Log in

Relevant bibliographies by topics / BHLH-PAS proteins / Journal articles

To see the other types of publications on this topic, follow the link: BHLH-PAS proteins.

Journal articles on the topic 'BHLH-PAS proteins'

Author: Grafiati

Published: 25 May 2024

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'BHLH-PAS proteins.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Bersten, David C., Adrienne E. Sullivan, Daniel J. Peet, and Murray L. Whitelaw. "bHLH–PAS proteins in cancer." Nature Reviews Cancer 13, no. 12 (2013): 827–41. http://dx.doi.org/10.1038/nrc3621.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Kolonko, Marta, and Beata Greb-Markiewicz. "bHLH–PAS Proteins: Their Structure and Intrinsic Disorder." International Journal of Molecular Sciences 20, no. 15 (2019): 3653. http://dx.doi.org/10.3390/ijms20153653.

Full text

Abstract:

The basic helix–loop–helix/Per-ARNT-SIM (bHLH–PAS) proteins are a class of transcriptional regulators, commonly occurring in living organisms and highly conserved among vertebrates and invertebrates. These proteins exhibit a relatively well-conserved domain structure: the bHLH domain located at the N-terminus, followed by PAS-A and PAS-B domains. In contrast, their C-terminal fragments present significant variability in their primary structure and are unique for individual proteins. C-termini were shown to be responsible for the specific modulation of protein action. In this review, we present

APA, Harvard, Vancouver, ISO, and other styles

3

Crews, Stephen T., and Chen-Ming Fan. "Remembrance of things PAS: regulation of development by bHLH–PAS proteins." Current Opinion in Genetics & Development 9, no. 5 (1999): 580–87. http://dx.doi.org/10.1016/s0959-437x(99)00003-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Reisz-Porszasz, S., M. R. Probst, B. N. Fukunaga, and O. Hankinson. "Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)." Molecular and Cellular Biology 14, no. 9 (1994): 6075–86. http://dx.doi.org/10.1128/mcb.14.9.6075-6086.1994.

Full text

Abstract:

The activated aryl hydrocarbon receptor (AHR) and the AHR nuclear translocator (ARNT) bind DNA as a heterodimer. Both proteins represent a novel class of basic helix-loop-helix (bHLH)-containing transcription factors in that (i) activation of AHR requires the binding of ligand (e.g., 2,3,7,8-tetrachlorodibenzo-p-dioxin [TCDD]), (ii) the xenobiotic responsive element (XRE) recognized by the AHR/ARNT heterodimer differs from the recognition sequence for nearly all other bHLH proteins, and (iii) both proteins contain a PAS homology region, which in the Drosophila PER and SIM proteins functions as

APA, Harvard, Vancouver, ISO, and other styles

5

Reisz-Porszasz, S., M. R. Probst, B. N. Fukunaga, and O. Hankinson. "Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)." Molecular and Cellular Biology 14, no. 9 (1994): 6075–86. http://dx.doi.org/10.1128/mcb.14.9.6075.

Full text

Abstract:

The activated aryl hydrocarbon receptor (AHR) and the AHR nuclear translocator (ARNT) bind DNA as a heterodimer. Both proteins represent a novel class of basic helix-loop-helix (bHLH)-containing transcription factors in that (i) activation of AHR requires the binding of ligand (e.g., 2,3,7,8-tetrachlorodibenzo-p-dioxin [TCDD]), (ii) the xenobiotic responsive element (XRE) recognized by the AHR/ARNT heterodimer differs from the recognition sequence for nearly all other bHLH proteins, and (iii) both proteins contain a PAS homology region, which in the Drosophila PER and SIM proteins functions as

APA, Harvard, Vancouver, ISO, and other styles

6

Greb-Markiewicz, Beata, and Marta Kolonko. "Subcellular Localization Signals of bHLH-PAS Proteins: Their Significance, Current State of Knowledge and Future Perspectives." International Journal of Molecular Sciences 20, no. 19 (2019): 4746. http://dx.doi.org/10.3390/ijms20194746.

Full text

Abstract:

The bHLH-PAS (basic helix-loop-helix/ Period-ARNT-Single minded) proteins are a family of transcriptional regulators commonly occurring in living organisms. bHLH-PAS members act as intracellular and extracellular “signals” sensors, initiating response to endo- and exogenous signals, including toxins, redox potential, and light. The activity of these proteins as transcription factors depends on nucleocytoplasmic shuttling: the signal received in the cytoplasm has to be transduced, via translocation, to the nucleus. It leads to the activation of transcription of particular genes and determines t

APA, Harvard, Vancouver, ISO, and other styles

7

Gilles-Gonzalez, Marie-Alda, and Gonzalo Gonzalez. "Signal transduction by heme-containing PAS-domain proteins." Journal of Applied Physiology 96, no. 2 (2004): 774–83. http://dx.doi.org/10.1152/japplphysiol.00941.2003.

Full text

Abstract:

The most common physiological strategy for detecting the gases oxygen, carbon monoxide, and nitric oxide is signal transduction by heme-based sensors, a broad class of modular proteins in which a heme-binding domain governs the activity of a neighboring transmitter domain. Different structures are possible for the heme-binding domains in these sensors, but, so far, the Per-ARNT-Sim motif, or PAS domain, is the one most commonly encountered. Heme-binding PAS (heme-PAS) domains can accomplish ligand-dependent switching of a variety of partner domains, including histidine kinase, phosphodiesteras

APA, Harvard, Vancouver, ISO, and other styles

8

Kolonko-Adamska, Marta, Vladimir N. Uversky, and Beata Greb-Markiewicz. "The Participation of the Intrinsically Disordered Regions of the bHLH-PAS Transcription Factors in Disease Development." International Journal of Molecular Sciences 22, no. 6 (2021): 2868. http://dx.doi.org/10.3390/ijms22062868.

Full text

Abstract:

The basic helix–loop–helix/Per-ARNT-SIM (bHLH-PAS) proteins are a family of transcription factors regulating expression of a wide range of genes involved in different functions, ranging from differentiation and development control by oxygen and toxins sensing to circadian clock setting. In addition to the well-preserved DNA-binding bHLH and PAS domains, bHLH-PAS proteins contain long intrinsically disordered C-terminal regions, responsible for regulation of their activity. Our aim was to analyze the potential connection between disordered regions of the bHLH-PAS transcription factors, post-tra

APA, Harvard, Vancouver, ISO, and other styles

9

Zelzer, E., P. Wappner, and B. Z. Shilo. "The PAS domain confers target gene specificity of Drosophila bHLH/PAS proteins." Genes & Development 11, no. 16 (1997): 2079–89. http://dx.doi.org/10.1101/gad.11.16.2079.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Aitola, Marjo H., and Markku T. Pelto-Huikko. "Expression of Arnt and Arnt2 mRNA in Developing Murine Tissues." Journal of Histochemistry & Cytochemistry 51, no. 1 (2003): 41–54. http://dx.doi.org/10.1177/002215540305100106.

Full text

Abstract:

The basic helix-loop-helix (bHLH-PAS) proteins aryl hydrocarbon receptor nuclear translocator (Arnt) and Arnt2 are transcriptional regulators that function as dimerizing partners for several bHLH-PAS proteins and also some nonrelated partners. They are involved in various biological functions, including regulation of developmental genes. In earlier studies, the developmental expression of Arnt was reported to be almost ubiquitous, whereas Arnt2 expression has been shown to be more limited, comprising neuronal tissues as the main site of expression. Here we provide a detailed description of the

APA, Harvard, Vancouver, ISO, and other styles

11

LI, YUMIN, YUCAI WEI, JIWU GUO, YUSHENG CHENG, and WENTING HE. "Interactional role of microRNAs and bHLH-PAS proteins in cancer (Review)." International Journal of Oncology 47, no. 1 (2015): 25–34. http://dx.doi.org/10.3892/ijo.2015.3007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Antonsson, C., M. L. Whitelaw, J. McGuire, J. A. Gustafsson, and L. Poellinger. "Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains." Molecular and Cellular Biology 15, no. 2 (1995): 756–65. http://dx.doi.org/10.1128/mcb.15.2.756.

Full text

Abstract:

The intracellular dioxin receptor mediates signal transduction by dioxin and functions as a ligand-activated transcription factor. It contains a basic helix-loop-helix (bHLH) motif contiguous with a Per-Arnt-Sim (PAS) homology region. In extracts from nonstimulated cells the receptor is recovered in an inducible cytoplasmic form associated with the 90-kDa heat shock protein (hsp90), a molecular chaperone. We have reconstituted ligand-dependent activation of the receptor to a DNA-binding form by using the dioxin receptor and its bHLH-PAS partner factor Arnt expressed by in vitro translation in

APA, Harvard, Vancouver, ISO, and other styles

13

Michael, Alicia K., Jennifer L. Fribourgh, Yogarany Chelliah, et al. "Formation of a repressive complex in the mammalian circadian clock is mediated by the secondary pocket of CRY1." Proceedings of the National Academy of Sciences 114, no. 7 (2017): 1560–65. http://dx.doi.org/10.1073/pnas.1615310114.

Full text

Abstract:

The basic helix–loop–helix PAS domain (bHLH-PAS) transcription factor CLOCK:BMAL1 (brain and muscle Arnt-like protein 1) sits at the core of the mammalian circadian transcription/translation feedback loop. Precise control of CLOCK:BMAL1 activity by coactivators and repressors establishes the ∼24-h periodicity of gene expression. Formation of a repressive complex, defined by the core clock proteins cryptochrome 1 (CRY1):CLOCK:BMAL1, plays an important role controlling the switch from repression to activation each day. Here we show that CRY1 binds directly to the PAS domain core of CLOCK:BMAL1,

APA, Harvard, Vancouver, ISO, and other styles

14

Li, M., E. A. Mead, and J. Zhu. "Heterodimer of two bHLH-PAS proteins mediates juvenile hormone-induced gene expression." Proceedings of the National Academy of Sciences 108, no. 2 (2010): 638–43. http://dx.doi.org/10.1073/pnas.1013914108.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Crews, S. T. "Control of cell lineage-specific development and transcription by bHLH-PAS proteins." Genes & Development 12, no. 5 (1998): 607–20. http://dx.doi.org/10.1101/gad.12.5.607.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Godlewski, Jakub, Shaoli Wang, and Thomas G. Wilson. "Interaction of bHLH-PAS proteins involved in juvenile hormone reception in Drosophila." Biochemical and Biophysical Research Communications 342, no. 4 (2006): 1305–11. http://dx.doi.org/10.1016/j.bbrc.2006.02.097.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Choi, Yoon-Jeong, Eun-Jeong Kwon, Joung-Sun Park, Ho-Sung Kang, Young-Shin Kim, and Mi-Ae Yoo. "Transcriptional regulation of the Drosophila caudal homeobox gene by bHLH–PAS proteins." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1769, no. 1 (2007): 41–48. http://dx.doi.org/10.1016/j.bbaexp.2006.11.008.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Jiang, Lan, and Stephen T. Crews. "The Drosophila dysfusion Basic Helix-Loop-Helix (bHLH)-PAS Gene Controls Tracheal Fusion and Levels of the Trachealess bHLH-PAS Protein." Molecular and Cellular Biology 23, no. 16 (2003): 5625–37. http://dx.doi.org/10.1128/mcb.23.16.5625-5637.2003.

Full text

Abstract:

ABSTRACT The development of the mature insect trachea requires a complex series of cellular events, including tracheal cell specification, cell migration, tubule branching, and tubule fusion. Here we describe the identification of the Drosophila melanogaster dysfusion gene, which encodes a novel basic helix-loop-helix (bHLH)-PAS protein conserved between Caenorhabditis elegans, insects, and humans, and controls tracheal fusion events. The Dysfusion protein functions as a heterodimer with the Tango bHLH-PAS protein in vivo to form a putative DNA-binding complex. The dysfusion gene is expressed

APA, Harvard, Vancouver, ISO, and other styles

19

Romero, Nuria M., Maximiliano Irisarri, Peggy Roth, Ana Cauerhff, Christos Samakovlis та Pablo Wappner. "Regulation of the Drosophila Hypoxia-Inducible Factor α Sima by CRM1-Dependent Nuclear Export". Molecular and Cellular Biology 28, № 10 (2008): 3410–23. http://dx.doi.org/10.1128/mcb.01027-07.

Full text

Abstract:

ABSTRACT Hypoxia-inducible factor α (HIF-α) proteins are regulated by oxygen levels through several different mechanisms that include protein stability, transcriptional coactivator recruitment, and subcellular localization. It was previously reported that these transcription factors are mainly nuclear in hypoxia and cytoplasmic in normoxia, but so far the molecular basis of this regulation is unclear. We show here that the Drosophila melanogaster HIF-α protein Sima shuttles continuously between the nucleus and the cytoplasm. We identified the relevant nuclear localization signal and two functi

APA, Harvard, Vancouver, ISO, and other styles

20

Epstein, D. J., L. Martinu, J. L. Michaud, K. M. Losos, C. Fan, and A. L. Joyner. "Members of the bHLH-PAS family regulate Shh transcription in forebrain regions of the mouse CNS." Development 127, no. 21 (2000): 4701–9. http://dx.doi.org/10.1242/dev.127.21.4701.

Full text

Abstract:

The secreted protein sonic hedgehog (Shh) is required to establish patterns of cellular growth and differentiation within ventral regions of the developing CNS. The expression of Shh in the two tissue sources responsible for this activity, the axial mesoderm and the ventral midline of the neural tube, is regulated along the anteroposterior neuraxis. Separate cis-acting regulatory sequences have been identified which direct Shh expression to distinct regions of the neural tube, supporting the view that multiple genes are involved in activating Shh transcription along the length of the CNS. We s

APA, Harvard, Vancouver, ISO, and other styles

21

Hirose, K., M. Morita, M. Ema, et al. "cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS factor (Arnt2) with close sequence similarity to the aryl hydrocarbon receptor nuclear translocator (Arnt)." Molecular and Cellular Biology 16, no. 4 (1996): 1706–13. http://dx.doi.org/10.1128/mcb.16.4.1706.

Full text

Abstract:

We isolated mouse cDNA clones (Arnt2) that are highly similar to but distinct from the aryl hydrocarbon receptor (AhR) nuclear translocator (Arnt). The composite cDNA covered a 2,443-bp sequence consisting of a putative 2,136-bp open reading frame encoding a polypeptide of 712 amino acids. The predicted Arnt2 polypeptide carries a characteristic basic helix-loop-helix (bHLH)/PAS motif in its N-terminal region with close similarity (81% identity) to that of mouse Arnt and has an overall sequence identity of 57% with Arnt. Biochemical properties and interaction of Arnt2 with other bHLH/PAS prote

APA, Harvard, Vancouver, ISO, and other styles

22

Button, Emily L., David C. Bersten, and Murray L. Whitelaw. "HIF has Biff – Crosstalk between HIF1a and the family of bHLH/PAS proteins." Experimental Cell Research 356, no. 2 (2017): 141–45. http://dx.doi.org/10.1016/j.yexcr.2017.03.055.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Kinoshita, K. "Altered DNA binding specificity of Arnt by selection of partner bHLH-PAS proteins." Nucleic Acids Research 32, no. 10 (2004): 3169–79. http://dx.doi.org/10.1093/nar/gkh637.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Wiesener, M. S., H. Turley, W. E. Allen та ін. "Induction of Endothelial PAS Domain Protein-1 by Hypoxia: Characterization and Comparison With Hypoxia-Inducible Factor-1α". Blood 92, № 7 (1998): 2260–68. http://dx.doi.org/10.1182/blood.v92.7.2260.

Full text

Abstract:

Abstract Hypoxia results in adaptive changes in the transcription of a range of genes including erythropoietin. An important mediator is hypoxia-inducible factor-1 (HIF-1), a DNA binding complex shown to contain at least two basic helix-loop-helix PAS-domain (bHLH-PAS) proteins, HIF-1α and aryl hydrocarbon nuclear receptor translocator (ARNT). In response to hypoxia, HIF-1α is activated and accumulates rapidly in the cell. Endothelial PAS domain protein 1 (EPAS-1) is a recently identified bHLH-PAS protein with 48% identity to HIF-1α, raising the question of its role in responses to hypoxia. We

APA, Harvard, Vancouver, ISO, and other styles

25

Wiesener, M. S., H. Turley, W. E. Allen та ін. "Induction of Endothelial PAS Domain Protein-1 by Hypoxia: Characterization and Comparison With Hypoxia-Inducible Factor-1α". Blood 92, № 7 (1998): 2260–68. http://dx.doi.org/10.1182/blood.v92.7.2260.2260_2260_2268.

Full text

Abstract:

Hypoxia results in adaptive changes in the transcription of a range of genes including erythropoietin. An important mediator is hypoxia-inducible factor-1 (HIF-1), a DNA binding complex shown to contain at least two basic helix-loop-helix PAS-domain (bHLH-PAS) proteins, HIF-1α and aryl hydrocarbon nuclear receptor translocator (ARNT). In response to hypoxia, HIF-1α is activated and accumulates rapidly in the cell. Endothelial PAS domain protein 1 (EPAS-1) is a recently identified bHLH-PAS protein with 48% identity to HIF-1α, raising the question of its role in responses to hypoxia. We develope

APA, Harvard, Vancouver, ISO, and other styles

26

Gradin, K., J. McGuire, R. H. Wenger, et al. "Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor." Molecular and Cellular Biology 16, no. 10 (1996): 5221–31. http://dx.doi.org/10.1128/mcb.16.10.5221.

Full text

Abstract:

Hypoxia-inducible factor 1 alpha (HIF-1 alpha) and the intracellular dioxin receptor mediate hypoxia and dioxin signalling, respectively. Both proteins are conditionally regulated basic helix-loop-helix (bHLH) transcription factors that, in addition to the bHLH motif, share a Per-Arnt-Sim (PAS) region of homology and form heterodimeric complexes with the common bHLH/PAS partner factor Arnt. Here we demonstrate that HIF-1 alpha required Arnt for DNA binding in vitro and functional activity in vivo. Both the bHLH and PAS motifs of Arnt were critical for dimerization with HIF-1 alpha. Strikingly,

APA, Harvard, Vancouver, ISO, and other styles

27

Ward, M. P., J. T. Mosher, and S. T. Crews. "Regulation of bHLH-PAS protein subcellular localization during Drosophila embryogenesis." Development 125, no. 9 (1998): 1599–608. http://dx.doi.org/10.1242/dev.125.9.1599.

Full text

Abstract:

The Drosophila Single-minded and Tango basic-helix-loop-helix-PAS protein heterodimer controls transcription and embryonic development of the CNS midline cells, while the Trachealess and Tango heterodimer controls tracheal cell and salivary duct transcription and development. Expression of both single-minded and trachealess is highly restricted to their respective cell lineages, however tango is broadly expressed. The developmental control of subcellular localization of these proteins is investigated because of their similarity to the mammalian basic-helix-loop-helix-PAS Aromatic hydrocarbon r

APA, Harvard, Vancouver, ISO, and other styles

28

Kim, Seon-Hee, Gyu-Seok Oh, Woon-Mok Sohn, Kihyun Lee, Hyun-Jong Yang та Young-An Bae. "Molecular characteristics and induction profiles of hypoxia-inducible factor-1αand other basic helix–loop–helix and Per–Arnt–Sim domain-containing proteins identified in a carcinogenic liver flukeClonorchis sinensis". Parasitology 146, № 2 (2018): 176–86. http://dx.doi.org/10.1017/s0031182018001245.

Full text

Abstract:

AbstractClonorchis sinensis(C. sinensis), a trematode parasite that invades the hypoxic hepatobiliary tract of vertebrate hosts requires a considerable amount of oxygen for its sexual reproduction and energy metabolism. However, little is known regarding the molecular mechanism ofC. sinensisinvolved in the adaptation to the hypoxic environments. In this study, we investigated the molecular structures and induction patterns of hypoxia-inducible factor-1α(HIF-1α) and other basic helix–loop–helix and Per–Arnt–Sim (bHLH–PAS) domain-containing proteins such as HIF-1β, single-minded protein and aryl

APA, Harvard, Vancouver, ISO, and other styles

29

Chang, Wai Hoong, and Alvina G. Lai. "Genome-wide analyses of the bHLH superfamily in crustaceans: reappraisal of higher-order groupings and evidence for lineage-specific duplications." Royal Society Open Science 5, no. 3 (2018): 172433. http://dx.doi.org/10.1098/rsos.172433.

Full text

Abstract:

The basic helix-loop-helix (bHLH) proteins represent a key group of transcription factors implicated in numerous eukaryotic developmental and signal transduction processes. Characterization of bHLHs from model species such as humans, fruit flies, nematodes and plants have yielded important information on their functions and evolutionary origin. However, relatively little is known about bHLHs in non-model organisms despite the availability of a vast number of high-throughput sequencing datasets, enabling previously intractable genome-wide and cross-species analyses to be now performed. We exten

APA, Harvard, Vancouver, ISO, and other styles

30

Coban, Mathew A., Patrick R. Blackburn, Murray L. Whitelaw, Mieke M. van Haelst, Paldeep S. Atwal, and Thomas R. Caulfield. "Structural Models for the Dynamic Effects of Loss-of-Function Variants in the Human SIM1 Protein Transcriptional Activation Domain." Biomolecules 10, no. 9 (2020): 1314. http://dx.doi.org/10.3390/biom10091314.

Full text

Abstract:

Single-minded homologue 1 (SIM1) is a transcription factor with numerous different physiological and developmental functions. SIM1 is a member of the class I basic helix-loop-helix-PER-ARNT-SIM (bHLH–PAS) transcription factor family, that includes several other conserved proteins, including the hypoxia-inducible factors, aryl hydrocarbon receptor, neuronal PAS proteins, and the CLOCK circadian regulator. Recent studies of HIF-a-ARNT and CLOCK-BMAL1 protein complexes have revealed the organization of their bHLH, PASA, and PASB domains and provided insight into how these heterodimeric protein co

APA, Harvard, Vancouver, ISO, and other styles

31

Korkalainen, Merja, Jere Lindén, Jouko Tuomisto, and Raimo Pohjanvirta. "Effect of TCDD on mRNA expression of genes encoding bHLH/PAS proteins in rat hypothalamus." Toxicology 208, no. 1 (2005): 1–11. http://dx.doi.org/10.1016/j.tox.2004.11.003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Moffett, P., M. Reece, and J. Pelletier. "The murine Sim-2 gene product inhibits transcription by active repression and functional interference." Molecular and Cellular Biology 17, no. 9 (1997): 4933–47. http://dx.doi.org/10.1128/mcb.17.9.4933.

Full text

Abstract:

The Drosophila single-minded (Dsim) gene encodes a master regulatory protein involved in cell fate determination during midline development. This protein is a member of a rapidly expanding family of gene products possessing basic helix-loop-helix (bHLH) and hydrophobic PAS (designated a conserved region among PER, ARNT [aryl hydrocarbon receptor nuclear translocator] and SIM) protein association domains. Members of this family function as central transcriptional regulators in cellular differentiation and in the response to environmental stimuli such as xenobiotics and hypoxia. We have previous

APA, Harvard, Vancouver, ISO, and other styles

33

Pecenova, L., and Robert Farkas. "Multiple functions and essential roles of nuclear receptor coactivators of bHLH-PAS family." Endocrine Regulations 50, no. 3 (2016): 165–81. http://dx.doi.org/10.1515/enr-2016-0019.

Full text

Abstract:

Abstract Classical non-peptide hormones, such as steroids, retinoids, thyroid hormones, vitamin D3 and their derivatives including prostaglandins, benzoates, oxysterols, and bile acids, are collectively designated as small lipophilic ligands, acting via binding to the nuclear receptors (NRs). The NRs form a large superfamily of transcription factors that participate virtually in every key biological process. They control various aspects of animal development, fertility, gametogenesis, and numerous metabolic pathways, and can be misregulated in many types of cancers. Their enormous functional p

APA, Harvard, Vancouver, ISO, and other styles

34

Zhou, Y. D., M. Barnard, H. Tian, et al. "Molecular characterization of two mammalian bHLH-PAS domain proteins selectively expressed in the central nervous system." Proceedings of the National Academy of Sciences 94, no. 2 (1997): 713–18. http://dx.doi.org/10.1073/pnas.94.2.713.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Annunziata, Rossella, Andrés Ritter, Antonio Emidio Fortunato, et al. "bHLH-PAS protein RITMO1 regulates diel biological rhythms in the marine diatomPhaeodactylum tricornutum." Proceedings of the National Academy of Sciences 116, no. 26 (2019): 13137–42. http://dx.doi.org/10.1073/pnas.1819660116.

Full text

Abstract:

Periodic light–dark cycles govern the timing of basic biological processes in organisms inhabiting land as well as the sea, where life evolved. Although prominent marine phytoplanktonic organisms such as diatoms show robust diel rhythms, the mechanisms regulating these processes are still obscure. By characterizing aPhaeodactylum tricornutumbHLH-PAS nuclear protein, hereby named RITMO1, we shed light on the regulation of the daily life of diatoms. Alteration of RITMO1 expression levels and timing by ectopic overexpression results in lines with deregulated diurnal gene expression profiles compa

APA, Harvard, Vancouver, ISO, and other styles

36

Emmons, R. B., D. Duncan, P. A. Estes, et al. "The spineless-aristapedia and tango bHLH-PAS proteins interact to control antennal and tarsal development in Drosophila." Development 126, no. 17 (1999): 3937–45. http://dx.doi.org/10.1242/dev.126.17.3937.

Full text

Abstract:

The Drosophila spineless (ss) gene encodes a basic-helix-loop-helix-PAS transcription factor that is required for proper specification of distal antennal identity, establishment of the tarsal regions of the legs, and normal bristle growth. ss is the closest known homolog of the mammalian aryl hydrocarbon receptor (Ahr), also known as the dioxin receptor. Dioxin and other aryl hydrocarbons bind to the PAS domain of Ahr, causing Ahr to translocate to the nucleus, where it dimerizes with another bHLH-PAS protein, the aryl hydrocarbon receptor nuclear translocator (Arnt). Ahr:Arnt heterodimers the

APA, Harvard, Vancouver, ISO, and other styles

37

Freeman, Samuel L., Hanna Kwon, Nicola Portolano, et al. "Heme binding to human CLOCK affects interactions with the E-box." Proceedings of the National Academy of Sciences 116, no. 40 (2019): 19911–16. http://dx.doi.org/10.1073/pnas.1905216116.

Full text

Abstract:

The circadian clock is an endogenous time-keeping system that is ubiquitous in animals and plants as well as some bacteria. In mammals, the clock regulates the sleep–wake cycle via 2 basic helix–loop–helix PER-ARNT-SIM (bHLH-PAS) domain proteins—CLOCK and BMAL1. There is emerging evidence to suggest that heme affects circadian control, through binding of heme to various circadian proteins, but the mechanisms of regulation are largely unknown. In this work we examine the interaction of heme with human CLOCK (hCLOCK). We present a crystal structure for the PAS-A domain of hCLOCK, and we examine

APA, Harvard, Vancouver, ISO, and other styles

38

Lavista-Llanos, Sofía, Lázaro Centanin, Maximiliano Irisarri, et al. "Control of the Hypoxic Response in Drosophila melanogaster by the Basic Helix-Loop-Helix PAS Protein Similar." Molecular and Cellular Biology 22, no. 19 (2002): 6842–53. http://dx.doi.org/10.1128/mcb.22.19.6842-6853.2002.

Full text

Abstract:

ABSTRACT In mammalian systems, the heterodimeric basic helix-loop-helix (bHLH)-PAS transcription hypoxia-inducible factor (HIF) has emerged as the key regulator of responses to hypoxia. Here we define a homologous system in Drosophila melanogaster, and we characterize its activity in vivo during development. By using transcriptional reporters in developing transgenic flies, we show that hypoxia-inducible activity rises to a peak in late embryogenesis and is most pronounced in tracheal cells. We show that the bHLH-PAS proteins Similar (Sima) and Tango (Tgo) function as HIF-α and HIF-β homologue

APA, Harvard, Vancouver, ISO, and other styles

39

Wang, Feng, Shengli Shi, Ruixue Zhang, and Oliver Hankinson. "Identifying target genes of the aryl hydrocarbon receptor nuclear translocator (Arnt) using DNA microarray analysis." Biological Chemistry 387, no. 9 (2006): 1215–18. http://dx.doi.org/10.1515/bc.2006.150.

Full text

Abstract:

Abstract The aryl hydrocarbon receptor nuclear translocator (Arnt) is a basic helix-loop-helix (bHLH) protein that also contains a Per-Arnt-Sim (PAS) domain. In addition to forming heterodimers with many other bHLH-PAS proteins, including the aryl hydrocarbon receptor (AhR) and hypoxia-inducible factors 1α, 2α and 3α, Arnt can also form homodimers when expressed from its cDNA in vitro or in vivo. However, target genes of the Arnt/Arnt homodimer remain to be identified. In this study, we have elucidated the profile of genes responsive to the reintroduction of Arnt expression in an Arnt-deficien

APA, Harvard, Vancouver, ISO, and other styles

40

Dardente, Hugues, Erin E. Fortier, Vincent Martineau, and Nicolas Cermakian. "Cryptochromes impair phosphorylation of transcriptional activators in the clock: a general mechanism for circadian repression." Biochemical Journal 402, no. 3 (2007): 525–36. http://dx.doi.org/10.1042/bj20060827.

Full text

Abstract:

CLOCK and BMAL1 [brain and muscle ARNT (arylhydrocarbon receptor nuclear translocator)-like protein 1] are central components of the molecular clock in mammals and belong to the bHLH (basic helix–loop–helix)/PAS [PER (Period)/ARNT/SIM (single-minded)] family. Features of their dimerization have never been investigated. Here, we demonstrate that PAS domain function requires regions extending over the short PAS core repeats. Strikingly, while deleting PAS core repeats does not overtly affect dimerization, it abolishes the transcriptional activity of the heterodimer. Interestingly, these deletion

APA, Harvard, Vancouver, ISO, and other styles

41

Deng, Jiao, Lijuan Wang, Lan Zhang, et al. "Tartary Buckwheat (Fagopyrum tataricum) FtTT8 Inhibits Anthocyanin Biosynthesis and Promotes Proanthocyanidin Biosynthesis." International Journal of Molecular Sciences 24, no. 24 (2023): 17368. http://dx.doi.org/10.3390/ijms242417368.

Full text

Abstract:

Tartary buckwheat (Fagopyrum tataricum) is an important plant, utilized for both medicine and food. It has become a current research hotspot due to its rich content of flavonoids, which are beneficial for human health. Anthocyanins (ATs) and proanthocyanidins (PAs) are the two main kinds of flavonoid compounds in Tartary buckwheat, which participate in the pigmentation of some tissue as well as rendering resistance to many biotic and abiotic stresses. Additionally, Tartary buckwheat anthocyanins and PAs have many health benefits for humans and the plant itself. However, little is known about t

APA, Harvard, Vancouver, ISO, and other styles

42

Bernardo, Travis J., and Edward B. Dubrovsky. "Molecular Mechanisms of Transcription Activation by Juvenile Hormone: A Critical Role for bHLH-PAS and Nuclear Receptor Proteins." Insects 3, no. 1 (2012): 324–38. http://dx.doi.org/10.3390/insects3010324.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Richardson, Vicki M., Michael J. Santostefano, and Linda S. Birnbaum. "Daily Cycle of bHLH-PAS Proteins, Ah Receptor and Arnt, in Multiple Tissues of Female Sprague–Dawley Rats." Biochemical and Biophysical Research Communications 252, no. 1 (1998): 225–31. http://dx.doi.org/10.1006/bbrc.1998.9634.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Bae, Kiho, Choogon Lee, David Sidote, Keng-yu Chuang, and Isaac Edery. "Circadian Regulation of a Drosophila Homolog of the Mammalian Clock Gene: PER and TIM Function as Positive Regulators." Molecular and Cellular Biology 18, no. 10 (1998): 6142–51. http://dx.doi.org/10.1128/mcb.18.10.6142.

Full text

Abstract:

ABSTRACT The Clock gene plays an essential role in the manifestation of circadian rhythms (≅24 h) in mice and is a member of the basic helix-loop-helix (bHLH) PER-ARNT-SIM (PAS) superfamily of transcription factors. Here we report the characterization of a novelDrosophila bHLH-PAS protein that is highly homologous to mammalian CLOCK. (Similar findings were recently described by Allada et al. Cell 93:791–804, 1998, and Darlington et al., Science 280:1599–1603, 1998.) Transcripts from this putative Clockortholog (designated dClock) undergo daily rhythms in abundance that are antiphase to the cyc

APA, Harvard, Vancouver, ISO, and other styles

45

Whitelaw, M. L., J. A. Gustafsson, and L. Poellinger. "Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation." Molecular and Cellular Biology 14, no. 12 (1994): 8343–55. http://dx.doi.org/10.1128/mcb.14.12.8343-8355.1994.

Full text

Abstract:

Gene regulation by dioxins is mediated via the dioxin receptor, a ligand-dependent basic helix-loop-helix (bHLH)/PAS transcription factor. The latent dioxin receptor responds to dioxin signalling by forming an activated heterodimeric complex with a specific bHLH partner, Arnt, an essential process for target DNA recognition. We have analyzed the transactivating potential within this heterodimeric complex by dissecting it into individual subunits, replacing the dimerization and DNA-binding bHLH motifs with heterologous zinc finger DNA-binding domains. The uncoupled Arnt chimera, maintaining 84%

APA, Harvard, Vancouver, ISO, and other styles

46

Whitelaw, M. L., J. A. Gustafsson, and L. Poellinger. "Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation." Molecular and Cellular Biology 14, no. 12 (1994): 8343–55. http://dx.doi.org/10.1128/mcb.14.12.8343.

Full text

Abstract:

Gene regulation by dioxins is mediated via the dioxin receptor, a ligand-dependent basic helix-loop-helix (bHLH)/PAS transcription factor. The latent dioxin receptor responds to dioxin signalling by forming an activated heterodimeric complex with a specific bHLH partner, Arnt, an essential process for target DNA recognition. We have analyzed the transactivating potential within this heterodimeric complex by dissecting it into individual subunits, replacing the dimerization and DNA-binding bHLH motifs with heterologous zinc finger DNA-binding domains. The uncoupled Arnt chimera, maintaining 84%

APA, Harvard, Vancouver, ISO, and other styles

47

Beischlag, Timothy V., Song Wang, David W. Rose, et al. "Recruitment of the NCoA/SRC-1/p160 Family of Transcriptional Coactivators by the Aryl Hydrocarbon Receptor/Aryl Hydrocarbon Receptor Nuclear Translocator Complex." Molecular and Cellular Biology 22, no. 12 (2002): 4319–33. http://dx.doi.org/10.1128/mcb.22.12.4319-4333.2002.

Full text

Abstract:

ABSTRACT The aryl hydrocarbon receptor complex heterodimeric transcription factor, comprising the basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain aryl hydrocarbon receptor (AHR) and aryl hydrocarbon receptor nuclear translocator (ARNT) proteins, mediates the toxic effects of TCDD (2,3,7,8 tetrachlorodibenzo-p-dioxin). The molecular events underlying TCDD-inducible gene activation, beyond the activation of the AHRC, are poorly understood. The SRC-1/NCoA-1, NCoA-2/GRIP-1/TIF-2, and p/CIP/AIB/ACTR proteins have been shown to act as mediators of transcriptional activation. In this report, we

APA, Harvard, Vancouver, ISO, and other styles

48

Fahim, Ammad, Zaira Rehman, Muhammad Faraz Bhatti, et al. "Structural insights and characterization of human Npas4 protein." PeerJ 6 (June 14, 2018): e4978. http://dx.doi.org/10.7717/peerj.4978.

Full text

Abstract:

Npas4 is an activity dependent transcription factor which is responsible for gearing the expression of target genes involved in neuro-transmission. Despite the importance of Npas4 in many neuronal diseases, the tertiary structure of Npas4 protein along with its physico-chemical properties is limited. In the current study, first we perfomed the phylogenetic analysis of Npas4 and determined the content of hydrophobic, flexible and order-disorder promoting amino acids. The protein binding regions, post-translational modifications and crystallization propensity of Npas4 were predicted through diff

APA, Harvard, Vancouver, ISO, and other styles

49

Aitola, Marjo, Christine M. Sadek, Jan-Åke Gustafsson, and Markku Pelto-Huikko. "Aint/Tacc3 Is Highly Expressed in Proliferating Mouse Tissues During Development, Spermatogenesis, and Oogenesis." Journal of Histochemistry & Cytochemistry 51, no. 4 (2003): 455–69. http://dx.doi.org/10.1177/002215540305100407.

Full text

Abstract:

Aint was originally identified on the basis of its interaction in vitro with the aryl hydrocarbon nuclear receptor translocator (Arnt). Arnt is a common heterodimerization partner in the basic helix-loop–helix (bHLH)-PER-ARNT-SIM (PAS) protein family and is involved in diverse biological functions. These include xenobiotic metabolism, hypoxic response, and circadian rhythm. In addition, Arnt has a crucial role during development. Aint is a member of a growing family of transforming acidic coiled-coil (TACC) proteins and is the murine homologue of human TACC3. Here we report the spatiotemporal

APA, Harvard, Vancouver, ISO, and other styles

50

Lafleur, Véronique N., Silvia Halim, Peter J. Ratcliffe, and David R. Mole. "Abstract 677: Bi-directional crosstalk between the HIF and AHR transcription factors in clear cell kidney cancer." Cancer Research 82, no. 12_Supplement (2022): 677. http://dx.doi.org/10.1158/1538-7445.am2022-677.

Full text

Abstract:

Abstract Hypoxia is a key feature of the solid tumour microenvironment, in which it is associated with poor prognosis and resistance to therapy. Hypoxia-inducible factor (HIF) is the central mediator of cellular responses to hypoxia and drives a transcriptional program with central roles in tumorigenesis. Clear cell renal cell cancers (ccRCC) exhibit the most direct and profound upregulation of the HIF pathway - through bi-allelic inactivation of the VHL tumour suppressor, a ubiquitin ligase that targets HIF-alpha subunits for degradation under normal oxygenated conditions. HIF-alpha proteins

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!