1. Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif

    This article has 14 authors:
    1. Ramiro Lorenzo
    2. Lucas A. Defelipe
    3. Lucio Aliperti
    4. Stephan Niebling
    5. Tânia F. Custódio
    6. Christian Löw
    7. Jennifer J. Schwarz
    8. Kim Remans
    9. Patricio O. Craig
    10. Lisandro H. Otero
    11. Sebastián Klinke
    12. María García-Alai
    13. Ignacio E. Sánchez
    14. Leonardo G. Alonso

    Reviewed by ScreenIT

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  2. Intra-Helical Salt Bridge Contribution to Membrane Protein Insertion

    This article has 5 authors:
    1. Gerard Duart
    2. John Lamb
    3. Juan Ortiz-Mateu
    4. Arne Elofsson
    5. Ismael Mingarro

    Reviewed by Review Commons

    This article has 4 evaluationsAppears in 1 listLatest version Latest activity
  3. Assembly of higher-order SMN oligomers is essential for metazoan viability and requires an exposed structural motif present in the YG zipper dimer

    This article has 10 authors:
    1. Kushol Gupta
    2. Ying Wen
    3. Nisha S Ninan
    4. Amanda C Raimer
    5. Robert Sharp
    6. Ashlyn M Spring
    7. Kathryn L Sarachan
    8. Meghan C Johnson
    9. Gregory D Van Duyne
    10. A Gregory Matera
    This article has been curated by 1 group:
    • Curated by eLife

      Summary:

      The manuscript describes a very detailed mutagenesis analysis of the dimerization / oligomerization behavior of the protein Survival Motor Neuron. Mutations in this protein cause Spinal Muscular Atrophy. Analysis of disease causing mutations show a correlation with their impact on oligomerization. A structural model that includes different domains of the protein involved in oligomerization is built from these analyses.

      This analysis is an excellent source for researchers working in the field of SMN proteins. A mechanistic interpretation of how changes in the oligomerization lead to the disease or impact the formation of membraneless organelles, is however missing. Thus, the manuscript provides an enormous amount of important mutational analysis data but does not lead to a significant advancement in our understanding of the disease mechanism.

      (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

    This article has 5 evaluationsAppears in 1 listLatest version Latest activity
  4. SARS-CoV-2 beta variant substitutions alter spike glycoprotein receptor binding domain structure and stability

    This article has 2 authors:
    1. Daniel L. Moss
    2. Jay Rappaport

    Reviewed by ScreenIT

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  5. Impacts on the structure-function relationship of SARS-CoV-2 spike by B.1.1.7 mutations

    This article has 10 authors:
    1. Tzu-Jing Yang
    2. Pei-Yu Yu
    3. Yuan-Chih Chang
    4. Kang-Hao Liang
    5. Hsian-Cheng Tso
    6. Meng-Ru Ho
    7. Wan-Yu Chen
    8. Hsiu-Ting Lin
    9. Han-Chung Wu
    10. Shang-Te Danny Hsu

    Reviewed by ScreenIT

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  6. AKAP79 enables calcineurin to directly suppress protein kinase A activity

    This article has 8 authors:
    1. Timothy W Church
    2. Parul Tewatia
    3. Saad Hannan
    4. João Antunes
    5. Olivia Eriksson
    6. Trevor G Smart
    7. Jeanette Hellgren Kotaleski
    8. Matthew G Gold
    This article has been curated by 1 group:
    • Curated by eLife

      Evaluation Summary:

      This manuscript will be of interest to neuroscientists as well as a broad audience of cell biologists, as it provides new insight into the myriad of cellular functions regulated by the well-studied cAMP-dependent protein kinase, PKA. Rigorous biochemical data supports a model for PKA inactivation wherein dephosphorylation of the PKA regulatory subunit within a multiprotein complex leads to rapid capture of the PKA catalytic subunit limiting signaling duration. Overall, the biochemical data and modeling support the conclusions although a few details can be addressed further and the in vivo data remains preliminary. The work nevertheless presents exciting findings that provide a tantalizing mechanism to selectively modulate PKA activity at precise subcellular locations.

      (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

    This article has 2 evaluationsAppears in 1 listLatest version Latest activity
  7. Mechanism of molnupiravir-induced SARS-CoV-2 mutagenesis

    This article has 8 authors:
    1. Florian Kabinger
    2. Carina Stiller
    3. Jana Schmitzová
    4. Christian Dienemann
    5. Goran Kokic
    6. Hauke S. Hillen
    7. Claudia Höbartner
    8. Patrick Cramer

    Reviewed by ScreenIT

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  8. Nanopore Dwell Time Analysis Permits Sequencing and Conformational Assignment of Pseudouridine in SARS-CoV-2

    This article has 4 authors:
    1. Aaron M. Fleming
    2. Nicole J. Mathewson
    3. Shereen A. Howpay Manage
    4. Cynthia J. Burrows

    Reviewed by ScreenIT

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  9. The method utilized to purify the SARS-CoV-2 N protein can affect its molecular properties

    This article has 6 authors:
    1. Aneta Tarczewska
    2. Marta Kolonko-Adamska
    3. Mirosław Zarębski
    4. Jurek Dobrucki
    5. Andrzej Ożyhar
    6. Beata Greb-Markiewicz

    Reviewed by ScreenIT

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
  10. In-solution buffer-free digestion for the analysis of SARS-CoV-2 RBD proteins allows a full sequence coverage and detection of post-translational modifications in a single ESI-MS spectrum

    This article has 34 authors:
    1. Luis Ariel Espinosa
    2. Yassel Ramos
    3. Ivan Andújar
    4. Enso Onill Torres
    5. Gleysin Cabrera
    6. Alejandro Martín
    7. Diamilé González
    8. Glay Chinea
    9. Mónica Becquet
    10. Isabel González
    11. Camila Canaán-Haden
    12. Elías Nelson
    13. Gertrudis Rojas
    14. Beatriz Pérez-Massón
    15. Dayana Pérez-Martínez
    16. Tamy Boggiano
    17. Julio Palacio
    18. Sum Lai Lozada-Chang
    19. Lourdes Hernández
    20. Kathya Rashida de la Luz Hernández
    21. Saloheimo Markku
    22. Vitikainen Marika
    23. Yury Valdés-Balbín
    24. Darielys Santana-Medero
    25. Daniel G. Rivera
    26. Vicente Vérez-Bencomo
    27. Mark Emalfarb
    28. Ronen Tchelet
    29. Gerardo Guillén
    30. Miladys Limonta
    31. Eulogio Pimentel
    32. Marta Ayala
    33. Vladimir Besada
    34. Luis Javier González

    Reviewed by ScreenIT

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
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