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World Stem Cell Summit 2010

Wednesday, June 4, 2008

Nature Structural & Molecular Biology Contents: June 2008 Volume #15 pp 537 - 651

NATURE STRUCTURAL & MOLECULAR BIOLOGY

June 2008 Volume 15 Number 6, pp 537 - 651

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The Source Event – London, 26/09/2008

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XXIIIrd International Conference on Magnetic Resonance in Biological Systems
August 24-29, 2008 - San Diego, California

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----------------------
EDITORIAL
----------------------
A teacupful of medicine? p537
Green tea has held a long-standing place in traditional Asian
medicine. Scientific research is now beginning to explain why.
doi:10.1038/nsmb0608-537
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgC0E1

----------------------
NEWS AND VIEWS
----------------------
How is SOS activated? Let us count the ways pp538 - 540
New work shows that activation of the Ras guanine nucleotide
exchange factor SOS is dependent upon the membrane density of
phosphatidylinositol-4,5-bisphosphate (PIP2) and GTP-bound Ras.
These signals synergize to release the autoinhibitory DH-PH
domain, while the histone domain fine-tunes SOS activation in
response to PIP2.
Greg M Findlay and Tony Pawson
doi:10.1038/nsmb0608-538
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgD0E2

Evil versus 'eph-ective' use of ephrin-B2 pp540 - 542
Crystal structures of the Nipah and Hendra virus attachment protein
complexed with ephrin-B2 shed light on the apparent paradox of
ephrin-B2's flexibility for binding multiple receptors.
Surprisingly, the switch from the use of glycan-based to
protein-based receptors seems to have evolved independently
from other protein-receptor-using paramyxoviruses such as the
measles virus.
Benhur Lee, Zeynep Akyol Ataman and Lei Jin
doi:10.1038/nsmb0608-540
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgE0E3

Simplifying a complex code pp542 - 544
Methylated lysines are essential components of the network of
histone modifications, or 'histone code', that regulates gene
expression. Work on the methyltransferase Dot1 shows how
modifications on different histones interact to modulate
activity and how its catalytic mechanism is matched to its
role in genome regulation.
Bryan M Turner
doi:10.1038/nsmb0608-542
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgF0E4

Escaping amyloid fate pp544 - 546
Small molecules that safely antagonize amyloidogenesis are
desperately needed for many devastating disorders that plague
humankind, including Alzheimer's and Parkinson's diseases.
New work brings important mechanistic insights into how one
promising candidate, (-)-epigallocatechin-3-gallate (EGCG),
diverts amyloid-beta and alpha-synuclein down innocuous
folding trajectories at the expense of the deleterious states
populated during amyloidogenesis.
Blake E Roberts and James Shorter
doi:10.1038/nsmb0608-544
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgG0E5

Endo-siRNAs: yet another layer of complexity in RNA silencing
pp546 - 548
Organisms possessing RNA-dependent RNA polymerase activity are
known to produce endogenous small interfering RNAs (esiRNAs).
It had been thought that organisms such as flies and mammals
lacking this activity would not produce esiRNAs. However, it
has now been shown that a functional esiRNA pathway is present
in such animals; the esiRNAs are derived from a variety of
endogenous double-stranded RNA substrates.
Timothy W Nilsen
doi:10.1038/nsmb0608-546
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgH0E6

Damage control p548
Ines Chen
doi:10.1038/nsmb0608-548
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgI0E7

----------------------
RESEARCH HIGHLIGHTS
----------------------
Research highlights p549
doi:10.1038/nsmb0608-549
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgJ0E8

----------------------
ARTICLES
----------------------
Nonprocessive methylation by Dot1 leads to functional redundancy of
histone H3K79 methylation states pp550 - 557
Floor Frederiks et al.
doi:10.1038/nsmb.1432
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgK0EA
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgL0EB

EGCG redirects amyloidogenic polypeptides into unstructured,
off-pathway oligomers pp558 - 566
Dagmar E Ehrnhoefer et al.
doi:10.1038/nsmb.1437
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgM0EC
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgN0ED

Structural basis of Nipah and Hendra virus attachment to their
cell-surface receptor ephrin-B2 pp567 - 572
Thomas A Bowden et al.
doi:10.1038/nsmb.1435
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgO0EE
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgP0EF

The central unit within the 19S regulatory particle of the
proteasome pp573 - 580
Rina Rosenzweig, Pawel A Osmulski, Maria Gaczynska and
Michael H Glickman
doi:10.1038/nsmb.1427
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgQ0EG
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgR0EH

Two distinct mechanisms generate endogenous siRNAs from bidirectional
transcription in Drosophila melanogaster pp581 - 590
Katsutomo Okamura et al.
doi:10.1038/nsmb.1438
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgS0EI
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgT0EJ

Long single alpha-helical tail domains bridge the gap between
structure and function of myosin VI pp591 - 597
Benjamin J Spink et al.
doi:10.1038/nsmb.1429
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgU0EK
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgV0EL

Telomerase recruitment by the telomere end binding protein-beta
facilitates G-quadruplex DNA unfolding in ciliates pp598 - 604
Katrin Paeschke et al.
doi:10.1038/nsmb.1422
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgW0EM
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgX0EN

A structural link between inactivation and block of a K+ channel
pp605 - 612
Christian Ader et al.
doi:10.1038/nsmb.1430
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgY0EO
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0BwgZ0EP

Internal dynamics control activation and activity of the autoinhibited
Vav DH domain pp613 - 618
Pilong Li, Ilidio R S Martins, Gaya K Amarasinghe and Michael K Rosen
doi:10.1038/nsmb.1428
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwga0EW
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgb0EX

Crystal structure of the aquaglyceroporin PfAQP from the malarial
parasite Plasmodium falciparum pp619 - 625
Zachary E R Newby et al.
doi:10.1038/nsmb.1431
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgc0EY
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgd0EZ

Structural insights into human KAP1 PHD finger-bromodomain and its
role in gene silencing pp626 - 633
Lei Zeng et al.
doi:10.1038/nsmb.1416
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwge0Ea
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgf0Eb

Triple-helix structure in telomerase RNA contributes to catalysis
pp634 - 640
Feng Qiao and Thomas R Cech
doi:10.1038/nsmb.1420
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgg0Ec
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgh0Ed

Protein disaggregation by the AAA+ chaperone ClpB involves partial
threading of looped polypeptide segments pp641 - 650
Tobias Haslberger et al.
doi:10.1038/nsmb.1425
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgi0Ee
Article: http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgj0Ef

----------------------
ERRATUM
----------------------
Erratum: Membrane-dependent signal integration by the Ras activator
Son of sevenless p651
Jodi Gureasko et al.
doi:10.1038/nsmb0608-651a
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgk0Eg

----------------------
CORRIGENDUM
----------------------
Corrigendum: The refined structure of nascent HDL reveals a key
functional domain for particle maturation and dysfunction p651
Zhiping Wu et al.
doi:10.1038/nsmb0608-651b
http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0Bwgl0Eh

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Nature Methods focus on Single Molecule Analysis -- June 2008

Biologists are becoming increasingly interested in methodologies that
can examine the mechanism of action of fundamental biological processes
at the molecular level. This focus will consist of four review-type
articles that provide practical guidance for some of the techniques
that are most integral to in vitro single-molecule experiments. These
will cover single-molecule fluorescence methods, microfluidic flow cells
to manipulate experimental conditions during experiments, and force
spectroscopy techniques such as atomic force microscopy (AFM) and
optical traps to manipulate individual molecules themselves.

http://ealerts.nature.com/cgi-bin24/DM/y/elLf0Xztnp0Hjh0K7N0EZ

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