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Article: Proteomic Interactome of C. elegans Mediator Complex Subunit 28 (MDT-28) Reveals Predominant Association with a Restricted Set of Core Mediator Subunits and an Affinity to Additional Structural and Enzymatic Proteins.

Yilma, P / Kostrouchová, M / Talacko, P / Kostrouchová, V / Kostrouch, D / Novák, P / Kostrouchová, M

2020 Volume 65, Issue 5-6, Page(s) 203–211

Abstract: Transcription factors exert their regulatory potential on RNA polymerase II machinery through a multiprotein complex called Mediator complex or Mediator. The Mediator complex integrates regulatory signals from cell regulatory cascades with the regulation ...

Abstract	Transcription factors exert their regulatory potential on RNA polymerase II machinery through a multiprotein complex called Mediator complex or Mediator. The Mediator complex integrates regulatory signals from cell regulatory cascades with the regulation by transcription factors. The Mediator complex consists of 25 subunits in Saccharomyces cerevisiae and 30 or more subunits in multicellular eukaryotes. Mediator subunit 28 (MED28), along with MED30, MED23, MED25 and MED26, belong to presumably evolutionarily new subunits that seem to be absent in unicellular eukaryotes and are likely to have evolved together with multicellularity and cell differentiation. Previously, we have shown that an originally uncharacterized predicted gene, F28F8.5, is the true MED28 orthologue in Caenorhabditis elegans (mdt-28) and showed that it is involved in a spectrum of developmental processes. Here, we studied the proteomic interactome of MDT-28 edited as GFP::MDT-28 using Crispr/Cas9 technology or MDT-28::GFP expressed from extrachromosomal arrays in transgenic C. elegans exploiting the GFPTRAP system and mass spectrometry. The results show that MDT-28 associates with the Head module subunits MDT-6, MDT-8, MDT-11, MDT-17, MDT- 20, MDT-22, and MDT-30 and the Middle module subunit MDT-14. The analyses also identified additional proteins as preferential MDT-28 interactants, including chromatin-organizing proteins, structural proteins and enzymes. The results provide evidence for MDT-28 engagement in the Mediator Head module and support the possibility of physical (direct or indirect) interaction of MDT-28 with additional proteins, reflecting the transcription-regulating potential of primarily structural and enzymatic proteins at the level of the Mediator complex.
MeSH term(s)	Alleles ; Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Mediator Complex/metabolism ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Subunits/metabolism ; Proteomics
Chemical Substances	Caenorhabditis elegans Proteins ; MDT-28 protein, C elegans ; Mediator Complex ; Nuclear Proteins ; Protein Subunits
Language	English
Publishing date	2020-04-07
Publishing country	Czech Republic
Document type	Journal Article
ZDB-ID	419223-0
ISSN	0015-5500
ISSN	0015-5500
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: ALKB-8, a 2-Oxoglutarate-Dependent Dioxygenase and S-Adenosine Methionine-Dependent Methyltransferase Modulates Metabolic Events Linked to Lysosome-Related Organelles and Aging in C. elegans.

Kollárová, J / Kostrouchová, M / Benda, A / Kostrouchová, M

Folia biologica

2018 Volume 64, Issue 2, Page(s) 46–58

Abstract: ALKB-8 is a 2-oxoglutarate-dependent dioxygenase homologous to bacterial AlkB, which oxidatively demethylates DNA substrates. The mammalian AlkB family contains AlkB homologues denominated ALKBH1 to 8 and FTO. The C. elegans genome includes five AlkB- ... ...

Abstract	ALKB-8 is a 2-oxoglutarate-dependent dioxygenase homologous to bacterial AlkB, which oxidatively demethylates DNA substrates. The mammalian AlkB family contains AlkB homologues denominated ALKBH1 to 8 and FTO. The C. elegans genome includes five AlkB-related genes, homologues of ALKBH1, 4, 6, 7, and 8, but lacks homologues of ALKBH2, 3, and 5 and FTO. ALKBH8 orthologues differ from other AlkB family members by possessing an additional methyltransferase module and an RNA binding N-terminal module. The ALKBH8 methyltransferase domain generates the wobble nucleoside 5-methoxycarbonylmethyluridine from its precursor 5-carboxymethyluridine and its (R)- and (S)-5-methoxycarbonylhydroxymethyluridine hydroxylated forms in tRNA Arg/UCG and tRNA Gly/UCC. The ALKBH8/ALKB-8 methyltransferase domain is highly similar to yeast TRM9, which selectively modulates translation of mRNAs enriched with AGA and GAA codons under both normal and stress conditions. In this report, we studied the role of alkb-8 in C. elegans. We show that downregulation of alkb-8 increases detection of lysosome-related organelles visualized by Nile red in vivo. Reversely, forced expression of alkb-8 strongly decreases the detection of this compartment. In addition, overexpression of alkb-8 applied in a pulse during the L1 larval stage increases the C. elegans lifespan.
MeSH term(s)	Aging/metabolism ; AlkB Enzymes/genetics ; AlkB Enzymes/metabolism ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Dioxygenases/metabolism ; Down-Regulation/genetics ; Embryo, Nonmammalian/metabolism ; Gene Expression Regulation, Developmental ; Green Fluorescent Proteins/metabolism ; Ketoglutaric Acids/metabolism ; Larva/metabolism ; Longevity ; Lysosomes/metabolism ; Methyltransferases/metabolism ; Operon ; Promoter Regions, Genetic ; RNA Interference ; S-Adenosylmethionine/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; Ketoglutaric Acids ; Green Fluorescent Proteins (147336-22-9) ; S-Adenosylmethionine (7LP2MPO46S) ; Dioxygenases (EC 1.13.11.-) ; ALKB-8 protein, C elegans (EC 1.14.11.33) ; AlkB Enzymes (EC 1.14.11.33) ; Methyltransferases (EC 2.1.1.-)
Language	English
Publishing date	2018-07-25
Publishing country	Czech Republic
Document type	Journal Article
ZDB-ID	419223-0
ISSN	0015-5500
ISSN	0015-5500
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Valproic Acid Decreases the Nuclear Localization of MDT-28, the Nematode Orthologue of MED28.

Kostrouchová, M / Kostrouchová, V / Yilma, P / Benda, A / Mandys, V / Kostrouchová, M

Folia biologica

2018 Volume 64, Issue 1, Page(s) 1–9

Abstract: Mediator is a multiprotein complex that connects regulation mediated by transcription factors with RNA polymerase II transcriptional machinery and integrates signals from the cell regulatory cascades with gene expression. One of the Mediator subunits, ... ...

Abstract	Mediator is a multiprotein complex that connects regulation mediated by transcription factors with RNA polymerase II transcriptional machinery and integrates signals from the cell regulatory cascades with gene expression. One of the Mediator subunits, Mediator complex subunit 28 (MED28), has a dual nuclear and cytoplasmic localization and function. In the nucleus, MED28 functions as part of Mediator and in the cytoplasm, it interacts with cytoskeletal proteins and is part of the regulatory cascades including that of Grb2. MED28 thus has the potential to bring cytoplasmic regulatory interactions towards the centre of gene expression regulation. In this study, we identified MDT-28, the nematode orthologue of MED28, as a likely target of lysine acetylation using bioinformatic prediction of posttranslational modifications. Lysine acetylation was experimentally confirmed using anti-acetyl lysine antibody on immunoprecipitated GFP::MDT-28 expressed in synchronized C. elegans. Valproic acid (VPA), a known inhibitor of lysine deacetylases, enhanced the lysine acetylation of GFP::MDT-28. At the subcellular level, VPA decreased the nuclear localization of GFP::MDT-28 detected by fluorescencelifetime imaging microscopy (FLIM). This indicates that the nuclear pool of MDT-28 is regulated by a mechanism sensitive to VPA and provides an indirect support for a variable relative proportion of MED28 orthologues with other Mediator subunits.
MeSH term(s)	Acetylation ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/drug effects ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/chemistry ; Caenorhabditis elegans Proteins/metabolism ; Cell Nucleus/drug effects ; Cell Nucleus/metabolism ; Computational Biology ; Densitometry ; Green Fluorescent Proteins/metabolism ; Humans ; Larva/drug effects ; Lysine/metabolism ; Mediator Complex/chemistry ; Mediator Complex/metabolism ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Protein Transport/drug effects ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid ; Valproic Acid/pharmacology
Chemical Substances	Caenorhabditis elegans Proteins ; MDT-28 protein, C elegans ; Mediator Complex ; Nuclear Proteins ; Recombinant Fusion Proteins ; Green Fluorescent Proteins (147336-22-9) ; Valproic Acid (614OI1Z5WI) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2018-03-30
Publishing country	Czech Republic
Document type	Journal Article
ZDB-ID	419223-0
ISSN	0015-5500
ISSN	0015-5500
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Caenorhabditis elegans Perilipin Is Implicated in Cold-Induced Lipolysis and Inhibits Autophagy in Early Embryos.

Kassak, F / Chughtai, A A / Kassak, S / Kostrouchova, M

Folia biologica

2021 Volume 66, Issue 5-6, Page(s) 179–185

Abstract: Animals use neutral lipids, particularly triacylglycerols (TAGs), to store energy. TAGs are universally organized into dynamic cytoplasmic structures called lipid droplets (LDs). In mammals TAG breakdown is catalysed by lipases, such as hormonesensitive ... ...

Abstract	Animals use neutral lipids, particularly triacylglycerols (TAGs), to store energy. TAGs are universally organized into dynamic cytoplasmic structures called lipid droplets (LDs). In mammals TAG breakdown is catalysed by lipases, such as hormonesensitive lipase (HSL). LD membrane-resident proteins called perilipins (PLINs) regulate some of these lipases. The model organism Caenorhabditis elegans has a single known PLIN homologue and orthologues of most lipases including HSL. HOSL-1 (the HSL orthologue in C. elegans) is responsible for production of cryoprotective glycerol in cold conditions, in addition to its role in fasting-induced lipolysis. We employed this model of cold exposure to study the role of PLIN-1 in the regulation of HOSL-1. Our results suggest that both HOSL-1 and PLIN-1 are required for cold tolerance and for lipid breakdown in cold. However, the loss of PLIN-1 partially rescued the phenotype of hosl-1 null mutants exposed to cold, suggesting the presence of an alternative pathway generating glycerol via lipolysis. In early embryos, PLIN-1 knock-out results in accumulation of lipids and formation of cytoplasmic clusters of autophagic marker LGG-1, supporting the role of autophagy as an alternative lipolytic pathway in C. elegans, as is the case in mammals.
MeSH term(s)	Animals ; Autophagy ; Caenorhabditis elegans ; Lipolysis ; Membrane Proteins ; Perilipin-1
Chemical Substances	Membrane Proteins ; Perilipin-1
Language	English
Publishing date	2021-06-04
Publishing country	Czech Republic
Document type	Journal Article
ZDB-ID	419223-0
ISSN	0015-5500
ISSN	0015-5500
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Novel Mutation (T273R) in Thyroid Hormone Receptor β Gene Provides Further Insight into Cryptic Negative Regulation by Thyroid Hormone.

Kaššák, F / Hána, V / Saudek, V / Kostrouchová, M

Folia biologica

2016 Volume 63, Issue 2, Page(s) 60–66

Abstract: Production of thyroid hormone is precisely regulated in a negative feed-back mechanism that depends critically on thyroid hormone receptor β (TRβ). This mechanism decreases production of thyrotropin- releasing hormone (TRH) and thyrotropin (TSH) in the ... ...

Abstract	Production of thyroid hormone is precisely regulated in a negative feed-back mechanism that depends critically on thyroid hormone receptor β (TRβ). This mechanism decreases production of thyrotropin- releasing hormone (TRH) and thyrotropin (TSH) in the hypothalamus and pituitary gland in response to high levels of circulating thyroid hormones (TH). Despite the wealth of accumulated knowledge, it is still not clear how exactly this negative regulation is executed. The syndrome of resistance to thyroid hormone (RTH), in which the levels of TH are not properly sensed, represents naturally occurring situations in which molecular components of this regulation are displayed and may be uncovered. TRβ, which is central to this regulation, is in the majority of RTH cases mutated in a way that preserves some functions of the receptor. Approximately 150 different mutations in TRβ have been identified to date. Here, we hypothesized that additional pathogenic mutations in TRβ are likely to exist in human population and analysed clinical cases with suspected RTH. In keeping with our prediction, analysis of 17 patients from nine families led to identification of four presumed pathogenic mutations of TRβ, including a previously unknown mutation, T273R. This suggests that threonine 273 is likely to be critical for the normal function of TRβ, possibly due to its role in helix 12 mobility and interaction with coactivators, and thus supports the concept that TRβ-dependent trans-activating function is necessary for the inhibition of TRH and TSH expression in response to elevated levels of TH.
MeSH term(s)	Female ; Humans ; Hypothalamus/metabolism ; Male ; Mutation ; Thyroid Hormone Receptors beta/genetics ; Thyroid Hormones/metabolism ; Thyrotropin/metabolism ; Thyrotropin-Releasing Hormone/metabolism
Chemical Substances	Thyroid Hormone Receptors beta ; Thyroid Hormones ; Thyrotropin-Releasing Hormone (5Y5F15120W) ; Thyrotropin (9002-71-5)
Language	English
Publishing date	2016-12-24
Publishing country	Czech Republic
Document type	Journal Article
ZDB-ID	419223-0
ISSN	0015-5500
ISSN	0015-5500
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of

Kostrouchová, Markéta / Kostrouch, David / Chughtai, Ahmed A / Kaššák, Filip / Novotný, Jan P / Kostrouchová, Veronika / Benda, Aleš / Krause, Michael W / Saudek, Vladimír / Kostrouchová, Marta / Kostrouch, Zdeněk

PeerJ

2017 Volume 5, Page(s) e3390

Abstract: The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, the Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, ... ...

Abstract	The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, the Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polymerase II activity. One Mediator subunit, MED28, is known to interact with cytoplasmic structural proteins, providing a potential direct link between cytoplasmic dynamics and the control of gene transcription. Although identified in many animals and plants, MED28 is not present in yeast; no bona fide MED28 has been described previously in
Language	English
Publishing date	2017-06-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2703241-3
ISSN	2167-8359
ISSN	2167-8359
DOI	10.7717/peerj.3390
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Trichoplax adhaerens

Novotný, Jan Philipp / Chughtai, Ahmed Ali / Kostrouchová, Markéta / Kostrouchová, Veronika / Kostrouch, David / Kaššák, Filip / Kaňa, Radek / Schierwater, Bernd / Kostrouchová, Marta / Kostrouch, Zdenek

PeerJ

2017 Volume 5, Page(s) e3789

Abstract: Trichoplax ... ...

Abstract	Trichoplax adhaerens
Language	English
Publishing date	2017-09-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	2703241-3
ISSN	2167-8359
ISSN	2167-8359
DOI	10.7717/peerj.3789
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: SKIP and BIR-1/Survivin have potential to integrate proteome status with gene expression.

Kostrouch, David / Kostrouchová, Markéta / Yilma, Petr / Chughtai, Ahmed Ali / Novotný, Jan Philipp / Novák, Petr / Kostrouchová, Veronika / Kostrouchová, Marta / Kostrouch, Zdeněk

Journal of proteomics

2014 Volume 110, Page(s) 93–106

Abstract: SKIP and BIR are evolutionarily conserved proteins; SKIP (SKP-1) is a known transcription and splicing cofactor while BIR-1/Survivin regulates cell division, gene expression and development. Their loss of function induces overlapping developmental ... ...

Abstract	SKIP and BIR are evolutionarily conserved proteins; SKIP (SKP-1) is a known transcription and splicing cofactor while BIR-1/Survivin regulates cell division, gene expression and development. Their loss of function induces overlapping developmental phenotypes. We searched for SKP-1 and BIR-1 interaction on protein level using yeast two-hybrid screens and identified partially overlapping categories of proteins as SKIP-1 and BIR-1 interactors. The interacting proteins included ribosomal proteins, transcription factors, translation factors and cytoskeletal and motor proteins suggesting involvement in multiple protein complexes. To visualize the effect of BIR-1 on the proteome in Caenorhabditis elegans we induced a short time pulse BIR-1 overexpression in synchronized L1 larvae. This led to a dramatic alteration of the whole proteome pattern indicating that BIR-1 alone has the capacity to alter the chromatographic profile of many target proteins including proteins found to be interactors in yeast two hybrid screens. The results were validated for ribosomal proteins RPS3 and RPL5, non-muscle myosin and TAC-1, a transcription cofactor and a centrosome associated protein. Together, these results suggest that SKP-1 and BIR-1 are multifunctional proteins that form multiple protein complexes in both shared and distinct pathways and have the potential to connect proteome signals with the regulation of gene expression. Biological significance: The genomic organization of the genes encoding BIR-1 and SKIP (SKP-1) in C. elegans have suggested that these two factors, each evolutionarily conserved, have related functions. However, these functional connections have remained elusive and underappreciated in light of limited information from C. elegans and other biological systems. Our results provide further evidence for a functional link between these two factors and suggest they may transmit proteome signals towards the regulation of gene expression.
MeSH term(s)	Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Gene Expression Regulation/physiology ; Nuclear Proteins/metabolism ; Proteome/metabolism ; Signal Transduction/physiology ; Survivors ; Ubiquitin-Protein Ligase Complexes
Chemical Substances	Caenorhabditis elegans Proteins ; Nuclear Proteins ; Proteome ; bir-1 protein, C elegans ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; skp-1 protein, C elegans (EC 2.3.2.23)
Language	English
Publishing date	2014-08-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2400835-7
ISSN	1876-7737 ; 1874-3919
ISSN (online)	1876-7737
ISSN	1874-3919
DOI	10.1016/j.jprot.2014.07.023
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Valproic acid, a molecular lead to multiple regulatory pathways.

Kostrouchová, M / Kostrouch, Z / Kostrouchová, M

Folia biologica

2007 Volume 53, Issue 2, Page(s) 37–49

Abstract: Valproic acid (2-propyl pentanoic acid) is a drug used for the treatment of epilepsy and bipolar disorder. Although very rare, side effects such as spina bifida and other defects of neural tube closure indicate that valproic acid interferes with ... ...

Abstract	Valproic acid (2-propyl pentanoic acid) is a drug used for the treatment of epilepsy and bipolar disorder. Although very rare, side effects such as spina bifida and other defects of neural tube closure indicate that valproic acid interferes with developmental regulatory pathways. Recently obtained data show that valproic acid affects cell growth, differentiation, apoptosis and immunogenicity of cultured cancer cells and tumours. Focused studies uncovered the potential of valproic acid to interfere with multiple regulatory mechanisms including histone deacetylases, GSK3 alpha and beta, Akt, the ERK pathway, the phosphoinositol pathway, the tricarboxylic acid cycle, GABA, and the OXPHOS system. Valproic acid is emerging as a potential anticancer drug and may also serve as a molecular lead that can help design drugs with more specific and more potent effects on the one side and drugs with wide additive but weaker effects on the other. Valproic acid is thus a powerful molecular tool for better understanding and therapeutic targeting of pathways that regulate the behaviour of cancer cells.
MeSH term(s)	Animals ; Antineoplastic Agents/administration & dosage ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Antineoplastic Combined Chemotherapy Protocols/therapeutic use ; Gene Expression Regulation, Neoplastic/drug effects ; Humans ; Neoplasms/drug therapy ; Neoplasms/genetics ; Teratogens/toxicity ; Valproic Acid/analogs & derivatives ; Valproic Acid/chemistry ; Valproic Acid/pharmacology ; Valproic Acid/therapeutic use
Chemical Substances	Antineoplastic Agents ; Teratogens ; Valproic Acid (614OI1Z5WI)
Language	English
Publishing date	2007
Publishing country	Czech Republic
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	419223-0
ISSN	0015-5500
ISSN	0015-5500
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Nuclear receptors in nematode development: Natural experiments made by a phylum.

Kostrouchova, Marta / Kostrouch, Zdenek

Biochimica et biophysica acta

2015 Volume 1849, Issue 2, Page(s) 224–237

Abstract: The development of complex multicellular organisms is dependent on regulatory decisions that are necessary for the establishment of specific differentiation and metabolic cellular states. Nuclear receptors (NRs) form a large family of transcription ... ...

Abstract	The development of complex multicellular organisms is dependent on regulatory decisions that are necessary for the establishment of specific differentiation and metabolic cellular states. Nuclear receptors (NRs) form a large family of transcription factors that play critical roles in the regulation of development and metabolism of Metazoa. Based on their DNA binding and ligand binding domains, NRs are divided into eight NR subfamilies from which representatives of six subfamilies are present in both deuterostomes and protostomes indicating their early evolutionary origin. In some nematode species, especially in Caenorhabditis, the family of NRs expanded to a large number of genes strikingly exceeding the number of NR genes in vertebrates or insects. Nematode NRs, including the multiplied Caenorhabditis genes, show clear relation to vertebrate and insect homologues belonging to six of the eight main NR subfamilies. This review summarizes advances in research of nematode NRs and their developmental functions. Nematode NRs can reveal evolutionarily conserved mechanisms that regulate specific developmental and metabolic processes as well as new regulatory adaptations. They represent the results of a large number of natural experiments with structural and functional potential of NRs for the evolution of the phylum. The conserved and divergent character of nematode NRs adds a new dimension to our understanding of the general biology of regulation by NRs. This article is part of a Special Issue entitled: Nuclear receptors in animal development.
MeSH term(s)	Animals ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans/genetics ; Conserved Sequence ; Evolution, Molecular ; Nematoda/embryology ; Nematoda/genetics ; Nematoda/growth & development ; Receptors, Cytoplasmic and Nuclear/classification ; Receptors, Cytoplasmic and Nuclear/physiology
Chemical Substances	Receptors, Cytoplasmic and Nuclear
Language	English
Publishing date	2015-02
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagrm.2014.06.016
Database	MEDical Literature Analysis and Retrieval System OnLINE

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