Biochemistry

Glutamine metabolism modulates chondrocyte inflammatory response

1. Manoj Arra
2. Gaurav Swarnkar
3. Naga Suresh Adapala
4. Syeda Kanwal Naqvi
5. Lei Cai
6. Muhammad Farooq Rai
7. Srikanth Singamaneni
8. Gabriel Mbalaviele
9. Robert Brophy
10. Yousef Abu-Amer

• Curated by eLife

  Evaluation Summary:

  This manuscript focuses on identifying how metabolism can influence the response of cartilage cells to inflammation. This has relevance to the painful disease known as osteoarthritis. Modulation of cell metabolism in the right direction can serve to protect joint cartilage from the negative effects of inflammation which causes onset and disease progression.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. The reviewers remained anonymous to the authors.)

Reviewed by eLife

Fusion with heat-resistant obscure (Hero) proteins have the potential to improve the molecular property of recombinant proteins

1. Eri Morimoto
2. Kotaro Tsuboyama
3. Yukihide Tomari

Reviewed by ASAPbio crowd review

Translational Activity Controls Ribophagic Flux and Turnover of Distinct Ribosome Pools

1. Jakob Trendel
2. Milan Aleksić
3. Matilde Bertolini
4. Marco Jochem
5. Günter Kramer
6. Stefan Pfeffer
7. Bernd Bukau
8. Jeroen Krijgsveld

Reviewed by ASAPbio crowd review

Increasing protein stability by inferring substitution effects from high-throughput experiments

1. Rasmus Krogh Norrild
2. Kristoffer Enøe Johansson
3. Charlotte O’Shea
4. Jens Preben Morth
5. Kresten Lindorff-Larsen
6. Jakob Rahr Winther

Reviewed by ASAPbio crowd review

Double NPY motifs at the N-terminus of the yeast t-SNARE Sso2 synergistically bind Sec3 to promote membrane fusion

1. Maximilian Peer
2. Hua Yuan
3. Yubo Zhang
4. Katharina Korbula
5. Peter Novick
6. Gang Dong

Reviewed by Review Commons

Specific binding of Hsp27 and phosphorylated Tau mitigates abnormal Tau aggregation-induced pathology

1. Shengnan Zhang
2. Yi Zhu
3. Jinxia Lu
4. Zhenying Liu
5. Amanda G Lobato
6. Wen Zeng
7. Jiaqi Liu
8. Jiali Qiang
9. Shuyi Zeng
10. Yaoyang Zhang
11. Cong Liu
12. Jun Liu
13. Zhuohao He
14. R Grace Zhai
15. Dan Li

• Curated by eLife

  Evaluation Summary:

  The authors found elevated Hsp 27 levels in brains from Alzheimer disease patients. Hsp27 co-localized with p-Tau, efficiently prevented pTau fibrillation in vitro, and mitigated neuropathology of pTau aggregation in a Drosophila tauopathy model. A series of biochemical assays is presented to supporrt the claim that Hsp27 prevents abnormal Tau aggregation and p-Tau pathology. Overall, the study is well designed and presented, and the data convincingly support this major conclusion, which is relevant to colleagues studying neurodegeneration.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 agreed to share their name with the authors.)

Reviewed by eLife

Structural and biochemical basis of interdependent FANCI‐FANCD2 ubiquitination

1. Kimon Lemonidis
2. Martin L Rennie
3. Connor Arkinson
4. Viduth K Chaugule
5. Mairi Clarke
6. James Streetley
7. Helen Walden

Reviewed by Review Commons

Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster

1. Trixia M Buscagan
2. Jens T Kaiser
3. Douglas C Rees

• Curated by eLife

  Evaluation Summary:

  This manuscript describes the unexpected observation of selenium exchange into an iron-sulfur cluster cofactor of a component of nitrogenase. The work sets the stage for future mechanistic study of this phenomenon. It also provides a roadmap for the study of sulfide exchange in other classes of iron-sulfur cluster enzymes.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. The reviewers remained anonymous to the authors.)

Reviewed by eLife

Pseudomonas aeruginosa C-Terminal Processing Protease CtpA Assembles into a Hexameric Structure That Requires Activation by a Spiral-Shaped Lipoprotein-Binding Partner

1. Hao-Chi Hsu
2. Michelle Wang
3. Amanda Kovach
4. Andrew J. Darwin
5. Huilin Li

• Curated by eLife

  Evaluation Summary:

  This paper demonstrates an inactive protease in Pseudomonas aeruginosa, CtpA, is regulated by am outer membrane lipoprotein LbcA. Using crystallization and EM strategies, they also provide a complex structure; however, the precise mechanism of regulation is speculative due to the flexible arrangement of protein domains.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 and Reviewer #2 agreed to share their names with the authors.)

Reviewed by eLife

Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin

1. Ennio A. d’Amico
2. Misbha Ud Din Ahmad
3. Verena Cmentowski
4. Mathias Girbig
5. Franziska Müller
6. Sabine Wohlgemuth
7. Andreas Brockmeyer
8. Stefano Maffini
9. Petra Janning
10. Ingrid R. Vetter
11. Andrew P. Carter
12. Anastassis Perrakis
13. Andrea Musacchio

Reviewed by Review Commons