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FEBS Journal

Cover image for Vol. 278 Issue 20

Special Issue: Protein Structure and Proteomics

October 2011

Volume 278, Issue 20

Pages 3795–3952

  1. Special Issue

    1. Top of page
    2. Special Issue
    3. Author Index
    1. You have free access to this content
      Special Issue: Protein Structure and Proteomics : Introduction (page 3795)

      Ettore Appella and Jan Johansson

      Article first published online: 15 SEP 2011 | DOI: 10.1111/j.1742-4658.2011.08313.x

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      The 18th International Methods in Protein Structure Analysis (MPSA) conference was held in Uppsala, Sweden in August 2010. These meetings bring together scientists in various fields to discuss new methods for protein analysis. The reviews in this Special Issue highlight some of the exciting research presented at the meeting, including a focus on protein misfolding in disease

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      Proteomic reactors and their applications in biology (pages 3796–3806)

      Hu Zhou, Zhibin Ning, Fangjun Wang, Deeptee Seebun and Daniel Figeys

      Article first published online: 6 SEP 2011 | DOI: 10.1111/j.1742-4658.2011.08292.x

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      The proteomic reactor is a microfluidic device that integrates the pre-MS analysis procedures, such as protein concentration/separation, reduction, alkylation, digestion and peptide fractionation, resulting in a reduction in sample loss and an improved limit of detection. This review summarizes the developments and biological applications of the proteomic reactor

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      Mass spectrometric characterization of proteins transferred from polyacrylamide gels to membrane filters (pages 3807–3814)

      Yoko Ino and Hisashi Hirano

      Article first published online: 15 SEP 2011 | DOI: 10.1111/j.1742-4658.2011.08303.x

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      A technique, by which proteins are transferred from electrophoresis gels onto PVDF membranes, digested on membranes with a protease, and analyzed directly by MALDI-MS has been developed to identify the gel-resolved proteins. This technique also has the potential to identify protein isoforms and post-translationally modified proteins. We describe some devices which enabled efficient MALDI-MS analysis of proteins on membranes

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      New developments in protein structure–function analysis by MS and use of hydrogen–deuterium exchange microfluidics (pages 3815–3821)

      Michael Landreh, Juan Astorga-Wells, Jan Johansson, Tomas Bergman and Hans Jörnvall

      Article first published online: 5 JUL 2011 | DOI: 10.1111/j.1742-4658.2011.08215.x

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      Mass spectrometry (MS) is a powerful tool in protein structure analysis. In this review, we summarize some of the recent developments and applications in gas phase fragmentation, ion mobility technology, chemical crosslinking and hydrogen/deuterium exchange (HDX) mass spectrometry. We also demonstrate the use of a microfluidic cell for on-line HDX-MS to monitor aggregation of the amyloid-β peptide 1-40

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      Protein alpha-N-acetylation studied by N-terminomics (pages 3822–3834)

      Petra Van Damme, Thomas Arnesen and Kris Gevaert

      Article first published online: 2 AUG 2011 | DOI: 10.1111/j.1742-4658.2011.08230.x

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      N-terminomics is a powerful tool for studying protein N-terminal modifications including protein N-terminal acetylation, an ubiquitous modification catalyzed by multi-subunit N-terminal acetyltransferase complexes. In this review, we highlight the recent advances made in this expanding field and provide an overview of the observed functional implications of alpha-N-acetylation and present state-of-the-art technologies, all permitting for a better understanding of N-terminal biology

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      Characterizing the complexity of enzymes on the basis of their mechanisms and structures with a bio-computational analysis (pages 3835–3845)

      Gemma L. Holliday, Julia D. Fischer, John B. O. Mitchell and Janet M. Thornton

      Article first published online: 13 JUN 2011 | DOI: 10.1111/j.1742-4658.2011.08190.x

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      In this review we examine the chemical versatility of enzymes, the complex mapping of reactions to proteins (rarely one-to-one) and the structural complexity of enzymes and their active sites. This work highlights how the enzymes we see today reflect millions of years of evolution, involving de novo design followed by exquisite regulation and modulation to create optimal fitness for life

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      Membrane protein integration into the endoplasmic reticulum (pages 3846–3858)

      Luis Martínez-Gil, Ana Saurí, Marc A. Marti-Renom and Ismael Mingarro

      Article first published online: 13 JUN 2011 | DOI: 10.1111/j.1742-4658.2011.08185.x

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      Most integral membrane proteins are targeted, inserted and assembled in the endoplasmic reticulum (ER) membrane. The sequential and potentially overlapping events for membrane protein integration take place at sites termed translocons, which comprise a specific set of membrane proteins acting in concert with ribosomes and molecular chaperones to ensure the success of the whole process

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      Unravelling the twists and turns of the serpinopathies (pages 3859–3867)

      Benoit D. Roussel, James A. Irving, Ugo I. Ekeowa, Didier Belorgey, Imran Haq, Adriana Ordóñez, Antonina J. Kruppa, Annelyse Duvoix, Sheikh Tamir Rashid, Damian C. Crowther, Stefan J. Marciniak and David A. Lomas

      Article first published online: 20 JUN 2011 | DOI: 10.1111/j.1742-4658.2011.08201.x

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      Mutants of the serpins form ordered polymers that result in a group of diseases termed the serpinopathies. These are typified by mutations in α1-antitrypsin to cause cirrhosis and in neuroserpin to cause the dementia FENIB. We review the pathobiology of the serpinopathies and the development of novel therapeutic strategies to treat the inclusions that cause disease

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      Understanding the complex mechanisms of β2-microglobulin amyloid assembly (pages 3868–3883)

      Timo Eichner and Sheena E. Radford

      Article first published online: 13 JUN 2011 | DOI: 10.1111/j.1742-4658.2011.08186.x

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      This review focuses on recent advances in developing a molecular description of the folding and aggregation mechanisms of the human amyloidogenic protein β2-microglobulin (β2m) under physiologically-relevant conditions. In particular, the structural and dynamic properties of the non-native folding intermediate IT and its role in the initiation of fibrillation and the development of dialysis-related amyloidosis are discussed

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      Protein engineering to stabilize soluble amyloid β-protein aggregates for structural and functional studies (pages 3884–3892)

      Torleif Härd

      Article first published online: 6 SEP 2011 | DOI: 10.1111/j.1742-4658.2011.08295.x

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      Oligomeric aggregates of the amyloid β-protein (Aβ) have been shown to play a fundamental neurotoxic role in Alzheimer’s disease. However, research is complicated by the multitude of different interconverting aggregates that Aβ can form in vitro and in vivo, and by the inhomogeneity and instability of in vitro preparations. Here we review recent studies in which protein engineering, and in particular disulfide engineering, has been applied to stabilize different Aβ aggregates

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      BRICHOS domain associated with lung fibrosis, dementia and cancer – a chaperone that prevents amyloid fibril formation? (pages 3893–3904)

      Hanna Willander, Erik Hermansson, Jan Johansson and Jenny Presto

      Article first published online: 5 JUL 2011 | DOI: 10.1111/j.1742-4658.2011.08209.x

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      The BRICHOS domain is found in several protein families associated with dementia, amyloid, interstitial lung disease and cancer. BRICHOS domains from Bri2 and proSP-C efficiently prevent the amyloid β-peptide, associated with Alzheimer′s disease, from forming amyloid fibrils.We speculate that the BRICHOS domain can chaperone β-prone regions in precursor proteins and thereby prevent aggregation and amyloid formation

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      Membrane and surface interactions of Alzheimer’s Aβ peptide – insights into the mechanism of cytotoxicity (pages 3905–3917)

      Thomas L. Williams and Louise C. Serpell

      Article first published online: 26 JUL 2011 | DOI: 10.1111/j.1742-4658.2011.08228.x

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      Alzheimer’s disease is associated with abnormal assembly of the amyloid-β (Aβ) peptide. Oligomeric forms of Aβ have been shown to be toxic in cellular assays and bind to and damage phospholipid membranes. Here we review the current understanding of the mechanism of membrane association of the Aβ peptide and discuss the role played in cytotoxicity

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      Localized amyloids important in diseases outside the brain – lessons from the islets of Langerhans and the thoracic aorta (pages 3918–3929)

      Gunilla T. Westermark and Per Westermark

      Article first published online: 8 SEP 2011 | DOI: 10.1111/j.1742-4658.2011.08298.x

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      Generation of small amyloid deposits in specific organs is often associated with increased cell death. We discuss two common localized amyloid fibril-forming proteins. IAPP aggregates and induces depletion of islet β-cells in type 2 diabetes and in islets transplanted into type 1 diabetic subjects while medin might be a player in the generation of thoracic aortic aneurysm and dissection

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      The carbohydrate recognition domain of collectins (pages 3930–3941)

      Edwin J. A. Veldhuizen, Martin van Eijk and Henk P. Haagsman

      Article first published online: 1 JUL 2011 | DOI: 10.1111/j.1742-4658.2011.08206.x

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      This review gives a comprehensive overview of the interaction between the carbohydrate recognition domain of collectins and saccharide ligands. Despite the overall similar structure of this domain among collectins, there is a striking diversity in ligand specificity. The available structural and functional data on collectin-ligand complexes is discussed and provides detailed clues on the basis of this diversity

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      Antimicrobial peptides important in innate immunity (pages 3942–3951)

      Andreas Cederlund, Gudmundur H. Gudmundsson and Birgitta Agerberth

      Article first published online: 19 SEP 2011 | DOI: 10.1111/j.1742-4658.2011.08302.x

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      Antimicrobial peptides (AMPs) can be considered as our own antibiotics. Through disruption of microbial cell membranes AMPs eliminate microorganisms and hence inhibit or prevent infections. They are also involved in regulating the composition of the microbiota. In this review the two major classes of mammalian AMPs, defensins and cathelicidins, are discussed with emphasis on their structures, functions and regulation

  2. Author Index

    1. Top of page
    2. Special Issue
    3. Author Index
    1. You have free access to this content
      Author index (page 3952)

      Article first published online: 28 SEP 2011 | DOI: 10.1111/j.1742-4658.2011.07856.x

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