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| July 2012 Volume 13 Number 7 | ||||||||||||||||||||||||||||||||||||||||||||||
In this issue
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| REVIEWS | Top | |||||||||||||||||||||||||||||||||||||||||||||
New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs Bryan A. Gibson & W. Lee Kraus p411 | doi:10.1038/nrm3376 Poly(ADP-ribosyl)ation (PARylation) is a dynamic protein modification, the control of which is important for diverse cell biological processes and normal physiology. Common mechanistic themes are being characterized by which PARylation alters the functions of target proteins, and the PAR-binding modules that mediate this. Abstract | Full Text | PDF | ||||||||||||||||||||||||||||||||||||||||||||||
| Towards a molecular architecture of centriole assembly Pierre Gönczy p425 | doi:10.1038/nrm3373 The centriole is crucial for the formation of flagella, cilia and centrosomes. The ultrastructure of the centriole reveals a striking ninefold radial arrangement of microtubules. Emerging insights into the molecular mechanisms of centriole assembly include the function of spindle assembly abnormal 6 (SAS-6) proteins in imparting the ninefold symmetry. Abstract | Full Text | PDF | ||||||||||||||||||||||||||||||||||||||||||||||
| New insights into nucleosome and chromatin structure: an ordered state or a disordered affair? Karolin Luger, Mekonnen L. Dechassa & David J. Tremethick p436 | doi:10.1038/nrm3382 Chromatin compaction has profound implications for the regulation of transcription, replication and DNA repair. Changes in nucleosome structure and stability — due to the incorporation of variant histones and post-translational modifications of histones — affect chromatin compaction. Chromatin structures are not nearly as uniform as previously assumed, which should be taken into account in the context of specific biological functions. Abstract | Full Text | PDF | ||||||||||||||||||||||||||||||||||||||||||||||
Vertebrate protein glycosylation: diversity, synthesis and function Kelley W. Moremen, Michael Tiemeyer & Alison V. Nairn p448 | doi:10.1038/nrm3383 Approximately half of human proteins are glycosylated, and the resulting diverse glycan patterns encode an additional level of information. The process of protein glycosylation is mediated by numerous enzymes with dynamic localization, regulation and specificity. High-throughput techniques facilitate the study of complex protein glycans and may give further insights into their roles in protein homeostasis, cell signalling and cell adhesion. Abstract | Full Text | PDF | ||||||||||||||||||||||||||||||||||||||||||||||
| PERSPECTIVES | Top | |||||||||||||||||||||||||||||||||||||||||||||
| OPINION Coordination between RAB GTPase and phosphoinositide regulation and functions Steve Jean & Amy A. Kiger p463 | doi:10.1038/nrm3379 Membrane trafficking relies on changes in membrane identity, which are determined by RAB GTPases and phosphoinositides. Coordinated regulation of RABs and phosphoinositides, which is achieved by direct physical and functional interactions between their regulatory enzymes, is emerging as a central mechanism to ensure membrane trafficking fidelity. Abstract | Full Text | PDF | ||||||||||||||||||||||||||||||||||||||||||||||
| VIEWPOINT Stem cells assessed Cédric Blanpain, George Q. Daley, Konrad Hochedlinger, Emmanuelle Passegué, Janet Rossant & Shinya Yamanaka p471 | doi:10.1038/nrm3371 Six scientists in the field of stem cell research comment on our basic understanding of stem cells and other pluripotent cells, on their potential therapeutic use and on key challenges that remain. Abstract | Full Text | PDF | ||||||||||||||||||||||||||||||||||||||||||||||
| ADDENDUM | Top | |||||||||||||||||||||||||||||||||||||||||||||
| Illuminating the functional and structural repertoire of human TBC/RABGAPs Marieke A. M. Frasa, Katja T. Koessmeier, M. Reza Ahmadian & Vania M. M. Braga p476 | doi:10.1038/nrm3364 Full Text | PDF | Supplementary information | ||||||||||||||||||||||||||||||||||||||||||||||
| Erratum: TFIIH: when transcription met DNA repair Emmanuel Compe & Jean-Marc Egly p476 | doi:10.1038/nrm3377 Full Text | PDF | ||||||||||||||||||||||||||||||||||||||||||||||
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| *Journal Citation Reports, Thomson, 2011 |
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