1. Profiling dynamic RNA–protein interactions using small-molecule-induced RNA editing

    This article has 2 authors:
    1. Kyung W. Seo
    2. Ralph E. Kleiner

    Reviewed by ASAPbio crowd review

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  2. N-terminal domain on dystroglycan enables LARGE1 to extend matriglycan on α-dystroglycan and prevents muscular dystrophy

    This article has 12 authors:
    1. Hidehiko Okuma
    2. Jeffrey M Hord
    3. Ishita Chandel
    4. David Venzke
    5. Mary E Anderson
    6. Ameya S Walimbe
    7. Soumya Joseph
    8. Zeita Gastel
    9. Yuji Hara
    10. Fumiaki Saito
    11. Kiichiro Matsumura
    12. Kevin P Campbell
    This article has been curated by 1 group:
    • Curated by eLife

      eLife assessment

      The authors show that the amino terminus of dystroglycan is required for the production of full-length matriglycan, and in its absence, a shorter matriglycan is produced that is still capable of binding laminin. alpha-DGN deficient mice have abnormal neuromuscular synapses and reduced lengthening contraction-induced force. Overall, the well-controlled and convincing data mostly support the main conclusions, which will be of interest to scientists in membrane biology, muscle biology, and glycobiology.

    Reviewed by eLife

    This article has 3 evaluationsAppears in 1 listLatest version Latest activity
  3. The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)

    This article has 5 authors:
    1. Michael J Rale
    2. Brianna Romer
    3. Brian P Mahon
    4. Sophie M Travis
    5. Sabine Petry
    This article has been curated by 1 group:
    • Curated by eLife

      eLife assessment

      This paper is of interest to cell biologists studying the mechanisms and control of microtubule nucleation. In this work, the authors use a novel protocol for the purification of gamma-TuRCs and for the production of gamma-TuNA that enables them to demonstrate a clear activating effect of gamma-TuNA on microtubule nucleation that depends on the dimerization of gamma-TuNA protein chains.

    Reviewed by eLife

    This article has 4 evaluationsAppears in 1 listLatest version Latest activity
  4. ATP-competitive and allosteric inhibitors induce differential conformational changes at the autoinhibitory interface of Akt

    This article has 6 authors:
    1. Alexandria L Shaw
    2. Matthew AH Parson
    3. Linda Truebestein
    4. Meredith L Jenkins
    5. Thomas A Leonard
    6. John E Burke

    Reviewed by ASAPbio crowd review

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  5. MitoStores: chaperone‐controlled protein granules store mitochondrial precursors in the cytosol

    This article has 7 authors:
    1. Lena Krämer
    2. Niko Dalheimer
    3. Markus Räschle
    4. Zuzana Storchová
    5. Jan Pielage
    6. Felix Boos
    7. Johannes M Herrmann

    Reviewed by ASAPbio crowd review

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  6. Tuning aromatic contributions by site-specific encoding of fluorinated phenylalanine residues in bacterial and mammalian cells

    This article has 12 authors:
    1. Grace D. Galles
    2. Daniel T. Infield
    3. Colin J. Clark
    4. Marcus L. Hemshorn
    5. Shivani Manikandan
    6. Frederico Fazan
    7. Ali Rasouli
    8. Emad Tajkhorshid
    9. Jason D. Galpin
    10. Richard B. Cooley
    11. Ryan A. Mehl
    12. Christopher A. Ahern
    This article has been curated by 1 group:
    • Curated by Biophysics Colab

      Endorsement statement (3 October 2022)

      The preprint by Galles et al. reports the generation of pyrrolysine-based aminoacyl-tRNA synthetases capable of incorporating fluorinated phenylalanine non-canonical amino acids into proteins expressed in either bacteria or mammalian cells. For the most extensively characterized synthetases, fluorinated phenylalanine derivatives were successfully incorporated into GFP and two membrane proteins (CFTR and Nav1.5) at expression levels adequate for biochemical studies, suggesting that the approach could be combined with multiple different structural and biophysical techniques. The work provides a valuable tool that will enable the functional role of cation-pi interactions to be interrogated in both soluble and integral membrane proteins.

      (This endorsement by Biophysics Colab refers to version 2 of this preprint, which has been revised in response to peer review of version 1.)

    Reviewed by Biophysics Colab

    This article has 3 evaluationsAppears in 2 listsLatest version Latest activity
  7. Adiponectin reverses β‐Cell damage and impaired insulin secretion induced by obesity

    This article has 9 authors:
    1. Ana Cláudia Munhoz
    2. Julian D. C. Serna
    3. Eloisa Aparecida Vilas‐Boas
    4. Camille C. Caldeira da Silva
    5. Tiago G. Santos
    6. Francielle C. Mosele
    7. Sergio L. Felisbino
    8. Vilma Regina Martins
    9. Alicia J. Kowaltowski

    Reviewed by ASAPbio crowd review

    This article has 1 evaluationAppears in 2 listsLatest version Latest activity
  8. Structural basis of Yta7 ATPase-mediated nucleosome disassembly

    This article has 5 authors:
    1. Feng Wang
    2. Xiang Feng
    3. Qing He
    4. Hua Li
    5. Huilin Li
    This article has been curated by 1 group:
    • Curated by eLife

      eLife Assessment:

      This manuscript presents the cryo-EM structure of the Yta7 chromatin remodeler, which provides new mechanistic insight into how this AAA+ protein unfolds histone H3 in yeast for DNA replication. The study details the putative role of the C-terminal bromodomains, as well as an N-terminal bromo-interaction motif, in engaging nucleosomes for subsequent capture of the H3 tail for ATP-driven translocation by the upper AAA1 ring. The accompanying functional work helps establish the proposed nucleosome recognition mechanism, providing a structural framework that may be generally used by AAA+ nucleosome remodelers. The work will be of interest to colleagues in chromatin biology as well as all who study the very large family of AAA-ATPases.

      (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 #3 agreed to share their name with the authors.)

    Reviewed by eLife

    This article has 4 evaluationsAppears in 1 listLatest version Latest activity
  9. Didemnin B and ternatin-4 differentially inhibit conformational changes in eEF1A required for aminoacyl-tRNA accommodation into mammalian ribosomes

    This article has 10 authors:
    1. Manuel F Juette
    2. Jordan D Carelli
    3. Emily J Rundlet
    4. Alan Brown
    5. Sichen Shao
    6. Angelica Ferguson
    7. Michael R Wasserman
    8. Mikael Holm
    9. Jack Taunton
    10. Scott C Blanchard
    This article has been curated by 1 group:
    • Curated by eLife

      eLife Assessment:

      Juette and coworkers employed single-molecule fluorescence, cryogenic-electron microscopy structures, and in vivo measurements to investigate the mechanism whereby two natural products with potential as cancer therapeutics, didemnin B and ternatin-4, act. The compounds are shown to inhibit tRNA accommodation within the ribosomal A site during translation elongation by interfering with movement of eukaryotic elongation factor 1 alpha after its activation by the GTPase activation site of the ribosome, with the degree and nature of this restriction differing subtly between the two compounds, leading to more marked differences in their effects on global translation and cell growth. The compelling results of this interdisciplinary work solidify prior conclusions, particularly on didemnin B, and illuminate the similarities and differences on how these two drugs interfere with the normal functioning of the elongating ribosome in vitro and inhibit protein synthesis and cell growth in vivo. Some revisions of figures and text are required to clarify the results and the authors' interpretations.

      (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, Reviewer #2 and Reviewer #3 agreed to share their names with the authors.)

    Reviewed by eLife

    This article has 5 evaluationsAppears in 1 listLatest version Latest activity
  10. A novel fold for acyltransferase-3 (AT3) proteins provides a framework for transmembrane acyl-group transfer

    This article has 6 authors:
    1. Kahlan E Newman
    2. Sarah N Tindall
    3. Sophie L Mader
    4. Syma Khalid
    5. Gavin H Thomas
    6. Marjan W Van Der Woude
    This article has been curated by 1 group:
    • Curated by eLife

      Evaluation Summary:

      By integrating a range of computational techniques, the authors generated a structural model for the AT3 domain, which is predicted to adopt a new fold. The key features of the structural model are consistent with the activity of the enzyme as an acyltransferase, with a transmembrane channel that can accommodate an acyl-CoA donor, and an outer cavity formed with a second domain that can accommodate a nascent LPS molecule as substrate. Overall, the study will help stimulate specific experimental analyses that can further evaluate and improve the model for better mechanistic understanding of this class of enzymes. The work will be of interest to structural biologists, and all studying acyltransferase 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. Reviewer #2 agreed to share their name with the authors.)

    Reviewed by eLife

    This article has 3 evaluationsAppears in 1 listLatest version Latest activity
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