X-ray image captured in record time

Summaries of newsworthy papers include Molecule required for bone repair identified – Nature Genetics, Problems with a potential Alzheimer disease treatment – Nature Neuroscience


For papers that will be published online on 12 November 2006

This press release is copyrighted to the Nature journals mentioned below.

This press release contains:

· Summaries of newsworthy papers:

X-ray image captured in record time – Nature Physics

Molecule required for bone repair identified – Nature Genetics

Problems with a potential Alzheimer disease treatment – Nature Neuroscience

· 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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***********************NATURE PHYSICS*******************************

[1] X-ray image captured in record time
DOI: 10.1038/nphys461

An X-ray image of micrometre-sized stick figures taken in a record time of just 25 femtoseconds is described by Henry Chapman and colleagues in the December issue of Nature Physics. The image, patterned into a metal film, was taken at around a trillion times faster than a conventional flash photograph — just moments before the film evaporated at a temperature of 60,000 degrees Celsius.

The image was collected using radiation produced by the FLASH 'free-electron laser' that began operation at the DESY facility in Germany earlier this year. This feat demonstrates an important proof-of-principle for a technique that should enable atomic-scale imaging of the structure of a much wider range of molecules than is possible using conventional synchrotron sources.

Free-electron lasers represent an exciting development in fields ranging from structural biology to nanotechnology. These lasers produce an intense and extremely short burst of X-rays enabling the structure of individual organic molecules to be collected, without the need to first form them into a crystal as is needed in conventional X-ray analysis. Although atomic-scale resolution is not demonstrated in the present work, this could soon be possible when the first of a new generation of more powerful free-electron sources, such as the Linac Coherent Light Source (LCLS) at the Stanford Linear Accelerator Center in the US, are complete.

Author contact:

Henry Chapman (University of California, Livermore, CA, USA)

Tel: +1 925 423 1580; Email: [email protected]

Other papers from Nature Physics to be published online at the same time and with the same embargo:

[2] Imaging and controlling electron transport inside a quantum ring
DOI: 10.1038/nphys459

[3] Initialization and read-out of spins in coupled core–shell quantum dots
DOI: 10.1038/nphys458

**********************************NATURE GENETICS *********************

[4] Molecule required for bone repair identified
DOI: 10.1038/ng1916

A molecule that regulates the first steps of bone repair in mice is reported in a study in the December issue of Nature Genetics. The molecule, bone morphogenetic protein 2 (BMP2), was long known to be part of a family of proteins that can promote bone growth, but this is the first study to establish one of the BMP proteins as absolutely required for the natural regenerative response.

Vicki Rosen and colleagues deleted the gene encoding BMP2 specifically in developing limbs in mice. While there were no abnormalities observed at birth, by 13 weeks of age all of the mice examined had reduced bone mineral density and spontaneous forearm fractures. Moreover, none of the fractures showed any sign of the normal healing response, despite the presence of progenitor cells at the site of fracture that are the precursors to the bone-generating process. These progenitor cells, which express the receptor for BMP2, failed to differentiate in the BMP2-deficient limbs.

Author contact:

Vicki Rosen (Harvard University, Boston, MA, USA)

Tel: +1 617 432 5910; E-mail: [email protected]

Other papers from Nature Genetics to be published online at the same time and with the same embargo:

[5] A chromatin-mediated mechanism for specification of conditional transcription factor targets
DOI: 10.1038/ng1917

[6] Genomic and functional evolution of the Drosophila melanogaster sperm proteome
DOI: 10.1038/ng1915

[7] Regional copy number–independent deregulation of transcription in cancer
DOI: 10.1038/ng1923

**************************NATURE NEUROSCIENCE *************************

[8] Problems with a potential Alzheimer disease treatment
DOI: 10.1038/nn1797

An enzyme that produces a toxic protein involved in Alzheimer disease is also important for myelination or insulation of nerve cell axons, according to a study in the December issue of Nature Neuroscience. These results suggest that targeting this enzyme (BACE1) as a treatment for Alzheimer disease may produce significant adverse side effects.

Most nerve cell axons are wrapped with a layer of myelin, which acts like an insulator of electrical wires to allow nerve impulses to travel more quickly to their destination. Riqiang Yan and colleagues studied mice with a deletion of the BACE1 gene to determine the effects of eliminating this enzyme. The thickness of the myelin sheath in these mice was reduced along axons throughout the brain and spinal cord. These effects were visible as early as 15 days following birth and lasted into adulthood. The authors show that under normal conditions BACE1 exerts its effect by activating neuregulin, a known participant in the initiation of myelination.

Behavioral testing also revealed that these mice exhibited lower pain thresholds and decreased grip strength — typical signs of demyelination. Although inhibition of BACE1 may be a viable candidate for reducing the conversion of amyloid precursor protein into the plaques deposits seen in Alzheimer disease, these results suggest that as a therapeutic technique, it should be approached with caution.

Author contact:

Riqiang Yan (Cleveland Clinic, Cleveland, Ohio, USA)
Tel: +1 216 445 2690; E-mail: [email protected]

Other papers from Nature Neuroscience to be published online at the same time and with the same embargo:

[9] Cortical feed-forward networks for binding different streams of sensory information
DOI: 10.1038/nn1798

[10] In vivo time-lapse imaging shows dynamic oligodendrocyte progenitor behavior during zebrafish development
DOI: 10.1038/nn1803


Items from other Nature journals to be published online at the same time and with the same embargo:

Nature (http://www.nature.com/nature)

[11] Early events in the thymus affect the balance of effector and regulatory T cells
DOI: 10.1038/nature05368

NATURE MATERIALS (http://www.nature.com/naturematerials)

[12] Length scales in alloy dissolution and measurement of absolute interfacial free energy
DOI: 10.1038/nmat1780

Nature MEDICINE (http://www.nature.com/naturemedicine)

[13] Low nitric oxide bioavailability contributes to the genesis of experimental cerebral malaria
DOI: 10.1038/nm1499

[14] A selective Sema3A inhibitor enhances regenerative responses and functional recovery of the injured spinal cord
DOI: 10.1038/nm1505

Nature STRUCTURAL & MOLECULAR BIOLOGY (http://www.nature.com/natstructmolbiol)

[15] Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
DOI: 10.1038/nsmb1168

[16] SUMO protease SENP1 induces isomerization of the scissile peptide bond
DOI: 10.1038/nsmb1172

[17] RNA polymerase III transcribes human microRNAs
DOI: 10.1038/nsmb1167

[18] The chromatin-remodeling enzyme ACF is an ATP-dependent DNA length sensor that regulates nucleosome spacing
DOI: 10.1038/nsmb1170

NATURE METHODS (http://www.nature.com/nmeth)

[19] A highly sensitive protein-protein interaction assay based on Gaussia luciferase
DOI: 10.1038/nmeth979

[20] SCALEs: multiscale analysis of library enrichment
DOI: 10.1038/nmeth946



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.

Canberra: 9

Louvain-la-Neuve: 2


Montreal: 19


Creteil: 7

Grenoble: 2

Paris: 7

Saint Martin d’Heres: 2

Villeneuve d’Ascq: 2


Berlin: 1

Freiburg: 10

Hamburg: 1


Kanagawa: 14

Osaka: 14

Tokyo: 14


Lisbon: 11


Singapore: 7


Uppsala: 1


Zurich: 9


Bath: 6, 10

Cheshire: 7

Dundee: 16

London: 11

Newbury: 11

York: 7



Tempe: 12


Fayetteville: 3


La Jolla: 13

Livermore: 1

Menlo Park: 1

Sacramento: 1

San Francisco: 7, 18

Santa Barbara: 3


Boulder: 20


New Haven: 11


Gainesville: 4


Iowa City: 17


Baltimore: 8, 12


Boston: 4, 14

New York

New York: 15

North Carolina

Chapel Hill: 5


Cleveland: 8


Nashville: 10


Charlottesville: 6


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 Genetics (New York)
Orli Bahcall
Tel: +1 212 726 9311; E-mail: [email protected]

Nature Materials (London)
Maria Bellantone
Tel: +44 20 7843 4556; 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 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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Published: 12 Nov 2006

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