Biochemistry

Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

1. Alexandra C. Walls
2. Young-Jun Park
3. M. Alejandra Tortorici
4. Abigail Wall
5. Andrew T. McGuire
6. David Veesler

Reviewed by ScreenIT

X-ray Structure of Main Protease of the Novel Coronavirus SARS-CoV-2 Enables Design of α-Ketoamide Inhibitors

1. Linlin Zhang
2. Daizong Lin
3. Xinyuanyuan Sun
4. Katharina Rox
5. Rolf Hilgenfeld

Reviewed by ScreenIT

Structural basis for the recognition of the 2019-nCoV by human ACE2

1. Renhong Yan
2. Yuanyuan Zhang
3. Yingying Guo
4. Lu Xia
5. Qiang Zhou

Reviewed by ScreenIT

Structure of dimeric full-length human ACE2 in complex with B ⁰ AT1

1. Renhong Yan
2. Yuanyuan Zhang
3. Yaning Li
4. Lu Xia
5. Qiang Zhou

Reviewed by ScreenIT

Alpha-ketoamides as broad-spectrum inhibitors of coronavirus and enterovirus replication

1. Linlin Zhang
2. Daizong Lin
3. Yuri Kusov
4. Yong Nian
5. Qingjun Ma
6. Jiang Wang
7. Albrecht von Brunn
8. Pieter Leyssen
9. Kristina Lanko
10. Johan Neyts
11. Adriaan de Wilde
12. Eric J. Snijder
13. Hong Liu
14. Rolf Hilgenfeld

Reviewed by ScreenIT

Molecular Modeling Evaluation of the Binding Effect of Ritonavir, Lopinavir and Darunavir to Severe Acute Respiratory Syndrome Coronavirus 2 Proteases

1. Shen Lin
2. Runnan Shen
3. Jingdong He
4. Xinhao Li
5. Xushun Guo

Reviewed by ScreenIT

Nuclear bodies protect phase separated proteins from degradation in stressed proteome

1. Kwan Ho Jung
2. Jiarui Sun
3. Chia-Heng Hsiung
4. Xiaojun Lance Lian
5. Yu Liu
6. Xin Zhang

• Curated by eLife

  eLife assessment

  This study presents a novel fluorescence based imaging strategy to investigate the folding status of RNA-binding proteins (RBPs) and their association with molecular chaperones under stress. It provides fundamental findings that will potentially advance our understanding in the folding and aggregation status of RBPs in nuclear stress bodies in a significant manner. However, there is also the concern that the evidence regarding protein fate is incomplete and additional controls are needed to fully support the conclusion. The imaging methodology can be adapted to study many other proteins that undergo liquid-liquid phase separation under specific cellular conditions.

Reviewed by eLife

Sterol derivative binding to the orthosteric site causes conformational changes in an invertebrate Cys-loop receptor

1. Steven De Gieter
2. Casey I Gallagher
3. Eveline Wijckmans
4. Diletta Pasini
5. Chris Ulens
6. Rouslan G Efremov

• Curated by eLife

  eLife assessment

  This study presents valuable structures of a pentameric ligand-gated ion channel from a thermophilic worm that is a homologue of the well-known mammalian nicotinic receptors. Although the function of the worm receptor is unknown, the authors convincingly identify interesting features for this class of receptors including a steroid detergent that is bound in the canonical neurotransmitter site and that induces conformational changes of the extracellular domains. These observations will be of broad interest to the ligand-gated ion channel community, although it is difficult at this moment to relate these observations to channel function as the channel's activating ligand remains unknown.

Reviewed by eLife

Genome-wide screen reveals Rab12 GTPase as a critical activator of Parkinson’s disease-linked LRRK2 kinase

1. Herschel S Dhekne
2. Francesca Tonelli
3. Wondwossen M Yeshaw
4. Claire Y Chiang
5. Charles Limouse
6. Ebsy Jaimon
7. Elena Purlyte
8. Dario R Alessi
9. Suzanne R Pfeffer

• Curated by eLife

  eLife assessment

  Dhekne et al report a novel pathway for activation of the multi-domain LRRK2 protein kinase by Rab12 GTPase. LRRK2, which is mutated in Parkinson's Disease phosphorylates a subset of Rab proteins involved in intracellular trafficking, and Parkinson's disease-linked mutations increase this phosphorylation. This work adds an important new layer of understanding of this highly complex pathway by revealing that LRRK2's binding to Rab12 enhances its ability to phosphorylate Rab10. This conclusion is supported by compelling evidence from a wide array of rigorous approaches.

Reviewed by eLife

Structural insights into the organization and channel properties of human Pannexin isoforms 1 and 3

1. Nazia Hussain
2. Ashish Apotikar
3. Shabareesh Pidathala
4. Sourajit Mukherjee
5. Ananth Prasad Burada
6. Sujit Kumar Sikdar
7. Vinothkumar R. Kutti
8. Aravind Penmatsa

Reviewed by Biophysics Colab