Telehealth and GP service Babylon has rolled out a "COVID-19 Care Assistant" with a raft of features designed to help subscribers cope with symptoms during the pandemic, from the safety of their phone screen

Startups moving to the scale-up phase will naturally experience growing pains, here's how to manage your team through that period with as little disruption as possible

The relationship wellness app is seeing a significant uptick in interest as couples are locked down together during the COVID-19 pandemic

Robert Grizzard and Jeffrey D. Vaaler
Trans. Amer. Math. Soc. 373 (2020), 3235-3259.
Abstract, references and article information

I. Arab and P. E. Oliveira
Theor. Probability and Math. Statist. 99 (2020), 19-37.
Abstract, references and article information

Time: 9:00 AM, Location: Senate Chamber

Cédric Arhancet
Proc. Amer. Math. Soc. 148 (2020), 2551-2563.
Abstract, references and article information

Qingying Bu
Proc. Amer. Math. Soc. 148 (2020), 2459-2467.
Abstract, references and article information

To celebrate the 30th anniversary of the Cultural Centre, the Leisure & Cultural Services Department will hold a fun day from noon to 5.30pm on November 9.

The centre’s venue partners, the Hong Kong Chinese Orchestra, the Hong Kong Philharmonic Orchestra, the Hong Kong Ballet and Zuni Icosahedron will use the latest technology in the foyer to present Western and Chinese music, a ballet performance and sound and scene recreation of the former Kowloon-Canton Railway Station.

At the piazza areas, more than 40 dancers will perform works by acclaimed and emerging choreographers and lead visitors to discover every corner of the centre.

Artist Enoch Cheng will curate "Unseen Scene" in the backstage area to display the magic behind a show through music, dance, projections and other special performances.

Additional programmes will include the Stage & Technology Workshop and the 30th anniversary exhibition "Traces of the Past & Future".

Besides free events on the fun day, the centre will hold a celebratory concert at 8pm on November 29 and 30. Pieces specially selected from the repertoire of the centre's opening concert 30 years ago will be presented.

Click here for details.

Asian Ethnic Cultural Performances 2019 will be staged on Sunday to demonstrate the diversity of Asia’s cultures.

The event will feature ethnic performances and activities with representatives from 19 Asian countries and places taking part.

Korean traditional Nongak and Taepyeongmu dances, a Japanese Tokushima Awa dance, Indian classical and Bollywood dances, and folk dance performances of countries such as Bangladesh, Laos, Vietnam, the Philippines and Sri Lanka will be showcased.

Hong Kong and Macau arts groups will stage a hip hop lion dance and a cheerleading performance.

Other activities include traditional arts and crafts, costume and food displays, as well as a bamboo musical instrument workshop.

A CIBS mobile studio supported by Radio Television Hong Kong will also be set up to let members of the public learn about broadcasting.

The event will be held from 2pm to 6pm at the Cultural Centre Piazza. Admission is free.

Click here for details.

The East Kowloon Cultural Centre Public Artwork Commissioning Project is inviting artists, designers and architects to create an art landscape for the centre.

Presented by the Leisure & Cultural Services Department and organised by the Art Promotion Office, the project endeavors to capture and showcase the past, present and future of East Kowloon.

The commissioned artworks will represent five themes - memory, impression, moment, dream and imagination - aiming to display the district’s changing nature, and to manifest the local community’s cultural sustainability, aspirations and dreams.

Interested participants must submit their preliminary proposal with their curriculum vitae, documentation of their previous artwork and the artistic concept of the proposed artwork.

All proposals must be delivered to the centre’s Public Art Project Management Team at G/F, 50-54 Lok Ku Road, Sheung Wan before 7pm on May 4.

Participants shortlisted by the selection panel are required to submit detailed proposals before 7pm on June 30 for the next stage of the selection process.

Up to three proposals shall be chosen by the selection panel for commissioning and installing in the centre.

Plans for a new multi-million euro film production hub in County Limerick have been set in motion. An agreement has been arranged between Limerick City and County Council and Ardmore Studios, which in the past has provided facilities for several popular film and television productions such as ‘Braveheart’, ‘Excalibur’, ‘The Tudors’ and ‘Camelot’, and more recently for ‘Frank’ and ‘Penny Dreadful’.

To reduce social contact in light of the COVID-19 epidemic, the Primary One Central Allocation results will be posted to parents.

Announcing the move today, the Education Bureau said it will deliver door-to-door the Primary One Registration Form with Central Allocation results to parents from June 3 to 4 through Hongkong Post’s Local CourierPost service.

If no one is present to receive the item at the time of delivery, a mail collection notification card will be left for parents to collect it from the designated post office from the afternoon of the following working day.

If parents have not received the Primary One Registration Form or the notification card by June 5, they can collect the registration form at the designated Collection Centre from June 6 to 7.

The Education Bureau will send letters to parents tomorrow to notify them of the arrangements.

Parents can get updates on the latest arrangements for the release of Central Allocation results and registration through the bureau’s press releases and messages posted on its website.

Call 2891 0088 for information on Primary One admission. For further enquiries, contact the bureau's School Places Allocation Section (Primary One Admission) on 2832 7700 or 2832 7740.

Toni Tripp-Reimer
Jan 1, 2001; 14:
Articles

Brenna Cholerton
Nov 1, 2016; 29:210-219
From Research to Practice

Ruban Dhaliwal
Feb 1, 2014; 27:9-20
Research to Practice

Ryan A. Ristau
Nov 1, 2013; 26:211-215
From Research to Practice

Sue McLaughlin
Oct 1, 2010; 23:272-277
Special Report

Mays H. Vue
Aug 1, 2011; 24:171-177
Pharmacy and Therapeutics

Katherine S. O’Neal
Nov 1, 2016; 29:249-252
Pharmacy and Therapeutics

Abdur Rehman
Nov 1, 2011; 24:234-238
Pharmacy and Therapeutics

updated April 1, 2020

In response to current challenges that colleges and universities face as a result of the spread of COVID-19, the American Mathematical Society is offering libraries and institutions additional support, in line with recommendations in the ICOLC Statement on the Global COVID-19 Pandemic and Its Impact on Library Services and Resources.

The AMS is also participating in the Copyright Clearance Center Education Continuity License program, providing access to our content for distance learning and other educational uses at no cost to the user.

We are extending grace access for content hosted on our platforms (including MathSciNet) through the end of May for our existing customers. We will re-evaluate this timing as needed.

As courses transition to online, we can provide instructors with complimentary electronic “reserve” copies of our textbooks for cases in which students do not have access to their print copies.

E-books purchased through the perpetual access model on the AMS platform are always available DRM-free with unlimited simultaneous use. In addition, we are partnering with ProQuest to allow multi-user access through mid-June to all e-books purchased on their platforms. Read ProQuest’s statement.

We are providing remote access to all our content, including MathSciNet. In normal circumstances, this remote access can be set up while on campus or while connected via institution VPN (in order to validate IP-based access). We realize many students, faculty, and researchers did not have an opportunity to initiate this access before leaving campus, so we have given instructions to our library partners on how patrons can connect to our content. Please contact your librarian for assistance.

Libraries: if you have not received instructions to share with your patrons, please email us at cust-serv@ams.org or be in touch about any other of your library’s needs.

Review all AMS Resources & Updates.

General Stations: 1 to 2 (Health Risk: Low)

Roadside Stations: 2 (Health Risk: Low)

(University of Southampton) Scientists have published highly detailed images of lab-grown neurons using Extreme Ultraviolet radiation that could aid the analysis of neurodegenerative diseases.

(Ecole Polytechnique Fédérale de Lausanne) EPFL chemists have developed sponges to capture various target substances, like gold, mercury and lead, dissolved in solution. The sponges are actually porous crystals called metal organic frameworks, and now one exists for capturing toxic hexavalent chromium from water.

(University of Illinois Grainger College of Engineering) Three Nick Holonyak Jr., Micro and Nanotechnology Lab (HMNTL) faculty members received NSF Rapid Response Research (RAPID) program grants, all of which aim to shorten the amount of time it takes to process a COVID-19 test with less false negatives. Current tests can take as long as five days for results to be.

Protein phosphatase 2A (PP2A) is a large enzyme family responsible for most cellular Ser/Thr dephosphorylation events. PP2A substrate specificity, localization, and regulation by second messengers rely on more than a dozen regulatory subunits (including B/R2, B'/R5, and B″/R3), which form the PP2A heterotrimeric holoenzyme by associating with a dimer comprising scaffolding (A) and catalytic (C) subunits. Because of partial redundancy and high endogenous expression of PP2A holoenzymes, traditional approaches of overexpressing, knocking down, or knocking out PP2A regulatory subunits have yielded only limited insights into their biological roles and substrates. To this end, here we sought to reduce the complexity of cellular PP2A holoenzymes. We used tetracycline-inducible expression of pairs of scaffolding and regulatory subunits with complementary charge-reversal substitutions in their interaction interfaces. For each of the three regulatory subunit families, we engineered A/B charge–swap variants that could bind to one another, but not to endogenous A and B subunits. Because endogenous Aα was targeted by a co-induced shRNA, endogenous B subunits were rapidly degraded, resulting in expression of predominantly a single PP2A heterotrimer composed of the A/B charge–swap pair and the endogenous catalytic subunit. Using B'δ/PPP2R5D, we show that PP2A complexity reduction, but not PP2A overexpression, reveals a role of this holoenzyme in suppression of extracellular signal–regulated kinase signaling and protein kinase A substrate dephosphorylation. When combined with global phosphoproteomics, the PP2A/B'δ reduction approach identified consensus dephosphorylation motifs in its substrates and suggested that residues surrounding the phosphorylation site play roles in PP2A substrate specificity.

Although a robust inflammatory response is needed to combat infection, this response must ultimately be terminated to prevent chronic inflammation. One mechanism that terminates inflammatory signaling is the production of alternative mRNA splice forms in the Toll-like receptor (TLR) signaling pathway. Whereas most genes in the TLR pathway encode positive mediators of inflammatory signaling, several, including that encoding the MyD88 signaling adaptor, also produce alternative spliced mRNA isoforms that encode dominant-negative inhibitors of the response. Production of these negatively acting alternatively spliced isoforms is induced by stimulation with the TLR4 agonist lipopolysaccharide (LPS); thus, this alternative pre-mRNA splicing represents a negative feedback loop that terminates TLR signaling and prevents chronic inflammation. In the current study, we investigated the mechanisms regulating the LPS-induced alternative pre-mRNA splicing of the MyD88 transcript in murine macrophages. We found that 1) the induction of the alternatively spliced MyD88 form is due to alternative pre-mRNA splicing and not caused by another RNA regulatory mechanism, 2) MyD88 splicing is regulated by both the MyD88- and TRIF-dependent arms of the TLR signaling pathway, 3) MyD88 splicing is regulated by the NF-κB transcription factor, and 4) NF-κB likely regulates MyD88 alternative pre-mRNA splicing per se rather than regulating splicing indirectly by altering MyD88 transcription. We conclude that alternative splicing of MyD88 may provide a sensitive mechanism that ensures robust termination of inflammation for tissue repair and restoration of normal tissue homeostasis once an infection is controlled.

Hippo pathway signaling limits cell growth and proliferation and maintains the stem-cell niche. These cellular events result from the coordinated activity of a core kinase cassette that is regulated, in part, by interactions involving Hippo, Salvador, and dRassF. These interactions are mediated by a conserved coiled-coil domain, termed SARAH, in each of these proteins. SARAH domain–mediated homodimerization of Hippo kinase leads to autophosphorylation and activation. Paradoxically, SARAH domain–mediated heterodimerization between Hippo and Salvador enhances Hippo kinase activity in cells, whereas complex formation with dRassF inhibits it. To better understand the mechanism by which each complex distinctly modulates Hippo kinase and pathway activity, here we biophysically characterized the entire suite of SARAH domain–mediated complexes. We purified the three SARAH domains from Drosophila melanogaster and performed an unbiased pulldown assay to identify all possible interactions, revealing that isolated SARAH domains are sufficient to recapitulate the cellular assemblies and that Hippo is a universal binding partner. Additionally, we found that the Salvador SARAH domain homodimerizes and demonstrate that this interaction is conserved in Salvador's mammalian homolog. Using native MS, we show that each of these complexes is dimeric in solution. We also measured the stability of each SARAH domain complex, finding that despite similarities at both the sequence and structural levels, SARAH domain complexes differ in stability. The identity, stoichiometry, and stability of these interactions characterized here comprehensively reveal the nature of SARAH domain–mediated complex formation and provide mechanistic insights into how SARAH domain–mediated interactions influence Hippo pathway activity.