IUBMB Life

Cover image for Vol. 66 Issue 3

Edited By: Angelo Azzi and William J. Whelan

Impact Factor: 2.789

ISI Journal Citation Reports © Ranking: 2012: 108/185 (Cell Biology); 148/290 (Biochemistry & Molecular Biology)

Online ISSN: 1521-6551

Associated Title(s): Biochemistry and Molecular Biology Education, Biotechnology and Applied Biochemistry, BioFactors

Featured

  • The function of spermine

    The function of spermine

    Structure of SpmSyn. Panel (A) shows the enzymatically active dimer of human SpmSyn. The two chains are in yellow and magenta with bound molecules of substrates shown in sphere representation with carbon atoms in gray. Panel (B) shows a monomer of SpmSyn with the dimerization interface in magenta. Panel (C) compares the structures of the monomers of SpmSyn, spermidine synthase (labelled SpdSyn) and AdoMetDC. Panel (D) shows the topology diagrams for these proteins. In these panels, the N-terminal domain, connecting loop, central domain and C-terminal domain in SpmSyn are in blue, yellow, orange, and greencyan, respectively. Spermidine synthase domains are color-coded similarly except for the first two b strands that structurally align with long inter-domain loop of SpmSyn, which are shown are in yellow, and the three C-terminal helices that are not present in SpmSyn, which are shown in red. The bound substrates are shown in sphere representation, with carbon atoms in gray. The AdoMetDC is in purple. This figure was originally published in the Journal of Biological Chemistry. Wu, H., Min, J., Zeng, H., McCloskey, D. E., Ikeguchi, Y., Loppnau, P., Michael, A. J., Pegg, A. E., and Plotnikov, A. N. Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J. Biol. Chem. 2008, 283, 16135–16146 © The American Society for Biochemistry and Molecular Biology.

  • Processing, signaling, and physiological function of chemerin

    Processing, signaling, and physiological function of chemerin

    Chemerin is involved in a variety of functions in inflammation, skin, obesity, and cell differentiation. [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]

  • SUMO Ubc9 enzyme as a viral target

    SUMO Ubc9 enzyme as a viral target

    Ubc9 binds SUMO both covalently (solid line) and noncovalently (dotted line) mediating protein interactions between sumoylated proteins (for example SIM). Ubc9 bound noncovalently to SUMO also interacts with sumoylated Ubc9, affecting S. cerevisiae meiosis. Several factors can potentially impact Ubc9 that may or may not be covalently sumoylated; they include microRNA, sumoylation, phosphorylation, hypoxia, and acetylation. The cellular outcome may be altered protein localization, stability, transformation, and changes in the Ubc9 interactome. Similarly, viral proteins that interact with Ubc9, as shown in the figure, also alter cellular functions to sustain viral replication as in the case of gp120 and MMLV. Alternatively, viral proteins can also target protein complexes and pathways (for example B5, Gam1, and E1A) that perhaps are important for viral maintenance. [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]

  • Understanding circadian gene function: Animal models of tissue-specific circadian disruption

    Understanding circadian gene function: Animal models of tissue‐specific circadian disruption

    BMAL1 and CLOCK form a heterodimer that acts on E-box elements to drive the transcription of their own genes, as well as the transcription of Period and Cryptochrome family genes, Rora, and Rev-erbα. PER and CRY proteins form a heterodimer that inhibits the pro-transcription activity of BMAL1/CLOCK, thus inhibiting their own expression. REV-ERBα acts on ROR elements to inhibit the transcription of Bmal1, also acting to inhibit its own expression, while RORA activates Bmal1's transcription by acting on ROR elements. [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]

  • Guardian of the Furnace: Mitochondria, TRAP1, ROS and stem cell maintenance

    Guardian of the Furnace: Mitochondria, TRAP1, ROS and stem cell maintenance

    Potential experimental approaches in investigating the role of TRAP1 in HSC self-renewal and differentiation. (A) In vitro differentiation following TRAP1 RNAi, and (B) In vivo homing, repopulation and mobilization of TRAP1−/− genome edited HSCs in a mouse model. See text for further details.

  • Genomic lens on neuroglobin transcription

    Genomic lens on neuroglobin transcription

    (A): NGB expression in human brain by AHBA. From left to right, magnetic resonance (MR) images in axial section, coronal section and 3D reconstruction are reported. The NGB expression data are shown by red and green dots indicating upregulation and downregulation, respectively. MNI coordinates at cross-hairs are indicated. The heat map reported in the bottom part of (A) shows NGB expression in dissected substructures. (B): Heat map showing coexpression of TFs and NGB in specific neuroanatomic regions. The rows legend is indicated on the left part of the panel. The TFs are selected on the basis of NGB expression (Z-Score > 1). Columns represent TFs ordered left to right by decreasing Pearson coefficient computed respect NGB expression. (C): Heat map representing Pearson coefficient of the most correlated/anti-correlated TFs (absolute coefficient > 0.4) with NGB expression considering the data provided by both NGB probes. Expression levels are reported as Z-scores.

  • The phytotoxin fusicoccin differently regulates 14-3-3 proteins association to mode III targets

    The phytotoxin fusicoccin differently regulates 14‐3‐3 proteins association to mode III targets

    Modeling of mode III peptides bound to 14-3-3ζ. (A) Close-up view of p27Kip1 (purple) modeled with FC (cyan) in the binding groove of 14-3-3ζ (gray α-helices). (B) IL-9Rα/14-3-3ζ complex. FC was also modeled to show the predicted steric clash between Phe in position +1 and the toxin. (C–F) Predicted ternary complexes with KCNK3 (C), GPR15 (D), HAP1 (E), and PLDδ (F). [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]

  • The function of spermine
  • Processing, signaling, and physiological function of chemerin
  • SUMO Ubc9 enzyme as a viral target
  • Understanding circadian gene function: Animal models of tissue‐specific circadian disruption
  • Guardian of the Furnace: Mitochondria, TRAP1, ROS and stem cell maintenance
  • Genomic lens on neuroglobin transcription
  • The phytotoxin fusicoccin differently regulates 14‐3‐3 proteins association to mode III targets

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Editor's Choice

The Wonders of 2-Deoxy-D-Glucose
Haibin Xi, Metin Kurtoglu, Theodore J. Lampidis
Volume 66, Issue 2

Through the eons of time, out of all possible configurations, nature has selected glucose not only as a vital source of energy to sustain life but also as the molecule who's structure supplies the appropriate elements required for a cell to grow and multiply. This understanding, at least in part, explains the profound effects that the analog of glucose, 2-deoxy-d-glucose, has been shown to have on as common and widespread diseases as cancer, viral infection, aging-related morbidity, epilepsy, and others. This review is confined to summarizing some of the salient findings of this remarkable compound as they relate mainly to cancer.

To read this article FREE for a limited time, click HERE.

IUBMB Life Video Highlights

Video Highlight from Theodore J. Lampidis on his recently published Critical Review in IUBMB Life titled, The Wonders of 2-Deoxy-D-Glucose.

Virtual Issue: Molecular basis of disease

Understanding causes and targeting therapies

Molecular basis of disease: understanding causes and targeting therapies
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 Molecular basis of disease
 5-year Impact Factor IUB Life


2013 IUBMB Life Young Investigator Award

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On behalf of the IUBMB, IUBMB Life, and Wiley, it is with great pleasure and honor that we announce Dr. Catia Azzolini as the recipient of the IUBMB Life’s 2013 Wiley Young Investigator Award for her article, Sodium-dependent transport of ascorbic acid in U937 cell mitochondria, now available online.

Dr. Azzolini is affiliated with the Department of Biomolecular Science at University of Urbino.  She will be honored with IUBMB Life’s 2013 Wiley Young Investigator Award at the 14th IUBMB Conference this November 16 - 20, in Marrakech, Morocco, and her award-winning article will be FREELY available online through the conference.

Please join us in congratulating Dr. Azzolini as the recipient of the annual IUBMB Life – Wiley Young Investigator Award.

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