NATURE RESEARCH JOURNALS PRESS RELEASE
For papers that will be published online on 22 July 2007
This press release is copyrighted to the Nature journals mentioned below.
This press release contains:
· Summaries of newsworthy papers:
Two anticancer drugs target the spliceosome – Nature Chemical Biology
Probing for prions – Nature Methods
· Mention of papers to be published at the same time with the same embargo
· Geographical listing of authors
PDFs of all the papers mentioned on this release can be found in the relevant journal’s section of http://press.nature.com. Press contacts for the Nature journals are listed at the end of this release.
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PLEASE CITE THE SPECIFIC NATURE JOURNAL AND WEBSITE AS THE SOURCE OF THE FOLLOWING ITEMS. IF PUBLISHING ONLINE, PLEASE CARRY A HYPERLINK TO THE APPROPRIATE JOURNAL’S WEBSITE.
*************************************NATURE CHEMICAL BIOLOGY ***********************************
(http://www.nature.com/nchembio)
[1] & [2] Two anticancer drugs target the spliceosome
DOI: 10.1038/nchembio.2007.18
DOI: 10.1038/nchembio.2007.16
Scientists have identified the cellular target of two important anticancer molecules as a component of the spliceosome, according to two papers to be published in the September issue of Nature Chemical Biology.
The spliceosome is a large biological ‘machine’ that helps turn DNA into proteins. In particular, it binds to pre-mRNA (which is a direct copy of the DNA sequence) and cuts out the unnecessary nucleotides, resulting in mRNA that can then be converted into proteins. Until this point, no small molecules were known that could inhibit this process.
The two separate studies, led by Minoru Yoshida and Yoshiharu Mizui, were focused on finding out how two potent antitumour compounds actually work inside the cell. In both cases, the researchers now identify the cellular target of their compounds as SF3b, which is one portion of the spliceosome. These reports are important because they tell us that the spliceosome can be inhibited by small molecules, which highlights the potential of the splicesome as an anticancer target. By knowing the target of these molecules, scientists will be able to improve the design of anticancer compounds as well as create new potential drugs. In addition, the use of targeted compounds as ‘chemical probes’ will also allow researchers to learn more about the spliceosome, both in normal and cancerous cells.
Author contact:
Minoru Yoshida (RIKEN, Saitama, Japan) Author paper [1]
Tel: +81 48 467 9516, Email: [email protected]
Author contact:
Yoshiharu Mizui, (Eisai Co Ltd, Ibaraki, Japan) Author paper [2]
Tel: +81 29 847 5808, Email: [email protected]
********************************************NATURE METHODS ******************************************
[3] Probing for prions
DOI: 10.1038/nmeth1066
A rapid and very sensitive technique for the detection of infectious prion proteins is reported online this week in Nature Methods.
Prions, the cause of neurodegenerative diseases such as mad cow, scrapie in sheep or Creutzfeldt-Jakob disease in humans (CJD), are infectious proteins in the brain. They are so similar to their healthy cellular counterparts that they cannot be distinguished by antibodies, making their detection difficult.
To develop methods for prion detection scientists have taken advantage of the fact that prions will convert certain normally folded protein into infectious aggregates which can be more easily measured. If a sample contains prions they will trigger protein aggregation in a healthy brain tissue substrate which can then be measured. Downsides of this technique are that it is not very sensitive, takes weeks and the whole brain tissue required is more difficult to obtain.
Byron Caughey and colleagues have improved matters; their adaptation allows the use of recombinant protein rather than brain tissue as a substrate for the aggregation reaction. They can distinguish between prion-infected and healthy hamsters using only minute amounts of body fluids in 2-3 days.
Their method will not only be of considerable interest to the developers of diagnostic assays, it will also allow the study of components affecting prion aggregation and the screening for inhibitors of the process.
Author contact:
Byron Caughey (National Institute of Allergy and Infectious Diseases, Bethesda, MA, USA)
Tel: +1 406 363 9264; E-mail: [email protected]
Other papers from Nature Methods to be published online at the same time and with the same embargo:
[4] High throughput cloning and expression in recalcitrant bacteria
DOI: 10.1038/nmeth1073
***************************************************************************************************************
Items from other Nature journals to be published online at the same time and with the same embargo:
Nature PHYSICS (http://www.nature.com/naturephysics)
[5] Three-body interactions with cold polar molecules
DOI: 10.1038/nphys678
[6] Bridging length scales in colloidal liquids and interfaces from near-critical divergence to single particles
DOI: 10.1038/nphys679
NATURE MATERIALS (http://www.nature.com/naturematerials)
[7] High friction on a bubble mattress
DOI: 10.1038/nmat1962
[8] Electronic control of Ca2+ signalling in neuronal cells using an organic electronic ion pump
DOI: 10.1038/nmat1963
[9] Charging and discharging of single conjugated-polymer nanoparticles
DOI: 10.1038/nmat1959
[10] Elastic membranes of close-packed nanoparticle arrays
DOI: 10.1038/nmat1965
NATURE NANOTECHNOLOGY (http://www.nature.com/nnano)
[11] Alternating current Josephson effect and resonant superconducting transport through vibrating Nb nanowires
DOI: 10.1038/nnano.2007.218
[12] Targeted delivery of magnetic aerosol droplets to the lung (N&V)
DOI: 10.1038/nnano.2007.217
Nature MEDICINE (http://www.nature.com/naturemedicine)
[13] IL-15 constrains mast cell–dependent antibacterial defenses by suppressing chymase activities
DOI: 10.1038/nm1615
NATURE GENETICS (http://www.nature.com/naturegenetics)
[14] Target mimicry provides a new mechanism for regulation of microRNA activity
DOI: 10.1038/ng2079
[15] Axonal loss and neuroinflammation caused by peroxisome-deficient oligodendrocytes
DOI: 10.1038/ng2070
Nature NEUROSCIENCE (http://www.nature.com/natureneuroscience)
[16] Crystal structure of the extracellular domain of nAChRalpha1 bound to alpha-bungarotoxin at 1.94Å resolution
DOI: 10.1038/nn1942
[17] A Drosophila kinesin required for synaptic bouton formation and synaptic vesicle transport
DOI: 10.1038/nn1936
Nature IMMUNOLOGY (http://www.nature.com/natureimmunology)
[18] Crystal structure of the IL-15–IL-15Ralpha complex, a cytokine-receptor unit presented in trans
DOI:10.1038/ni1492
NATURE CELL BIOLOGY (http://www.nature.com/naturecellbiology)
[19] Exocytotic catecholamine release is not associated with cation flux through channels in the vesicle membrane but Na+ influx through the fusion pore
DOI: 10.1038/ncb1617
[20] PIM1-dependent phosphorylation of histoneH3 at serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation
DOI: 10.1038/ncb1618
[21] The Smc5–Smc6 complex and SUMO modification of Rad52 regulates recombinational repair at the ribosomal gene locus
DOI: 10.1038/ncb1619
[22] A reciprocal tensin-3–cten switch mediates EGF-driven mammary cell migration
DOI: 10.1038/ncb1622
[23] Cathepsin l activity controls adipogenesis and glucose tolerance
DOI: 10.1038/ncb1623
[24] Formation of NHEJ-derived reciprocal chromosomal translocations does not require Ku70
DOI: 10.1038/ncb1624
Nature STRUCTURAL & MOLECULAR BIOLOGY (http://www.nature.com/natstructmolbiol)
[25] Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms
DOI: 10.1038/nsmb1274
[26] CCDC98 is a BRCA1-BRCT domain–binding protein involved in DNA damage response
DOI: 10.1038/nsmb1277
[27] CCDC98 targets BRCA1 to DNA damage sites
DOI: 10.1038/nsmb1279
***************************************************************************************************************
GEOGRAPHICAL LISTING OF AUTHORS
The following list of places refers to the whereabouts of authors on the papers numbered in this release. The listing may be for an author's main affiliation, or for a place where they are working temporarily. Please see the PDF of the paper for full details.
AUSTRIA
Innsbruck: 5
Vienna: 25
BELGIUM
Leuven: 15
CANADA:
Hamilton: 3
CHINA
Guangzhou: 23
DENMARK
Copenhagen: 21
FRANCE
Lyon: 7
Paris: 23
Villejuif: 13
Villeurbanne: 7
GERMANY
Berlin: 12, 13
Borstel: 13
Goettingen: 15
Heidelberg: 15
Lubeck: 13
Martinsried: 21
Munich: 12
Tubingen: 14
ISRAEL
Rehovot: 22
Tel Aviv: 22
ITALY
Siena: 20
JAPAN
Hyogo: 2
Ibaraki: 1, 2
Kumamoto: 1, 18
Saitama: 1
Tokushima: 23
Tokyo: 1, 6, 18
Yamagata: 2
Yokohama: 1
NETHERLANDS
Groningen: 4
PORTUGAL
Porto: 22
SPAIN
Lleida: 21
Madrid: 14
Seville: 19
SWEDEN
Norrkoping: 8
Stockholm: 8
UNITED KINGDOM
Bristol: 6
London: 21
Oxford: 6, 18
UNITED STATES OF AMERICA
California
Berkeley: 25
Los Angeles: 16
Sacramento: 22
San Francisco: 17, 23
Stanford: 13
Connecticut
New Haven: 19, 26
Georgia
Atlanta: 11
Illinois
Argonne: 10
Chicago: 10
Westmont: 22
Massachusetts
Boston: 17, 22, 23
Michigan
Ann Arbor: 27
New York
Ithaca: 19
New York: 21, 24
North Carolina
Research Triangle Park: 22
Texas
Austin: 9
PRESS CONTACTS…
For media inquiries relating to embargo policy for all the Nature Research Journals:
Katherine Anderson (Nature London)
Tel: +44 20 7843 4502; E-mail: [email protected]
Ruth Francis (Senior Press Officer, Nature, London)
Tel: +44 20 7843 4562; E-mail: [email protected]
For media inquiries relating to editorial content/policy for the Nature Research Journals, please contact the journals individually:
Nature Cell Biology (London)
Bernd Pulverer
Tel: +44 20 7843 4892; E-mail: [email protected]
Nature Chemical Biology (Boston)
Andrea Garvey
Tel: +1 617 475 9241, E-mail: [email protected]
Nature Genetics (New York)
Orli Bahcall
Tel: +1 212 726 9311; E-mail: [email protected]
Nature Immunology (New York)
Laurie Dempsey
Tel: +1 212 726 9372; E-mail: [email protected]
Nature Materials (London)
Fabio Pulizzi
Tel: +44 20 7014 4024; E-mail: [email protected]
Nature Medicine (New York)
Juan Carlos Lopez
Tel: +1 212 726 9325; E-mail: [email protected]
Nature Methods (New York)
Allison Doerr
Tel: +1 212 726 9393; E-mail: [email protected]
Nature Nanotechnology (London)
Peter Rodgers
Tel: +44 20 7014 4019; Email: [email protected]
Nature Neuroscience (New York)
Sandra Aamodt (based in California)
Tel: +1 530 795 3256; E-mail: [email protected]
Nature Physics (London)
Alison Wright
Tel: +44 20 7843 4555; E-mail: [email protected]
Nature Structural & Molecular Biology (New York)
Michelle Montoya
Tel: +1 212 726 9326; E-mail: [email protected]
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