Results 81 to 90 of about 1,786,374 (279)

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

Intrinsically disordered proteins: controlled chaos or random walk

open access: yesInternational Journal of Plant Biology, 2016
Traditional conventions that a protein’s sequence dictates its definitive, tertiary structure, and that this fixed structure provides the protein with the ability to carry out its designated role(s) are still correct but not for all proteins.
T.C. Howton   +3 more
doaj   +1 more source

Single‐cell DNA methylation profiling: Technologies, computation, and applications in precision oncology

open access: yesMolecular Oncology, EarlyView.
Single‐cell DNA methylation (scDNAme) profiling maps epimutational clonal evolution, revealing mechanisms of malignancy and therapeutic resistance across diverse cancer types. By providing a high‐resolution landscape of intratumoral heterogeneity, these technologies empower precise patient stratification, guide the development of enhanced ...
Ik Soo Kim
wiley   +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  

Mechanisms 
of
 change 
in 
protein 
architecture [PDF]

open access: yes, 2011
Proteins are the basic building blocks and functional units in all living organisms. Moreover, differences between species can frequently be explained with differences in their protein complements.

core   +2 more sources

PANoptosis in the pathogenesis of myelodysplastic syndromes

open access: yesMolecular Oncology, EarlyView.
PANoptosis, a combination of three types of programmed cell death, is mediated by a large protein complex called a PANoptosome. In healthy bone marrow hematopoietic cells, PANoptosis is restricted by inhibitory signaling. In MDS, bone marrow cells become sensitive to the PANoptotic stimuli due to the aberrant inactivation of inhibitory signaling or ...
Rohit Thalla   +4 more
wiley   +1 more source

Protein order and disorder: A quantitative in silico analysis [PDF]

open access: yesEPJ Web of Conferences
Proteins are fundamental biological macromolecules responsible for a wide range of cellular functions. Traditionally, a central paradigm linked the amino acid sequence to a unique, ordered three-dimensional structure that underlies biological activity ...
de Brevern Alexandre G.
doaj   +1 more source

New technologies to analyse protein function: an intrinsic disorder perspective [version 1; peer review: 2 approved]

open access: yesF1000Research, 2020
Functions of intrinsically disordered proteins do not require structure. Such structure-independent functionality has melted away the classic rigid “lock and key” representation of structure–function relationships in proteins, opening a new page in ...
Vladimir N. Uversky
doaj   +1 more source

ADP‐ribosylation: An emerging regulator of the epigenome

open access: yesMolecular Oncology, EarlyView.
ADP‐ribosylation has emerged as a dynamic epigenetic signaling mechanism that modifies histones and chromatin‐associated proteins. Through coordinated PARylation and MARylation, it integrates with other histone modifications to regulate chromatin structure, transcription factor activity, and gene expression, influencing genome function and disease ...
Cristel V. Camacho   +2 more
wiley   +1 more source

Self-organization of intrinsically disordered proteins with folded N-termini [PDF]

open access: yes, 2010
Thousands of human proteins lack recognizable tertiary structure in most of their chains. Here we hypothesize that some use their structured N-terminal domains (SNTDs) to organise the remaining protein chain via intramolecular interactions, generating ...
Philip C. Simister   +4 more
core  

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