We bring you the latest news from the healthcare about the health care in the United Kingdom.

donderdag 8 februari 2018

Nature Structural & Molecular Biology Contents: 2018 Volume #25 pp 115 - 194

If you are unable to see the message below, click here to view.
Nature Structural & Molecular Biology

Advertisement
To mark the 100th anniversary of the 1918 influenza pandemic, Nature Reviews Microbiology presents a collection including Reviews and research articles from across Nature Research to showcase the latest advances in our understanding of influenza virus biology, evolution and adaptation, and advances in surveillance and drug and vaccine development.

Access the collection online.
TABLE OF CONTENTS

February 2018 Volume 25, Issue 2

Review Articles
Brief Communications
Articles
Technical Reports
 
Advertisement
 
Nature Research ‘lab health’ survey 2018

The Nature Research’s lab health survey aims to find out what makes a research group supportive, productive, and rigorous. The survey should take 10 to 15 minutes to complete and you’ll have the chance to win a £100/$150 Amazon gift card. Your entries will be confidential and results will be featured in Nature

Complete the survey today >>

 
Advertisement
nature.com webcasts

Springer Nature presents a custom webcast on: Untangling Neurodegenerative Diseases using Cryo-Electron Microscopy
Date: Wednesday, February 7, 2018 

Register for the webcast and live Q&A session >>

Sponsored by: Thermo Fisher Scientific 
 

Advertisement
nature.com webcasts

Springer Nature presents a custom webcast on: Transforming Translational Research: CANscript™ - A Better Predictive Model For Oncology

Date: Tuesday, February 20, 2018 

Register for the webcast and live Q&A session 

Sponsored by: 
Mitra Biotech 
 

Review Articles

 

Structural insights into the design of novel anti-influenza therapies    pp115 - 121
Nicholas C. Wu & Ian A. Wilson
doi:10.1038/s41594-018-0025-9

Wu and Wilson review our structural knowledge of influenza virus HA and broadly neutralizing antibodies, which have opened the way for design of novel vaccines and therapeutics.

 

The ring-shaped hexameric helicases that function at DNA replication forks    pp122 - 130
Michael E. O'Donnell & Huilin Li
doi:10.1038/s41594-018-0024-x

In this Review, the authors discuss our current understanding of how the hexameric helicases that catalyze helix unwinding during DNA replication are physically and functionally integrated with other replisome components.

 

Brief Communications

 

Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp    pp131 - 134
Marcus Gallagher-Jones, Calina Glynn, David R. Boyer, Michael W. Martynowycz, Evelyn Hernandez et al.
doi:10.1038/s41594-017-0018-0

MicroED structure of a peptide from the β22 loop of the bank vole prion protein reveals a protofibril stabilized by a dense network of hydrogen bonds.

 

Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex    pp135 - 138

doi:10.1038/s41594-017-0020-6

The cryo-EM structure of the human core CPSF complex, containing CPSF160, WDR33, CPSF30 and Fip1 subunits, bound to its RNA target reveals the mechanism of PAS recognition.

 

Structural & Molecular Biology
JOBS of the week
Assistant Professor, Associate Professor & Professor-Cell & Molecular Biology
University of Mississippi
Assistant, Associate, or Full Professor
Thomas Jefferson University, Sidney Kimmel Cancer Center
PhD Students and Postdoctoral Scientists
University Medical Center Freiburg
Postdoctoral Fellow
University of Pennsylvania - Perelman School of Medicine
Postdoctoral Associate
University of Pittsburgh
More Science jobs from
Structural & Molecular Biology
EVENT
Molecular Biology and Pathogenesis of Avian Viruses
03.09.18
Oxford, UK
More science events from
Advertisement
 
A new open access, multi- and interdisciplinary journal dedicated to publishing the highest quality papers on aging and age-related diseases, the journal is now open for submissions.
 
Explore the benefits of submitting your next research.
 

Articles

 

Cryo-EM structure of the exocyst complex    pp139 - 146
Kunrong Mei, Yan Li, Shaoxiao Wang, Guangcan Shao, Jia Wang et al.
doi:10.1038/s41594-017-0016-2

The structure of the fully assembled yeast exocyst complex, which mediates the tethering of secretory vesicles to the plasma membrane during exocytosis, provides new insights to hierarchical complex assembly and the mechanism of vesicle tethering.

 

TRF1 participates in chromosome end protection by averting TRF2-dependent telomeric R loops    pp147 - 153
Yong Woo Lee, Rajika Arora, Harry Wischnewski & Claus M. Azzalin
doi:10.1038/s41594-017-0021-5

In vitro and cellular assays unexpectedly reveal that shelterin protein TRF2 binds TERRA and stimulates strand invasion within telomere repeats and that TRF1 suppresses this activity to prevent telomere loss and genome instability.

 

Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes    pp154 - 162
Simon Poepsel, Vignesh Kasinath & Eva Nogales
doi:10.1038/s41594-018-0023-y

Cryo-EM analyses of human PRC2 bound to dinucleosomes with one unmodified (substrate) and one H3K27me3-containing (activating) nucleosome support a model for H3K27me3-based PRC2 activation and spreading.

 

Solution structure and elevator mechanism of the membrane electron transporter CcdA    pp163 - 169
Yunpeng Zhou & John H. Bushweller
doi:10.1038/s41594-018-0022-z

An NMR structure of Thermus thermophilus membrane electron transporter CcdA in an oxidized, outward-facing state suggests an elevator-type mechanism shuttles reactive cysteines to relay reducing equivalents across the membrane.

 

Structural basis for recognition of diverse antidepressants by the human serotonin transporter    pp170 - 175
Jonathan A. Coleman & Eric Gouaux
doi:10.1038/s41594-018-0026-8

The X-ray structures of engineered variants of the human serotonin transporter show that the antidepressants sertraline, fluvoxamine and paroxetine occupy the central substrate-binding site and stabilize the transporter in an outward-open conformation.

 

Technical Reports

 

Spatiotemporal allele organization by allele-specific CRISPR live-cell imaging (SNP-CLING)    pp176 - 184
Philipp G. Maass, A. Rasim Barutcu, David M. Shechner, Catherine L. Weiner, Marta Melé et al.
doi:10.1038/s41594-017-0015-3

An allele-specific CRISPR-based DNA imaging technique provides insights into allelic positioning in live mouse cells. Spatiotemporal monitoring reveals that allele positions may fluctuate during cell state transitions.

 

Visualization and analysis of non-covalent contacts using the Protein Contacts Atlas    pp185 - 194
Melis Kayikci, A. J. Venkatakrishnan, James Scott-Brown, Charles N. J. Ravarani, Tilman Flock et al.
doi:10.1038/s41594-017-0019-z

The Protein Contacts Atlas is an interactive resource of non-covalent contacts that can generate multiple representations of non-covalent contacts from PDB structures at different scales, from atoms to subunits and entire complexes.

 

nature events
Natureevents is a fully searchable, multi-disciplinary database designed to maximise exposure for events organisers. The contents of the Natureevents Directory are now live. The digital version is available here.
Find the latest scientific conferences, courses, meetings and symposia on natureevents.com. For event advertising opportunities across the Nature Publishing Group portfolio please contact natureevents@nature.com
More Nature Events

You have been sent this Table of Contents Alert because you have opted in to receive it. You can change or discontinue your e-mail alerts at any time, by modifying your preferences on your nature.com account at: www.nature.com/myaccount
(You will need to log in to be recognised as a nature.com registrant)

For further technical assistance, please contact our registration department

For print subscription enquiries, please contact our subscription department

For other enquiries, please contact our customer feedback department

Springer Nature | One New York Plaza, Suite 4500 | New York | NY 10004-1562 | USA

Springer Nature's worldwide offices:
London - Paris - Munich - New Delhi - Tokyo - Melbourne
San Diego - San Francisco - Washington - New York - Boston

Macmillan Publishers Limited is a company incorporated in England and Wales under company number 785998 and whose registered office is located at The Campus, 4 Crinan Street, London, N1 9XW.

© 2018 Macmillan Publishers Limited, part of Springer Nature. All Rights Reserved.

Springer Nature