Results 81 to 90 of about 7,902,914 (332)

Association/dissociation Mechanisms of Intrinsically Disordered Region of Protein Beyond Conformational Selection and Induced Fit [PDF]

open access: yes, 2019
We investigate association and dissociation mechanisms of a typical intrinsically disordered region (IDR), transcriptional activation subdomain of tumor repressor protein p53 (TAD-p53) with murine double-minute clone 2 protein (MDM2).
Duy Phuoc Tran (7400249)   +3 more
core   +1 more source

Intrinsic disorder and protein multibinding in domain, terminal, and linker regions [PDF]

open access: yesMolecular BioSystems, 2010
Abstract Intrinsic disorder is believed to contribute to the ability of some proteins to interact with multiple partners which is important for protein functional promiscuity and regulation of the cross-talk between pathways.
Jessica H, Fong, Anna R, Panchenko
openaire   +2 more sources

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

open access: yesFEBS 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   +2 more
wiley   +1 more source

Disease association and comparative genomics of compositional bias in human proteins [version 2; peer review: 2 approved]

open access: yesF1000Research, 2023
Background: The evolutionary rate of disordered protein regions varies greatly due to the lack of structural constraints. So far, few studies have investigated the presence/absence patterns of compositional bias, indicative of disorder, across ...
Christos A. Ouzounis   +3 more
doaj   +1 more source

Unequivocal Single-Molecule Force Spectroscopy of Intrinsically Disordered Proteins [PDF]

open access: yes, 2012
Intrinsically disordered proteins (IDPs) are predicted to represent about one third of the eukaryotic proteome. The dynamic ensemble of conformations of this steadily growing class of proteins has remained hardly accessible for bulk biophysical ...
Rubén Hervás   +12 more
core   +1 more source

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

open access: yesFEBS 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   +2 more
wiley   +1 more source

The Disordered C-Terminus of the Chaperone DnaK Increases the Competitive Fitness of Pseudomonas putida and Facilitates the Toxicity of GraT

open access: yesMicroorganisms, 2021
Chaperone proteins are crucial for proper protein folding and quality control, especially when cells encounter stress caused by non-optimal temperatures. DnaK is one of such essential chaperones in bacteria. Although DnaK has been well characterized, the
Sirli Rosendahl   +2 more
doaj   +1 more source

Proteomimetic Strategy for the Modulation of Intrinsically Disordered Protein MYC

open access: yesJournal of the American Chemical Society
The difficulty in developing specific ligands for protein receptors is directly correlated to the presence of unique binding sites on the protein surface.
Thu Nguyen, Seong Ho Hong, P. Arora
semanticscholar   +1 more source

Empirical predictions of an intrinsically disordered protein theory approach to glycan/lectin reaction kinetics [PDF]

open access: yes, 2012
Newly-developed methods from the theory of intrinsically disordered proteins can be applied to the flexible glycan structures that coat cellular surfaces and provide rich channels for biological information transmission.
Rodrick Wallace
core  

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

open access: yesFEBS 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   +5 more
wiley   +1 more source

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