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
Year

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

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: A computational protein-protein docking method that predicts atomic details of protein-protein interactions from protein monomer structures is an invaluable tool for understanding the molecular mechanisms of protein interactions and for designing molecules that control such interactions. Compared to low-resolution docking, high-resolution docking explores the conformational space in atomic resolution to provide predictions with atomic details. This allows for applications to more challenging docking problems that involve conformational changes induced by binding. Recently, high-resolution methods have become more promising as additional information such as global shapes or residue contacts are now available from experiments or sequence/structure data. In this review article, we highlight developments in high-resolution docking made during the last decade, specifically regarding global optimization methods employed by the docking methods. We also discuss two major challenges in high-resolution docking: prediction of backbone flexibility and water-mediated interactions. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 08/2015; 35:24-31. DOI:10.1016/j.sbi.2015.08.001
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    ABSTRACT: Mitochondria comprise two membrane systems, a bordering outer membrane and an invaginated inner membrane containing the oxidative phosphorylation machinery for ATP synthesis. Most mitochondrial membrane proteins are produced as precursors in the cytosolic compartment of the cell and imported into the organelle, whereas only few proteins are synthesized in the mitochondrial matrix. The topologically correct integration of hydrophobic precursor proteins into phospholipid bilayers is a particular challenge for protein translocation systems. Because of this mechanistic complexity, membrane proteins with distinct transmembrane topologies require profoundly different biogenesis pathways. Here we discuss recent findings on the structure and function of the diverse molecular machineries for mitochondrial membrane protein insertion. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 08/2015; 33:92-102. DOI:10.1016/j.sbi.2015.07.013
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    ABSTRACT: Single-molecule Förster resonance energy transfer (smFRET) serves as a molecular ruler that is ideally posed to study static and dynamic heterogeneity in living cells. Observing smFRET in cells requires appropriately integrated labeling, internalization and imaging strategies, and significant progress has been made towards that goal. Pioneering studies have demonstrated smFRET detection in both prokaryotic and eukaryotic systems, using both wide-field and confocal microscopies, and have started to answer exciting biological questions. We anticipate that future technical developments will open the door to smFRET for the study of structure, conformational changes and kinetics of biomolecules in living cells. Copyright © 2015. Published by Elsevier Ltd.
    Current Opinion in Structural Biology 08/2015; 34:52-59. DOI:10.1016/j.sbi.2015.07.001
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    ABSTRACT: N-methyld-aspartate receptors (NMDARs) belong to the large family of ionotropic glutamate receptors (iGluRs), which are critically involved in basic brain functions as well as multiple neurological diseases and disorders. The NMDARs are large heterotetrameric membrane protein complexes. The extensive extracellular domains recognize neurotransmitter ligands and allosteric compounds and translate the binding information to regulate activity of the transmembrane ion channel. Here, we review recent advances in the structural biology of NMDARs with a focus on pharmacology and function. Structural analysis of the isolated extracellular domains in combination with the intact heterotetrameric NMDAR structure provides important insights into how this sophisticated ligand-gated ion channel may function. Copyright © 2015. Published by Elsevier Ltd.
    Current Opinion in Structural Biology 08/2015; 33:68-75. DOI:10.1016/j.sbi.2015.07.012
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    ABSTRACT: Diverse cell biological processes that involve shaping and remodeling of cell membranes are regulated by membrane lateral tension. Here we focus on the role of tension in driving membrane fusion. We discuss the physics of membrane tension, forces that can generate the tension in plasma membrane of a cell, and the hypothesis that tension powers expansion of membrane fusion pores in late stages of cell-to-cell and exocytotic fusion. We propose that fusion pore expansion can require unusually large membrane tensions or, alternatively, low line tensions of the pore resulting from accumulation in the pore rim of membrane-bending proteins. Increase of the inter-membrane distance facilitates the reaction. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 08/2015; 33:61-67. DOI:10.1016/j.sbi.2015.07.010
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    ABSTRACT: Cells from all domains of life encode energy-dependent trans-membrane transporters that can expel harmful substances including clinically applied therapeutic agents. As a collective body, these transporters perform as a super-system that confers tolerance to an enormous range of harmful compounds and consequently aid survival in hazardous environments. In the Gram-negative bacteria, some of these transporters serve as energy-transducing components of tripartite assemblies that actively efflux drugs and other harmful compounds, as well as deliver virulence agents across the entire cell envelope. We draw together recent structural and functional data to present the current models for the transport mechanisms for the main classes of multi-drug transporters and their higher-order assemblies. Copyright © 2015 The Authors. Published by Elsevier Ltd.. All rights reserved.
    Current Opinion in Structural Biology 08/2015; 33:76-91. DOI:10.1016/j.sbi.2015.07.015
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    ABSTRACT: Enveloped viruses enter the cell by fusing their envelope with a cellular membrane. Fusion is catalyzed by conformational changes of viral glycoproteins from pre-fusion to post-fusion states. Structural studies have defined three classes of viral fusion glycoproteins. Class III comprises the fusion glycoproteins from rhabdoviruses (G), herpesviruses (gB), and baculoviruses (GP64). Although sharing the same fold, those glycoproteins exhibit striking differences in their modes of activation and interaction with the target membrane. Furthermore, for gB and GP64, only the post-fusion structure is known and the extent of their conformational change is still an unresolved issue. Further structural studies are therefore required to get a detailed insight in the working of those fusion machines. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 08/2015; 33:52-60. DOI:10.1016/j.sbi.2015.07.011
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    ABSTRACT: There is an unprecedented interest in glycobiology due to the increasing appreciation of its impact on all aspects of life. Likewise, bacteriophage biology is enjoying a new renaissance as the post-antibiotic era fuels the search for novel ways to control harmful bacteria. Phages have spent the last 3 billion years developing ways of recognizing and manipulating bacterial surface glycans. Therefore, phages comprise a massive reservoir of glycan-binding and -hydrolyzing proteins with the potential to be exploited for glycan analysis, bacterial diagnostics and therapeutics. We discuss phage tail proteins that recognize bacterial surface polysaccharides, endolysins that bind and cleave peptidoglycan, Ig-like proteins that attach to mucin glycans, and phage effector proteins that recognize both bacterial and eukaryotic oligosaccharides. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 08/2015; 34:69-77. DOI:10.1016/j.sbi.2015.07.006
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    ABSTRACT: Several studies in recent years have drawn attention to the ability of proteins to adapt to intermolecular interactions by conformational changes along structure-encoded collective modes of motions. These so-called soft modes, primarily driven by entropic effects, facilitate, if not enable, functional interactions. They represent excursions on the conformational space along principal low-ascent directions/paths away from the original free energy minimum, and they are accessible to the protein even before protein-protein/ligand interactions. An emerging concept from these studies is the evolution of structures or modular domains to favor such modes of motion that will be recruited or integrated for enabling functional interactions. Structural dynamics, including the allosteric switches in conformation that are often stabilized upon formation of complexes and multimeric assemblies, emerge as key properties that are evolutionarily maintained to accomplish biological activities, consistent with the paradigm sequence→structure→dynamics→function where 'dynamics' bridges structure and function. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 08/2015; 35:17-23. DOI:10.1016/j.sbi.2015.07.007
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    ABSTRACT: The aromatic amino acid hydroxylases phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase are homotetramers, with each subunit containing a homologous catalytic domain and a divergent regulatory domain. The solution structure of the regulatory domain of tyrosine hydroxylase establishes that it contains a core ACT domain similar to that in phenylalanine hydroxylase. The isolated regulatory domain of tyrosine hydroxylase forms a stable dimer, while that of phenylalanine hydroxylase undergoes a monomer-dimer equilibrium, with phenylalanine stabilizing the dimer. These solution properties are consistent with the regulatory mechanisms of the two enzymes, in that phenylalanine hydroxylase is activated by phenylalanine binding to an allosteric site, while tyrosine hydroxylase is regulated by binding of catecholamines in the active site. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 07/2015; 35:1-6. DOI:10.1016/j.sbi.2015.07.004
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    ABSTRACT: Bilin-dependent GAF domain photoreceptors cover the whole spectrum of light with their absorbance properties. They can be divided into three groups according to the domain architecture of their photosensory module. Group I and Group II harbor phytochromes with PAS-GAF-PHY and GAF-PHY domain architecture, respectively. Group III consists of stand-alone GAF domain photoreceptors, the cyanobacteriochromes. Crystal structures of all three groups are now available to shed light on possible downstream signaling pathways. Structures of Group I and III photoreceptors in both states display changes in the secondary structures during photoconversion. The knowledge about the photoconversion in phytochromes and CBCRs make them promising targets for applications in life science and synthetic biology. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 07/2015; 35:7-16. DOI:10.1016/j.sbi.2015.07.005
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    ABSTRACT: The success of a directed evolution approach to creating custom-made enzymes relies in no small part on screening as many clones as possible. The miniaturisation of assays into pico to femtoliter compartments (emulsion droplets, vesicles or gel-shell beads) makes directed evolution campaigns practically more straightforward than current large scale industrial screening that requires liquid handling equipment and much manpower. Several recent experimental formats have established protocols to screen more than 10 million compartments per day, representing unprecedented throughput at low cost. This review introduces the emerging approaches towards making biomimetic man-made compartments that are poised to be adapted by a wider circle of researchers. In addition to cost and time saving, control of selection pressures and conditions, the quantitative readout that reports on every library members and the ability to develop strategies based on these data will increase the degrees of freedom in designing and testing strategies for directed evolution experiments. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 07/2015; 33. DOI:10.1016/j.sbi.2015.06.001
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    ABSTRACT: The antibody repertoire is the fundamental unit that enables development of antigen specific adaptive immune responses against pathogens. Different species have developed diverse genetic and structural strategies to create their respective antibody repertoires. Here we review the shark, chicken, camel, and cow repertoires as unique examples of structural and genetic diversity. Given the enormous importance of antibodies in medicine and biological research, the novel properties of these antibody repertoires may enable discovery or engineering of antibodies from these non-human species against difficult or important epitopes. Copyright © 2015. Published by Elsevier Ltd.
    Current Opinion in Structural Biology 07/2015; 33:27-41. DOI:10.1016/j.sbi.2015.06.002
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    ABSTRACT: Conformational changes are an essential feature of most molecular processes in biology. Optical tweezers have emerged as a powerful tool for probing conformational dynamics at the single-molecule level because of their high resolution and sensitivity, opening new windows on phenomena ranging from folding and ligand binding to enzyme function, molecular machines, and protein aggregation. By measuring conformational changes induced in a molecule by forces applied by optical tweezers, new insight has been gained into the relationship between dynamics and function. We discuss recent advances from studies of how structure forms in proteins and RNA, including non-native structures, fluctuations in disordered proteins, and interactions with chaperones assisting native folding. We also review the development of assays probing the dynamics of complex protein-nucleic acid and protein-protein assemblies that reveal the dynamic interactions between biomolecular machines and their substrates. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 07/2015; 34:43-51. DOI:10.1016/j.sbi.2015.06.006
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    ABSTRACT: The majority of the C-type lectin-like domains in the human genome likely to bind sugars have been investigated structurally, although novel mechanisms of sugar binding are still being discovered. In the immune system, adhesion and endocytic receptors that bind endogenous mammalian glycans are often conserved, while pathogen-binding C-type lectins on cells of the innate immune system are more divergent. Lack of orthology between some human and mouse receptors, as well as overlapping specificities of many receptors and formation of receptor hetero-oligomers, can make it difficult to define the roles of individual receptors. There is good evidence that C-type lectins initiate signalling pathways in several different ways, but this function remains the least well understood from a mechanistic perspective. Copyright © 2015 The Authors. Published by Elsevier Ltd.. All rights reserved.
    Current Opinion in Structural Biology 07/2015; 34:26-34. DOI:10.1016/j.sbi.2015.06.003
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    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/j.sbi.2015.01.007