the structural and biochemical bases of HIV inhibition by, and viral countermeasures of, the restriction factors TRIM5, MxB, APOBEC3, SAMHD1, and BST2/tetherin. Copyright © 2015. Published by Elsevier Ltd.
    Current Opinion in Structural Biology 05/2015; 31:106-114. DOI:10.1016/
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    ABSTRACT: A major goal of self-assembly research is the synthesis of biomolecular structures with diverse, intricate features across multiple length scales. Designing self-assembly processes becomes more difficult as the number of species or target structure size increases. Just as the ordered assembly of a machine or device makes complex manufacturing possible, ordered (or 'algorithmic') biomolecular self-assembly processes could enable the self-assembly of more complex structures. We discuss the design of ordered assembly processes with particular attention to DNA and RNA. The assembly of complexes can be ordered using selective, multivalent interactions or active components that change shape after assembly. The self-assembly of spatial gradients driven by reaction-diffusion can also be ordered. We conclude by considering topics for future research. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 04/2015; 31. DOI:10.1016/
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    ABSTRACT: Inflammasomes are caspase-1 activating, molecular inflammatory machines that proteolytically mature pro-inflammatory cytokines and induce pyroptotic cell death during innate immune responses. Recent structural studies of proteins that constitute inflammasomes have yielded fresh insights into their assembly mechanisms. In particular, these include a crystal structure of the CARD-containing NOD-like receptor NLRC4, the crystallographic and electron microscopy (EM) studies of the dsDNA sensors AIM2 and IFI16, and of the regulatory protein p202, and the cryo-EM filament structure of the PYD domain of the inflammasome adapter ASC. These data suggest inflammasome assembly that starts with ligand recognition and release of autoinhibition followed by step-wise rounds of nucleated polymerization from the sensors to the adapters, then to caspase-1. In this elegant manner, inflammasomes form by an 'all-or-none' cooperative mechanism, thereby amplifying the activation of caspase-1. The dense network of filamentous structures predicted by this model has been observed in cells as micron-sized puncta. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 04/2015; 31. DOI:10.1016/
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    ABSTRACT: Active transport of materials across the cellular membrane is one the most fundamental processes in biology. In order to accomplish this task, membrane transporters rely on a wide range of conformational changes spanning multiple time and size scales. These molecular events govern key functional aspects in membrane transporters, namely, coordinated gating motions underlying the alternating access mode of operation, and coupling of uphill transport of substrate to various sources of energy, for example, transmembrane electrochemical gradients and ATP binding and hydrolysis. Computational techniques such as molecular dynamics simulations and free energy calculations have equipped us with a powerful repertoire of biophysical tools offering unparalleled spatial and temporal resolutions that can effectively complement experimental methodologies, and therefore help fill the gap of knowledge in understanding the molecular basis of function in membrane transporters. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 04/2015; 31:96-105. DOI:10.1016/
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    ABSTRACT: Most membrane-proteins exist in complexes rather than isolated entities. To fully understand their biological function it is essential to study the intact membrane-protein assemblies. The overexpression and purification of many essential membrane-protein complexes is still a considerable and often unsurmountable challenge. In these cases, extraction from source is the only option for many large multi-subunit cellular machines. Here, we describe recent advances in overexpression of multi-subunit membrane-protein complexes, the strategies to stabilize these complexes and highlight major achievements in membrane-protein structural research that were facilitated by the prospect of achieving subnanometer to near-atomic resolution by electron cryo-microscopy. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 04/2015; 32:123-130. DOI:10.1016/
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    ABSTRACT: Over the past decade, there has been a rapid rise in the use of three-dimensional (3D) animation to depict molecular and cellular processes. Much of the growth in molecular animation has been in the educational arena, but increasingly, 3D animation software is finding its way into research laboratories. In this review, I will discuss a number of ways in which 3d animation software can play a valuable role in visualizing and communicating macromolecular structures and dynamics. I will also consider the challenges of using animation tools within the research sphere. Copyright © 2015. Published by Elsevier Ltd.
    Current Opinion in Structural Biology 04/2015; 31:84-88. DOI:10.1016/
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    ABSTRACT: Botulinum neurotoxins (BoNTs) are extremely poisonous protein toxins that cause the fatal paralytic disease botulism. They are naturally produced in bacteria with several nontoxic neurotoxin-associated proteins (NAPs) and together they form a progenitor toxin complex (PTC), the largest bacterial toxin complex known. In foodborne botulism, the PTC functions as a molecular machine that helps BoNT breach the host defense in the gut. Here, we discuss the substantial recent advance in elucidating the atomic structures and assembly of the 14-subunit PTC, including structures of BoNT and four NAPs. These structural studies shed light on the molecular mechanisms by which BoNT is protected against the acidic environment and proteolytic destruction in the gastrointestinal tract, and how it is delivered across the intestinal epithelial barrier. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 04/2015; 31:89-95. DOI:10.1016/
  • Current Opinion in Structural Biology 04/2015; 30. DOI:10.1016/
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    ABSTRACT: Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the development of new isotopic labeling strategies has opened the possibility of exploiting NMR spectroscopy in the study of supra-molecular complexes with molecular weights of up to 1MDa. At the core of these isotopic labeling developments is the specific introduction of [(1)H,(13)C]-labeled methyl probes into perdeuterated proteins. Here, we describe the evolution of these approaches and discuss their impact on structural and biological studies. The relevant protocols are succinctly reviewed for single and combinatorial isotopic-labeling of methyl-containing residues, and examples of applications on challenging biological systems, including high molecular weight and membrane proteins, are presented. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 04/2015; 32:113-122. DOI:10.1016/
  • Current Opinion in Structural Biology 03/2015; 30. DOI:10.1016/