Results 131 to 140 of about 2,121,701 (315)

Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes

open access: yeseLife, 2017
The yeast Chd1 protein acts to position nucleosomes across genomes. Here, we model the structure of the Chd1 protein in solution and when bound to nucleosomes.
Ramasubramanian Sundaramoorthy   +14 more
doaj   +1 more source

The role of miR‐335‐5p in the redifferentiation of BRAF p.V600E thyroid cancers

open access: yesMolecular Oncology, EarlyView.
The BRAF p.V600E mutation promotes thyroid cancer dedifferentiation and radioiodine resistance. Using a network approach, we identified miR‐335‐5p as a key regulator of BRAF‐mutated thyroid tumors. Restoring miR‐335‐5p increased thyroid‐specific gene expression and iodine uptake in cells and organoids.
Valeria Pecce   +11 more
wiley   +1 more source

Stability and dynamics of extradenticle modulates its function

open access: yesCurrent Research in Structural Biology
Extradenticle (EXD) is a partner protein of the HOX transcription factors and plays an important role in the development of Drosophila. It confers increased affinity and specificity of DNA-binding to the HOX proteins. However, the DNA-binding homeodomain
Aakanksha Singh   +6 more
doaj   +1 more source

TRAIL‐PEG‐Apt‐PLGA nanosystem as an aptamer‐targeted drug delivery system potential for triple‐negative breast cancer therapy using in vivo mouse model

open access: yesMolecular Oncology, EarlyView.
Aptamers are used both therapeutically and as targeting agents in cancer treatment. We developed an aptamer‐targeted PLGA–TRAIL nanosystem that exhibited superior therapeutic efficacy in NOD/SCID breast cancer models. This nanosystem represents a novel biotechnological drug candidate for suppressing resistance development in breast cancer.
Gulen Melike Demirbolat   +8 more
wiley   +1 more source

The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains [PDF]

open access: yes, 2011
The ATP-dependent chromatin-remodelling enzyme Chd1 is a 168-kDa protein consisting of a double chromodomain, Snf2-related ATPase domain, and a C-terminal DNA-binding domain.
Daniel P Ryan   +9 more
core   +1 more source

Fluorescent microplate-based analysis of protein-DNA interactions II: immobilized DNA

open access: yesBioTechniques, 2003
A simple protein-DNA interaction analysis has been developed using both a high-affinity/high-specificity zinc finger protein and a low-specificity zinc finger protein with nonspecific DNA binding capability.
Zhan-Ren Zhang   +4 more
doaj   +1 more source

Tumour–host interactions in Drosophila: mechanisms in the tumour micro‐ and macroenvironment

open access: yesMolecular Oncology, EarlyView.
This review examines how tumour–host crosstalk takes place at multiple levels of biological organisation, from local cell competition and immune crosstalk to organism‐wide metabolic and physiological collapse. Here, we integrate findings from Drosophila melanogaster studies that reveal conserved mechanisms through which tumours hijack host systems to ...
José Teles‐Reis, Tor Erik Rusten
wiley   +1 more source

Nucleic acid - protein fingerprints. Novel protein classification based on nucleic acid - protein recognition

open access: yes, 2012
Protein chemistry uses protein description and classification based on molecular mass and isoelectric point as general features. Enzymes are also compared by enzymatic reaction constants, namely Km and kcat values. Proteins are also studied by binding to
Renad Zhdanov, Alexander Krylov
core  

Recent advances in the structural molecular biology of Ets transcription factors: interactions, interfaces and inhibition.

open access: yes, 2014
The Ets family of eukaryotic transcription factors is based around the conserved Ets DNA-binding domain. Although their DNA-binding selectivity is biochemically and structurally well characterized, structures of homodimeric and ternary complexes point to
Gileadi, Opher   +8 more
core   +1 more source

Variable structure motifs for transcription factor binding sites [PDF]

open access: yes, 2010
Background: Classically, models of DNA-transcription factor binding sites (TFBSs) have been based on relatively few known instances and have treated them as sites of fixed length using position weight matrices (PWMs).
Evans, Kenneth J.   +17 more
core   +1 more source

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