Table of contents
June 2008, Volume 15 No 6 pp537-651
About the coverEditorial
A teacupful of medicine? - p537
doi:10.1038/nsmb0608-537
Green tea has held a long-standing place in traditional Asian medicine. Scientific research is now beginning to explain why.
Full Text - A teacupful of medicine? | PDF (276 KB) - A teacupful of medicine?
News and Views
How is SOS activated? Let us count the ways - pp538 - 540
Greg M Findlay & Tony Pawson
doi:10.1038/nsmb0608-538
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.
Full Text - How is SOS activated? Let us count the ways | PDF (801 KB) - How is SOS activated? Let us count the ways
Evil versus 'eph-ective' use of ephrin-B2 - pp540 - 542
Benhur Lee, Zeynep Akyol Ataman & Lei Jin
doi:10.1038/nsmb0608-540
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.
Full Text - Evil versus 'eph-ective' use of ephrin-B2 | PDF (641 KB) - Evil versus 'eph-ective' use of ephrin-B2
See also: Article by Bowden et al.
Simplifying a complex code - pp542 - 544
Bryan M Turner
doi:10.1038/nsmb0608-542
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.
Full Text - Simplifying a complex code | PDF (325 KB) - Simplifying a complex code
See also: Article by Frederiks et al.
Escaping amyloid fate - pp544 - 546
Blake E Roberts & James Shorter
doi:10.1038/nsmb0608-544
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-
and 
-synuclein down innocuous folding trajectories at the expense of the deleterious states populated during amyloidogenesis.
Full Text - Escaping amyloid fate | PDF (247 KB) - Escaping amyloid fate
See also: Article by Ehrnhoefer et al.
Endo-siRNAs: yet another layer of complexity in RNA silencing - pp546 - 548
Timothy W Nilsen
doi:10.1038/nsmb0608-546
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.
Full Text - Endo-siRNAs: yet another layer of complexity in RNA silencing | PDF (242 KB) - Endo-siRNAs: yet another layer of complexity in RNA silencing
See also: Article by Okamura et al.
Damage control - p548
Inês Chen
doi:10.1038/nsmb0608-548
Research Highlights
Research highlights - p549
doi:10.1038/nsmb0608-549
Full Text - Research highlights | PDF (103 KB) - Research highlights
Articles
Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states - pp550 - 557
Floor Frederiks, Manuel Tzouros, Gideon Oudgenoeg, Tibor van Welsem, Maarten Fornerod, Jeroen Krijgsveld & Fred van Leeuwen
doi:10.1038/nsmb.1432
Abstract - | Full Text - Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states | PDF (497 KB) - Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states | Supplementary information
See also: News and Views by Turner
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers - pp558 - 566
Dagmar E Ehrnhoefer, Jan Bieschke, Annett Boeddrich, Martin Herbst, Laura Masino, Rudi Lurz, Sabine Engemann, Annalisa Pastore & Erich E Wanker
doi:10.1038/nsmb.1437
Abstract - | Full Text - EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers | PDF (1,064 KB) - EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers | Supplementary information
See also: News and Views by Roberts & Shorter
Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2 - pp567 - 572
Thomas A Bowden, A Radu Aricescu, Robert J C Gilbert, Jonathan M Grimes, E Yvonne Jones & David I Stuart
doi:10.1038/nsmb.1435
Abstract - | Full Text - Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2 | PDF (597 KB) - Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2 | Supplementary information
See also: News and Views by Lee et al.
The central unit within the 19S regulatory particle of the proteasome - pp573 - 580
Rina Rosenzweig, Pawel A Osmulski, Maria Gaczynska & Michael H Glickman
doi:10.1038/nsmb.1427
Abstract - | Full Text - The central unit within the 19S regulatory particle of the proteasome | PDF (638 KB) - The central unit within the 19S regulatory particle of the proteasome | Supplementary information
Two distinct mechanisms generate endogenous siRNAs from bidirectional transcription in Drosophila melanogaster - pp581 - 590
Katsutomo Okamura, Sudha Balla, Raquel Martin, Na Liu & Eric C Lai
doi:10.1038/nsmb.1438
Abstract - | Full Text - Two distinct mechanisms generate endogenous siRNAs from bidirectional transcription in Drosophila melanogaster | PDF (824 KB) - Two distinct mechanisms generate endogenous siRNAs from bidirectional transcription in Drosophila melanogaster | Supplementary information
See also: News and Views by Nilsen
Long single 
-helical tail domains bridge the gap between structure and function of myosin VI - pp591 - 597
Benjamin J Spink, Sivaraj Sivaramakrishnan, Jan Lipfert, Sebastian Doniach & James A Spudich
doi:10.1038/nsmb.1429
Abstract - | Full Text - Long single -helical tail domains bridge the gap between structure and function of myosin VI | PDF (688 KB) - Long single -helical tail domains bridge the gap between structure and function of myosin VI | Supplementary information
Telomerase recruitment by the telomere end binding protein-
facilitates G-quadruplex DNA unfolding in ciliates - pp598 - 604
Katrin Paeschke, Stefan Juranek, Tomas Simonsson, Anne Hempel, Daniela Rhodes & Hans Joachim Lipps
doi:10.1038/nsmb.1422
Abstract - | Full Text - Telomerase recruitment by the telomere end binding protein- facilitates G-quadruplex DNA unfolding in ciliates | PDF (428 KB) - Telomerase recruitment by the telomere end binding protein- facilitates G-quadruplex DNA unfolding in ciliates | Supplementary information
A structural link between inactivation and block of a K+ channel - pp605 - 612
Christian Ader, Robert Schneider, Sönke Hornig, Phanindra Velisetty, Erica M Wilson, Adam Lange, Karin Giller, Iris Ohmert, Marie-France Martin-Eauclaire, Dirk Trauner, Stefan Becker, Olaf Pongs & Marc Baldus
doi:10.1038/nsmb.1430
Abstract - | Full Text - A structural link between inactivation and block of a K+ channel | PDF (1,302 KB) - A structural link between inactivation and block of a K+ channel | Supplementary information
Internal dynamics control activation and activity of the autoinhibited Vav DH domain - pp613 - 618
Pilong Li, Ilídio R S Martins, Gaya K Amarasinghe & Michael K Rosen
doi:10.1038/nsmb.1428
Abstract - | Full Text - Internal dynamics control activation and activity of the autoinhibited Vav DH domain | PDF (529 KB) - Internal dynamics control activation and activity of the autoinhibited Vav DH domain | Supplementary information
Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum - pp619 - 625
Zachary E R Newby, Joseph O'Connell III, Yaneth Robles-Colmenares, Shahram Khademi, Larry J Miercke & Robert M Stroud
doi:10.1038/nsmb.1431
PDB code
3D view
Abstract - | Full Text - Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum | PDF (557 KB) - Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum | Supplementary information
Structural insights into human KAP1 PHD finger–bromodomain and its role in gene silencing - pp626 - 633
Lei Zeng, Kyoko L Yap, Alexey V Ivanov, Xueqi Wang, Shiraz Mujtaba, Olga Plotnikova, Frank J Rauscher III & Ming-Ming Zhou
doi:10.1038/nsmb.1416
PDB code
3D view
Abstract - | Full Text - Structural insights into human KAP1 PHD finger–bromodomain and its role in gene silencing | PDF (732 KB) - Structural insights into human KAP1 PHD finger–bromodomain and its role in gene silencing | Supplementary information
Triple-helix structure in telomerase RNA contributes to catalysis - pp634 - 640
Feng Qiao & Thomas R Cech
doi:10.1038/nsmb.1420
Abstract - | Full Text - Triple-helix structure in telomerase RNA contributes to catalysis | PDF (587 KB) - Triple-helix structure in telomerase RNA contributes to catalysis | Supplementary information
Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments - pp641 - 650
Tobias Haslberger, Agnieszka Zdanowicz, Ingo Brand, Janine Kirstein, Kürsad Turgay, Axel Mogk & Bernd Bukau
doi:10.1038/nsmb.1425
Abstract - | Full Text - Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments | PDF (701 KB) - Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments | Supplementary information
Erratum
Erratum: Membrane-dependent signal integration by the Ras activator Son of sevenless - p651
Jodi Gureasko, William J Galush, Sean Boykevisch, Holger Sondermann, Dafna Bar-Sagi, Jay T Groves & John Kuriyan
doi:10.1038/nsmb0608-651a
Full Text - Erratum: Membrane-dependent signal integration by the Ras activator Son of sevenless | PDF (139 KB) - Erratum: Membrane-dependent signal integration by the Ras activator Son of sevenless
Corrigendum
Corrigendum: The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction - p651
Zhiping Wu, Matthew A Wagner, Lemin Zheng, John S Parks, Jacinto M Shy III, Jonathan D Smith, Valentin Gogonea & Stanley L Hazen
doi:10.1038/nsmb0608-651b
Full Text - Corrigendum: The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction | PDF (139 KB) - Corrigendum: The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction