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?

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

Full Text - Damage control | PDF (121 KB) - Damage control

Research highlights - p549

doi:10.1038/nsmb0608-549

Full Text - Research highlights | PDF (103 KB) - Research highlights

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

• PDB code

  • 2VSM
  • 2VSK

• 3D view

  • 2VSM
  • 2VSK

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

  • 3C02

• 3D view

  • 3C02

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

  • 2RO1

• 3D view

  • 2RO1

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: 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: 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