Biochemistry

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

ChIP-MS reveals the local chromatin composition by label-free quantitative proteomics

1. Wai Khang Yong
2. Grishma Rane
3. Nurkaiyisah Zaal Anuar
4. Xiaoman Shao
5. Chai Yeen Goh
6. Vartika Khanchandani
7. Vivian L. S. Kuan
8. Maya Jeitany
9. H. Phillip Koeffler
10. Lih-Wen Deng
11. Takaomi Sanda
12. Dennis Kappei

Reviewed by Review Commons

Conformational regulation and target-myristoyl switch of calcineurin B homologous protein 3

1. Florian Becker
2. Simon Fuchs
3. Lukas Refisch
4. Friedel Drepper
5. Wolfgang Bildl
6. Uwe Schulte
7. Shuo Liang
8. Jonas Immanuel Heinicke
9. Sierra C Hansen
10. Clemens Kreutz
11. Bettina Warscheid
12. Bernd Fakler
13. Evgeny V Mymrikov
14. Carola Hunte

• Curated by eLife

  eLife assessment

  In this work, the authors provide important mechanistic insights into how the intracellular effector protein Calcineurin B homologous protein 3 (CHP3) can be regulated in a calcium-independent manner to expose its lipid binding site. Compelling evidence demonstrates a binding partner protein (NHE1) triggers a conformation change and exposure of the myristoyl group in CHP3 resulting in membrane association. This provides mechanistic insight into the signalling mechanisms achieved by CHP3 in a target-dependent manner, which will be of broad scientific interest.

Reviewed by eLife

Purification and biochemical characterization of the DNA binding domain of the nitrogenase transcriptional activator NifA from Gluconacetobacter diazotrophicus

1. Heidi G. Standke
2. Lois Kim
3. Cedric P. Owens

Reviewed by Arcadia Science

Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity

1. Pauline Jacquet
2. Raphaël Billot
3. Amir Shimon
4. Nathan Hoekstra
5. Céline Bergonzi
6. Anthony Jenks
7. Eric Chabrière
8. David Daudé
9. Mikael H. Elias

Reviewed by Arcadia Science

Structural and biochemical characterisation of the N-Carbamoyl-β-Alanine Amidohydrolase from Rhizobium radiobacter MDC 8606

1. Ani Paloyan
2. Armen Sargsyan
3. Mariam D. Karapetyan
4. Artur Hambardzumyan
5. Sergey Kocharov
6. Henry Panosyan
7. Karine Dyukova
8. Marina Kinosyan
9. Anna Krüger
10. Cecilia Piergentili
11. Will A. Stanley
12. Arnaud Baslé
13. Jon Marles-Wright
14. Garabed Antranikian

Reviewed by Arcadia Science