Results 61 to 70 of about 148,826 (294)

Hybrids of the bHLH and bZIP protein motifs display different DNA-binding activities in vivo vs. in vitro.

open access: yesPLoS ONE, 2008
Minimalist hybrids comprising the DNA-binding domain of bHLH/PAS (basic-helix-loop-helix/Per-Arnt-Sim) protein Arnt fused to the leucine zipper (LZ) dimerization domain from bZIP (basic region-leucine zipper) protein C/EBP were designed to bind the E-box
Hiu-Kwan Chow   +5 more
doaj   +1 more source

Computational modeling of the bHLH domain of the transcription factor TWIST1 and R118C, S144R and K145E mutants

open access: yesBMC Bioinformatics, 2012
Background Human TWIST1 is a highly conserved member of the regulatory basic helix-loop-helix (bHLH) transcription factors. TWIST1 forms homo- or heterodimers with E-box proteins, such as E2A (isoforms E12 and E47), MYOD and HAND2.
Maia Amanda M   +4 more
doaj   +1 more source

MITF and TFEB cross-regulation in melanoma cells.

open access: yesPLoS ONE, 2020
The MITF, TFEB, TFE3 and TFEC (MiT-TFE) proteins belong to the basic helix-loop-helix family of leucine zipper transcription factors. MITF is crucial for melanocyte development and differentiation, and has been termed a lineage-specific oncogene in ...
Josué Ballesteros-Álvarez   +7 more
doaj   +1 more source

Basic helix-loop-helix proteins in murine type C retrovirus transcriptional regulation [PDF]

open access: yesJournal of Virology, 1994
E boxes, recognition sequences for basic helix-loop-helix (bHLH) transcription factors, are detected in the enhancer and promoter regions of several murine type C retroviruses. Here we show that ALF1, a member of bHLH protein family of transcription factors, in vitro binds with differing affinities to distinct E-box sequences found in the U3 regulatory
Nielsen, Anders Lade; id_orcid 0000-0003-4372-9961   +3 more
openaire   +3 more sources

A methionine‐lined active site governs carbocation stabilization and product specificity in a bacterial terpene synthase

open access: yesFEBS Letters, EarlyView.
This study reveals a unique active site enriched in methionine residues and demonstrates that these residues play a critical role by stabilizing carbocation intermediates through novel sulfur–cation interactions. Structure‐guided mutagenesis further revealed variants with significantly altered product profiles, enhancing pseudopterosin formation. These
Marion Ringel   +13 more
wiley   +1 more source

Phosphopeptide mapping of proteins ectopically expressed in tissue culture cell lines

open access: yesBiological Procedures Online, 2004
Post-translational modifications such as phosphorylation play a vital role in the regulation of protein function. In our study of the basic Helix-loop-Helix (bHLH) transcription factor HAND1, it was suspected that HAND1 was being phosphorylated during ...
Firulli Beth A.   +2 more
doaj   +1 more source

Molecular Dynamics Studies on 3D Structures of the Hydrophobic Region PrP(109-136) [PDF]

open access: yes, 2013
Prion diseases caused by the conversion from a soluble normal cellular prion protein into insoluble abnormally folded infectious prions, are invariably fatal and highly infectious degenerative diseases that affect a wide variety of mammalian species. The
Zhang, Jiapu, Zhang, Yuanli
core   +4 more sources

AAA+ protein unfoldases—the Moirai of the proteome

open access: yesFEBS Letters, EarlyView.
AAA+ unfoldases are essential molecular motors that power protein degradation and disaggregation. This review integrates recent cryo‐electron microscopy (cryo‐EM) structures and single‐molecule biophysical data to reconcile competing models of substrate translocation.
Stavros Azinas, Marta Carroni
wiley   +1 more source

Genome-wide identification and characterisation of bHLH transcription factors in Artemisia annua

open access: yesBMC Plant Biology, 2023
Background A. annua (also named Artemisia annua, sweet wormwood) is the main source of the anti-malarial drug artemisinin, which is synthesised and stored in its trichomes. Members of the basic Helix-Loop-Helix (bHLH) family of transcription factors (TFs)
Shuwei Chang   +4 more
doaj   +1 more source

Membrane interactions of S100A12 (Calgranulin C) [PDF]

open access: yes, 2013
S100A12 (Calgranulin C) is a small acidic calcium-binding peripheral membrane protein with two EF-hand structural motifs. It is expressed in macrophages and lymphocytes and highly up-regulated in several human inflammatory diseases.
Araujo, A.P.U.   +5 more
core   +1 more source

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