eLife

Latest preprint reviews

1. ᴅ-serine suppresses one-carbon metabolism by competing with mitochondrial ʟ-serine transport

   This article has 18 authors:

   1. Masataka Suzuki
   2. Kenichiro Adachi
   3. Pattama Wiriyasermukul
   4. Mariko Fukumura
   5. Ryota Tamura
   6. Yoshinori Hirano
   7. Yumi Aizawa
   8. Tetsuya Miyamoto
   9. Sakiko Taniguchi
   10. Masahiro Toda
   11. Hiroshi Homma
   12. Kohsuke Kanekura
   13. Kenji Yasuoka
   14. Takanori Kanai
   15. Masahiro Sugimoto
   16. Shushi Nagamori
   17. Masato Yasui
   18. Jumpei Sasabe

   This article has been curated by 1 group:

   • Curated by eLife

     eLife Assessment

     This work presents valuable new data on the role of D-Serine and how it competes with its stereoisomer L-Serine to influence metabolism. The work presents a variety of convincing experimental data combined with simulated results to investigate the mechanisms focused on one-carbon metabolism, which is relevant for several research fields. However, some claims are only partially supported by data, and critical areas comparing L- vs D-Serine and further mechanistic studies are required. Furthermore, while the work has potential for various fields, the work has only been studied in a limited cell type and context.

   Reviewed by eLife

2. Identification of nuclear pore proteins at plasmodesmata: potential role in intercellular transport?

   This article has 19 authors:

   1. T Moritz Schladt
   2. Manuel Miras
   3. Jona Obinna Ejike
   4. Mathieu Pottier
   5. Lin Xi
   6. Andrea Restrepo-Escobar
   7. Masayoshi Nakamura
   8. Niklas Pütz
   9. Sebastian Hänsch
   10. Chen Gao
   11. Julia Engelhorn
   12. Marcel Dickmanns
   13. Gwendolyn V Davis
   14. Ahan Dalal
   15. Sven Gombos
   16. Ronja Lange
   17. Rüdiger Simon
   18. Waltraud X Schulze
   19. Wolf B Frommer

   This article has been curated by 1 group:

   • Curated by eLife

     eLife Assessment

     Plasmodesmata are channels that allow cell-cell communication in plants; based on the functional similarities between facilitated transport at plasmodesmata and into the nucleus, the authors present the bold and potentially transformational hypothesis that nuclear pore complex proteins (NUPs) might be involved in plasmodesmata function. Here, the authors localize a subset of NUPs to plasmodesmata using proteomics and fluorescent imaging. They acknowledge many limitations to their work, including potential artifacts and the lack of functional validation of multiple NUPs, which may complicate the interpretation of their mostly solid results. Further experiments will be necessary to fully test this fundamental hypothesis about the function of NUPs at plasmodesmata.

   Reviewed by eLife

3. We couldn't get details of this article at this time:
   10.1101/2024.09.23.614588

4. We couldn't get details of this article at this time:
   10.1101/2025.03.13.643064

5. We couldn't get details of this article at this time:
   10.1101/2025.07.02.662715

6. We couldn't get details of this article at this time:
   10.1101/2025.07.07.663451

7. We couldn't get details of this article at this time:
   10.1101/2025.04.21.649841

8. An interpretable neural network unveils higher-order epistasis in large protein sequence-function relationships

   This article has 2 authors:

   1. Palash Sethi
   2. Juannan Zhou

   This article has been curated by 1 group:

   • Curated by eLife

     eLife Assessment

     In this important work, the authors present a new transformer-based neural network designed to isolate and quantify higher-order epistasis in protein sequences. They provide solid evidence that higher-order epistasis can play key roles in protein function. This work will be of interest to the communities interested in modeling biological sequence data and understanding mutational effects.

   Reviewed by eLife

9. We couldn't get details of this article at this time:
   10.1101/2024.02.04.578824

10. Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity

    This article has 14 authors:

    1. Eric Greene
    2. Richard Muniz
    3. Hiroki Yamamura
    4. Samuel E Hoff
    5. Priyanka Bajaj
    6. Markus Tecson CB Tecson
    7. Cyrina Geluz
    8. D John Lee
    9. Erin M Thompson
    10. Angelika Arada
    11. Gyun Min Lee
    12. Massimiliano Bonomi
    13. Justin M Kollman
    14. James S Fraser

    This article has been curated by 1 group:

    • Curated by eLife

      eLife Assessment

      This manuscript employs cryo-EM, mutational analysis, and biochemical assays to explore the molecular basis by which glutamine promotes filamentation and regulates the activity of human glutamine synthetase (hGS) by stabilizing interactions between hGS decamers. The combined structural and biochemical data supporting the proposed mechanism are solid, although the evidence for a higher-order filamentous architecture and the precise assignment of the interface density would benefit from additional support. This work will be of particular interest and useful to groups interested in understanding the molecular basis of nutrient sensing, cellular metabolism, and structural regulation of enzyme activity.

    Reviewed by eLife