Results 61 to 70 of about 29,414 (258)

Structure‐forward targeting of claudins with synthetic binders

FEBS Letters, EarlyView.
Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley   +1 more source

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

FEBS Letters, EarlyView.
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang, Ruslana Romaniuk, Hristo L. Svilenov   +2 more
wiley   +1 more source

Interactions by Disorder – A Matter of Context

Frontiers in Molecular Biosciences, 2020
Living organisms depend on timely and organized interactions between proteins linked in interactomes of high complexity. The recent increased precision by which protein interactions can be studied, and the enclosure of intrinsic structural disorder ...
Katrine Bugge, Katrine Bugge, Inna Brakti, Inna Brakti, Catarina B. Fernandes, Catarina B. Fernandes, Jesper E. Dreier, Jesper E. Dreier, Jeppe E. Lundsgaard, Jeppe E. Lundsgaard, Johan G. Olsen, Johan G. Olsen, Karen Skriver, Birthe B. Kragelund, Birthe B. Kragelund   +14 more
doaj   +1 more source

Protein intrinsically disordered region prediction by combining neural architecture search and multi-objective genetic algorithm

BMC Biology, 2023
Background Intrinsically disordered regions (IDRs) are widely distributed in proteins and related to many important biological functions. Accurately identifying IDRs is of great significance for protein structure and function analysis.
Yi-Jun Tang, Ke Yan, Xingyi Zhang, Ye Tian, Bin Liu   +4 more
doaj   +1 more source

Emerging experimental and computational methods for studying redox‐regulated structural transitions

FEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass, Dana Reichmann, Gábor Erdős   +2 more
wiley   +1 more source

The heterodimeric amino acid transporters (HAT) of the SLC7/SLC3 family: A structure−function relationships and relevance to human pathology

FEBS Letters, EarlyView.
Heterodimeric amino acid transporters consist of SLC7 and SLC3 family proteins arranged in a conserved structural organization. They regulate nutrient transport across cell membranes, supporting essential cellular functions. These transporters also contribute to xenobiotic/drug uptake and distribution.
Mariafrancesca Scalise, Tiziano Mazza, Raffaella Scanga, Lara Console, Michele Galluccio, Cesare Indiveri   +5 more
wiley   +1 more source

An assignment of intrinsically disordered regions of proteins based on NMR structures [PDF]

Journal of Structural Biology, 2013
Intrinsically disordered proteins (IDPs) do not adopt stable three-dimensional structures in physiological conditions, yet these proteins play crucial roles in biological phenomena. In most cases, intrinsic disorder manifests itself in segments or domains of an IDP, called intrinsically disordered regions (IDRs), but fully disordered IDPs also exist ...
Motonori, Ota, Ryotaro, Koike, Takayuki, Amemiya, Takeshi, Tenno, Pedro R, Romero, Hidekazu, Hiroaki, A Keith, Dunker, Satoshi, Fukuchi   +7 more
openaire   +2 more sources

CARs-DB: A Database of Cryptic Amyloidogenic Regions in Intrinsically Disordered Proteins

Frontiers in Molecular Biosciences, 2022
Proteome-wide analyses suggest that most globular proteins contain at least one amyloidogenic region, whereas these aggregation-prone segments are thought to be underrepresented in intrinsically disordered proteins (IDPs). In recent work, we reported that intrinsically disordered regions (IDRs) indeed sustain a significant amyloid load in the form of ...
Pintado-Grima, Carlos, Bárcenas, Oriol, Manglano-Artuñedo, Zoe, Vilaça, Rita, Macedo-Ribeiro, Sandra, Pallarès, Irantzu, Santos, Jaime, Ventura, Salvador   +7 more
openaire   +4 more sources

Smaller is better: nanobodies meet NMR

FEBS Letters, EarlyView.
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley   +1 more source

The ‘Shape-Shifter’ Peptide from the Disulphide Isomerase PmScsC Shows Context-Dependent Conformational Preferences

Biomolecules, 2021
Multiple crystal structures of the homo-trimeric protein disulphide isomerase PmScsC reveal that the peptide which links the trimerization stalk and catalytic domain can adopt helical, β-strand and loop conformations. This region has been called a ‘shape-
Lorna J. Smith, Chloe W. Green, Christina Redfield   +2 more
doaj   +1 more source