Nature Search

Opening opportunities for K_d determination and screening of MHC peptide complexes

The authors present a sensitive and rapid method to determine the binding strength of MHC class 1 peptide complexes using native mass spectrometry.

Janine-Denise Kopicki
Ankur Saikia
Charlotte Uetrecht
ResearchOpen Access23 May 2022
Communications Biology

Volume: 5, P: 1-11
Seasonal biogeochemical variations in a modern microbialite reef under early Earth-like conditions

Microbial communities, exposed to early Earth-like conditions in a modern microbialite reef, change cyclically due to seasonal environmental variations, implying evolved metabolic processes in microbialites over time, based on multiple chemical, physical, and biological analyses.

Federico A. Vignale
Laura Sánchez-García
María E. Farías
ResearchOpen Access17 Sept 2025
Communications Earth & Environment

Volume: 6, P: 1-19
Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection

Major Histocompatibility Complex (MHC) class I molecules present tightly binding peptides on the cell surface for recognition by cytotoxic T cells. Here, the authors present the crystal structures of a disulfide-stabilized human MHC class I molecule in the peptide-free state and bound with dipeptides, and find that peptide binding is accompanied by concerted conformational switches of the amino acid side chains in the binding pockets.

Raghavendra Anjanappa
Maria Garcia-Alai
Rob Meijers
ResearchOpen Access11 Mar 2020
Nature Communications

Volume: 11, P: 1-11
Epsin and Sla2 form assemblies through phospholipid interfaces

Adapter proteins assist clathrin coated pit assembly. Here, the authors combine native mass spectrometry, crystallography and SAXS measurements and show that the membrane–proximal domains of the adaptor proteins epsin and Sla2 form complexes mediated through phosphatidylinositol 4,5-bisphosphate interfaces leading to assembly formation.

Maria M. Garcia-Alai
Johannes Heidemann
Rob Meijers
ResearchOpen Access23 Jan 2018
Nature Communications

Volume: 9, P: 1-13
A bottom-up approach to find lead compounds in expansive chemical spaces

The vast scale of emerging on-demand chemical collections presents a challenge for efficiently identifying promising drug candidates. Here, the authors develop a bottom-up computational strategy to first explore fragment space and then exploit the most promising scaffolds, successfully identifying diverse and potent BRD4 binders.

Álvaro Serrano-Morrás
Andrea Bertran-Mostazo
Xavier Barril
ResearchOpen Access01 Aug 2025
Communications Chemistry

Volume: 8, P: 1-11
Subtleties in Clathrin heavy chain binding boxes provide selectivity among adaptor proteins of budding yeast

Clathrin helps cells internalize and transport cargo by interacting with membrane adaptor proteins. Here, the authors reveal that adaptor proteins bind selectively, hierarchically and simultaneously to three sites of clathrin’s N-terminal domain.

Lucas A. Defelipe
Katharina Veith
Maria M. García-Alai
ResearchOpen Access07 Nov 2024
Nature Communications

Volume: 15, P: 1-15
Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome

Although new amino acids with desirable properties can be devised, only a few have been successfully introduced into proteins by the cellular machinery. Even then, only one type of unnatural amino acid can be added to a given protein. Here, a new system has been designed that could allow the incorporation of up to 200 novel amino acids. The system involves an orthogonal ribosome that uses quadruplet — rather than triplet — codons, as well as orthogonal tRNA synthetase–tRNA pairs.

Heinz Neumann
Kaihang Wang
Jason W. Chin
Research14 Feb 2010
Nature

Volume: 464, P: 441-444
The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils

In this work the authors provide high-resolution structural support for the amyloid-antimicrobial link via functional amyloids displaying propeller-like and kinked cross-β fibrils.

Robert Bücker
Carolin Seuring
Meytal Landau
ResearchOpen Access27 Jul 2022
Nature Communications

Volume: 13, P: 1-11
Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis

During clathrin-mediated endocytosis in yeast, endocytic coat adaptors, Sla2 and Ent1, must remain attached to the plasma membrane to transmit force from the actin cytoskeleton required for membrane invagination. Here authors present a cryo-EM structure of a 16-mer complex of the ANTH and ENTH membrane-binding domains from Sla2 and Ent1 bound to PIP₂ that constitutes the anchor to the plasma membrane.

Javier Lizarrondo
David P. Klebl
Maria M. Garcia-Alai
ResearchOpen Access17 May 2021
Nature Communications

Volume: 12, P: 1-15
Quality control of protein reagents for the improvement of research data reproducibility

Proteins and peptides are amongst the most widely used research reagents but often their quality is inadequate and can result in poor data reproducibility. Here we propose a simple set of guidelines that, when correctly applied to protein reagents should provide more reliable experimental data.

Ario de Marco
Nick Berrow
Bertrand Raynal
Comments & OpinionOpen Access14 May 2021
Nature Communications

Volume: 12, P: 1-4
High-throughput stability screening for detergent-solubilized membrane proteins

Vadim Kotov
Kim Bartels
Maria M. Garcia-Alai
ResearchOpen Access17 Jul 2019
Scientific Reports

Volume: 9, P: 1-19
FoldAffinity: binding affinities from nDSF experiments

Stephan Niebling
Osvaldo Burastero
María García-Alai
ResearchOpen Access05 May 2021
Scientific Reports

Volume: 11, P: 1-17
Structural deficits in key domains of Shank2 lead to alterations in postsynaptic nanoclusters and to a neurodevelopmental disorder in humans

Fatemeh Hassani Nia
Daniel Woike
Hans-Jürgen Kreienkamp
ResearchOpen Access30 Nov 2022
Molecular Psychiatry

Volume: 29, P: 1683-1697
Antiviral activity of natural phenolic compounds in complex at an allosteric site of SARS-CoV-2 papain-like protease

Three natural phenolic compounds are found to bind to an allosteric site in SARS-CoV-2 papain-like protease and exhibit antiviral activity in vitro, showing potential as starting scaffolds for drug design.

Vasundara Srinivasan
Hévila Brognaro
Christian Betzel
ResearchOpen Access11 Aug 2022
Communications Biology

Volume: 5, P: 1-12

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