Results 91 to 100 of about 1,811,289 (287)

Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins

open access: yesFrontiers in Plant Science, 2012
Plant-specific remorin proteins reside in subdomains of plasma membranes, originally termed membrane rafts. They probably facilitate cellular signal transduction by direct interaction with signalling proteins such as receptor-like kinases (RLKs) and may ...
Macarena eMarín, Thomas eOtt
doaj   +1 more source

Intrinsic Disorder and Semi-disorder Prediction by SPINE-D

open access: yes, 2016
Over the past decade, it has become evident that a large proportion of proteins contain intrinsically disordered regions, which play important roles in pivotal cellular functions.
Zhang, Tuo   +7 more
core   +1 more source

Structure‐forward targeting of claudins with synthetic binders

open access: yesFEBS 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

Intrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation

open access: yeseLife, 2013
Anchoring proteins sequester kinases with their substrates to locally disseminate intracellular signals and avert indiscriminate transmission of these responses throughout the cell.
F Donelson Smith   +6 more
doaj   +1 more source

Discerning protein pools by selective staining with self‐labeling tags

open access: yesFEBS Letters, EarlyView.
Cell surface proteins have an intra‐ and extracellular pool. Combining genetic fusion to self‐labeling tags that can be addressed with small molecule fluorophores allows separating these pools. We highlight recent developments and techniques for state‐of‐the‐art interrogation of cell surface proteins in the complex tissue setting.
Kati Fischermanns, Johannes Broichhagen
wiley   +1 more source

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

Common protein sequence signatures associate with Sclerotinia borealis lifestyle and secretion in fungal pathogens of the Sclerotiniaceae

open access: yesFrontiers in Plant Science, 2015
Fungal plant pathogens produce secreted proteins adapted to function outside fungal cells to facilitate colonization of their hosts. In many cases such as for fungi from the Sclerotiniaceae family the repertoire and function of secreted proteins remains ...
Thomas eBadet   +5 more
doaj   +1 more source

Intrinsic disorder in E1B 55K.

open access: yes, 2019
PONDR VLXT, PONDR XL1_XT, PONDR VL3-BA, PONDR VSL2, IUPred and DISOPRED predictors were used for disorder analysis. All predictors indicate a high level of intrinsic disorder in the N- and C-terminus.
Thomas Dobner (181801)   +12 more
core   +1 more source

Epigenetic reprogramming of lineage switching in cancer

open access: yesFEBS Letters, EarlyView.
Cancer cells rarely commit to a single identity. Epigenetic mechanisms and tumor microenvironment cues push epithelial cells toward flexible, hybrid states that can shift into mesenchymal, neuroendocrine, or stem‐like fates, driving metastasis, drug resistance, and tumor heterogeneity. Targeting the epigenetic regulators behind these transitions, using
Ezgi Boyvatlı   +4 more
wiley   +1 more source

Conformational Recognition of an Intrinsically Disordered Protein [PDF]

open access: yesBiophysical Journal, 2014
There is a growing interest in understanding the properties of intrinsically disordered proteins (IDPs); however, the characterization of these states remains an open challenge. IDPs appear to have functional roles that diverge from those of folded proteins and revolve around their ability to act as hubs for protein-protein interactions.
Krieger J. M.   +7 more
openaire   +3 more sources

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