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Article ; Online: The Role of WNT Pathway Mutations in Cancer Development and an Overview of Therapeutic Options.

Groenewald, Wibke / Lund, Anders H / Gay, David Michael

2023 Volume 12, Issue 7

Abstract: It is well established that mutations in the canonical WNT-signalling pathway play a major role in various cancers. Critical to developing new therapeutic strategies is understanding which cancers are driven by WNT pathway activation and at what level ... ...

Abstract	It is well established that mutations in the canonical WNT-signalling pathway play a major role in various cancers. Critical to developing new therapeutic strategies is understanding which cancers are driven by WNT pathway activation and at what level these mutations occur within the pathway. Some cancers harbour mutations in genes whose protein products operate at the receptor level of the WNT pathway. For instance, tumours with
MeSH term(s)	Humans ; Wnt Signaling Pathway/genetics ; Ligands ; Neoplasms/genetics ; Neoplasms/therapy ; Neoplasms/metabolism ; Mutation/genetics
Chemical Substances	Ligands
Language	English
Publishing date	2023-03-24
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells12070990
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Creativity as an antidote to research becoming too predictable.

Baer, Markus / Groth, Anja / Lund, Anders H / Sonne-Hansen, Katrine

The EMBO journal

2023 Volume 42, Issue 4, Page(s) e112835

Abstract: In this commentary, Sonne-Hansen and colleagues argue that research leaders and organizations should encourage more "theory-guessing" by budding young scientists, rather than incentivizing safe mainstream research. ...

Abstract	In this commentary, Sonne-Hansen and colleagues argue that research leaders and organizations should encourage more "theory-guessing" by budding young scientists, rather than incentivizing safe mainstream research.
MeSH term(s)	Antidotes ; Creativity
Chemical Substances	Antidotes
Language	English
Publishing date	2023-01-25
Publishing country	England
Document type	Journal Article
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2022112835
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Article: Translational control through ribosome heterogeneity and functional specialization.

Gay, David M / Lund, Anders H / Jansson, Martin D

Trends in biochemical sciences

2021 Volume 47, Issue 1, Page(s) 66–81

Abstract: The conceptual origins of ribosome specialization can be traced back to the earliest days of molecular biology. Yet, this field has only recently begun to gather momentum, with numerous studies identifying distinct heterogeneous ribosome populations ... ...

Abstract	The conceptual origins of ribosome specialization can be traced back to the earliest days of molecular biology. Yet, this field has only recently begun to gather momentum, with numerous studies identifying distinct heterogeneous ribosome populations across multiple species and model systems. It is proposed that some of these compositionally distinct ribosomes may be functionally specialized and able to regulate the translation of specific mRNAs. Identification and functional characterization of specialized ribosomes has the potential to elucidate a novel layer of gene expression control, at the level of translation, where the ribosome itself is a key regulatory player. In this review, we discuss different sources of ribosome heterogeneity, evidence for ribosome specialization, and also the future directions of this exciting field.
MeSH term(s)	Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Ribosomal/metabolism ; Ribosomal Proteins/metabolism ; Ribosomes/genetics ; Ribosomes/metabolism
Chemical Substances	RNA, Messenger ; RNA, Ribosomal ; Ribosomal Proteins
Language	English
Publishing date	2021-07-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	194216-5
ISSN	1362-4326 ; 0968-0004 ; 0376-5067
ISSN (online)	1362-4326
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2021.07.001
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Article: Translational control through ribosome heterogeneity and functional specialization

Gay, David M. / Lund, Anders H. / Jansson, Martin D.

Trends in biochemical sciences. 2022 Jan., v. 47, no. 1

2022

Abstract	The conceptual origins of ribosome specialization can be traced back to the earliest days of molecular biology. Yet, this field has only recently begun to gather momentum, with numerous studies identifying distinct heterogeneous ribosome populations across multiple species and model systems. It is proposed that some of these compositionally distinct ribosomes may be functionally specialized and able to regulate the translation of specific mRNAs. Identification and functional characterization of specialized ribosomes has the potential to elucidate a novel layer of gene expression control, at the level of translation, where the ribosome itself is a key regulatory player. In this review, we discuss different sources of ribosome heterogeneity, evidence for ribosome specialization, and also the future directions of this exciting field.
Keywords	gene expression ; molecular biology ; momentum ; ribosomes
Language	English
Dates of publication	2022-01
Size	p. 66-81.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	194220-7
ISSN	0968-0004 ; 0376-5067
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2021.07.001
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Article ; Online: FUS regulates a subset of snoRNA expression and modulates the level of rRNA modifications.

Gawade, Kishor / Plewka, Patrycja / Häfner, Sophia J / Lund, Anders H / Marchand, Virginie / Motorin, Yuri / Szczesniak, Michal W / Raczynska, Katarzyna D

Scientific reports

2023 Volume 13, Issue 1, Page(s) 2974

Abstract: FUS is a multifunctional protein involved in many aspects of RNA metabolism, including transcription, splicing, translation, miRNA processing, and replication-dependent histone gene expression. In this work, we show that FUS depletion results in the ... ...

Abstract	FUS is a multifunctional protein involved in many aspects of RNA metabolism, including transcription, splicing, translation, miRNA processing, and replication-dependent histone gene expression. In this work, we show that FUS depletion results in the differential expression of numerous small nucleolar RNAs (snoRNAs) that guide 2'-O methylation (2'-O-Me) and pseudouridylation of specific positions in ribosomal RNAs (rRNAs) and small nuclear RNAs (snRNAs). Using RiboMeth-seq and HydraPsiSeq for the profiling of 2'-O-Me and pseudouridylation status of rRNA species, we demonstrated considerable hypermodification at several sites in HEK293T and SH-SY5Y cells with FUS knockout (FUS KO) compared to wild-type cells. We observed a similar direction of changes in rRNA modification in differentiated SH-SY5Y cells with the FUS mutation (R495X) related to the severe disease phenotype of amyotrophic lateral sclerosis (ALS). Furthermore, the pattern of modification of some rRNA positions was correlated with the abundance of corresponding guide snoRNAs in FUS KO and FUS R495X cells. Our findings reveal a new role for FUS in modulating the modification pattern of rRNA molecules, that in turn might generate ribosome heterogeneity and constitute a fine-tuning mechanism for translation efficiency/fidelity. Therefore, we suggest that increased levels of 2'-O-Me and pseudouridylation at particular positions in rRNAs from cells with the ALS-linked FUS mutation may represent a possible new translation-related mechanism that underlies disease development and progression.
MeSH term(s)	Humans ; RNA, Small Nucleolar/genetics ; Amyotrophic Lateral Sclerosis ; HEK293 Cells ; Neuroblastoma ; RNA, Ribosomal/genetics ; RNA-Binding Protein FUS/genetics
Chemical Substances	RNA, Small Nucleolar ; RNA, Ribosomal ; FUS protein, human ; RNA-Binding Protein FUS
Language	English
Publishing date	2023-02-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-023-30068-2
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Article ; Online: Initiation of a ZAKα-dependent ribotoxic stress response by the innate immunity endoribonuclease RNase L.

Xi, Jiajia / Snieckute, Goda / Martínez, José Francisco / Arendrup, Frederic Schrøder Wenzel / Asthana, Abhishek / Gaughan, Christina / Lund, Anders H / Bekker-Jensen, Simon / Silverman, Robert H

Cell reports

2024 Volume 43, Issue 4, Page(s) 113998

Abstract: RNase L is an endoribonuclease of higher vertebrates that functions in antiviral innate immunity. Interferons induce oligoadenylate synthetase enzymes that sense double-stranded RNA of viral origin leading to the synthesis of 2',5'-oligoadenylate (2-5A) ... ...

Abstract	RNase L is an endoribonuclease of higher vertebrates that functions in antiviral innate immunity. Interferons induce oligoadenylate synthetase enzymes that sense double-stranded RNA of viral origin leading to the synthesis of 2',5'-oligoadenylate (2-5A) activators of RNase L. However, it is unknown precisely how RNase L remodels the host cell transcriptome. To isolate effects of RNase L from other effects of double-stranded RNA or virus, 2-5A is directly introduced into cells. Here, we report that RNase L activation by 2-5A causes a ribotoxic stress response involving the MAP kinase kinase kinase (MAP3K) ZAKα, MAP2Ks, and the stress-activated protein kinases JNK and p38α. RNase L activation profoundly alters the transcriptome by widespread depletion of mRNAs associated with different cellular functions but also by JNK/p38α-stimulated induction of inflammatory genes. These results show that the 2-5A/RNase L system triggers a protein kinase cascade leading to proinflammatory signaling and apoptosis.
MeSH term(s)	Endoribonucleases/metabolism ; Endoribonucleases/genetics ; Immunity, Innate ; Humans ; Adenine Nucleotides/metabolism ; Oligoribonucleotides/metabolism ; Animals ; Stress, Physiological ; Transcriptome/genetics ; RNA, Double-Stranded/metabolism
Chemical Substances	Endoribonucleases (EC 3.1.-) ; 2-5A-dependent ribonuclease (EC 3.1.26.-) ; 2',5'-oligoadenylate (61172-40-5) ; Adenine Nucleotides ; Oligoribonucleotides ; RNA, Double-Stranded
Language	English
Publishing date	2024-03-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2024.113998
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Article ; Online: Great expectations - Epigenetics and the meandering path from bench to bedside.

Häfner, Sophia J / Lund, Anders H

Biomedical journal

2016 Volume 39, Issue 3, Page(s) 166–176

Abstract: Making quick promises of major biomedical breakthroughs based on exciting discoveries at the bench is tempting. But the meandering path from fundamental science to life-saving clinical applications can be fraught with many hurdles. Epigenetics, the study ...

Abstract	Making quick promises of major biomedical breakthroughs based on exciting discoveries at the bench is tempting. But the meandering path from fundamental science to life-saving clinical applications can be fraught with many hurdles. Epigenetics, the study of potentially heritable changes of gene function without modification of the underlying DNA sequence, has dominated the biological research field during the last decade and encountered a large public success. Driven by the unfolding of molecular biology and recent technological progress, the term has evolved significantly and shifted from a conceptual framework to a mechanistic understanding. This shift was accompanied by much hype and raised high hopes that epigenetics might hold both the key to deciphering the molecular underpinning of complex, non-Mendelian diseases and offer novel therapeutic approaches for a large panel of pathologies. However, while exciting reports of biological phenomena involving DNA methylation and histone modifications fill up the scientific literature, the realistic clinical applications of epigenetic medicines remain somewhat blurry. Here, we discuss the state of the art and speculate how epigenetics might contribute to prognostic and therapy approaches in the future.
MeSH term(s)	Animals ; DNA ; DNA Methylation/genetics ; Epigenesis, Genetic ; Genetic Predisposition to Disease ; Histone Code/genetics ; Humans ; Research
Chemical Substances	DNA (9007-49-2)
Language	English
Publishing date	2016-08-10
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2698541-X
ISSN	2320-2890 ; 2319-4170
ISSN (online)	2320-2890
ISSN	2319-4170
DOI	10.1016/j.bj.2016.01.008
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Article ; Online: Emerging roles of lncRNAs in senescence.

Montes, Marta / Lund, Anders H

The FEBS journal

2016 Volume 283, Issue 13, Page(s) 2414–2426

Abstract: Cellular senescence is a complex stress response that leads to an irreversible state of cell growth arrest. Senescence may be induced by various stimuli such as telomere shortening, DNA damage or oncogenic insult, among others. Senescent cells are ... ...

Abstract	Cellular senescence is a complex stress response that leads to an irreversible state of cell growth arrest. Senescence may be induced by various stimuli such as telomere shortening, DNA damage or oncogenic insult, among others. Senescent cells are metabolically highly active, producing a wealth of cytokines and chemokines that, depending on the context, may have a beneficial or deleterious effect on the organism. Senescence is considered a tightly regulated stress response that is largely governed by the p53/p21 and p16/Rb pathways. Many molecules have been identified as regulators of these two networks, such as transcription factors, chromatin modifiers and non-coding RNAs. The expression level of several long non-coding RNAs is affected during different types of senescence; however, which of these are important for the biological function remains poorly understood. Here we review our current knowledge of the mechanistic roles of lncRNAs affecting the main senescence pathways, and discuss the importance of identifying new regulators.
MeSH term(s)	Animals ; Cellular Senescence/genetics ; Cellular Senescence/physiology ; DNA Damage/genetics ; DNA Damage/physiology ; Humans ; Models, Biological ; RNA, Long Noncoding/genetics ; Signal Transduction/genetics ; Signal Transduction/physiology
Chemical Substances	RNA, Long Noncoding
Language	English
Publishing date	2016-07
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13679
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Article: Emerging roles of lncRNAs in senescence

Montes, Marta / Lund, Anders H

FEBS journal. 2016 July, v. 283, no. 13

2016

Abstract	Cellular senescence is a complex stress response that leads to an irreversible state of cell growth arrest. Senescence may be induced by various stimuli such as telomere shortening, DNA damage or oncogenic insult, among others. Senescent cells are metabolically highly active, producing a wealth of cytokines and chemokines that, depending on the context, may have a beneficial or deleterious effect on the organism. Senescence is considered a tightly regulated stress response that is largely governed by the p53/p21 and p16/Rb pathways. Many molecules have been identified as regulators of these two networks, such as transcription factors, chromatin modifiers and non‐coding RNAs. The expression level of several long non‐coding RNAs is affected during different types of senescence; however, which of these are important for the biological function remains poorly understood. Here we review our current knowledge of the mechanistic roles of lncRNAs affecting the main senescence pathways, and discuss the importance of identifying new regulators.
Keywords	DNA damage ; cell cycle checkpoints ; cell senescence ; chemokines ; chromatin ; non-coding RNA ; stress response ; telomeres ; transcription factors
Language	English
Dates of publication	2016-07
Size	p. 2414-2426.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	REVIEW
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13679
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Article ; Online: Nitric oxide-induced ribosome collision activates ribosomal surveillance mechanisms.

Ryder, Laura / Arendrup, Frederic Schrøder / Martínez, José Francisco / Snieckute, Goda / Pecorari, Chiara / Shah, Riyaz Ahmad / Lund, Anders H / Blasius, Melanie / Bekker-Jensen, Simon

Cell death & disease

2023 Volume 14, Issue 7, Page(s) 467

Abstract: Impairment of protein translation can cause stalling and collision of ribosomes and is a signal for the activation of ribosomal surveillance and rescue pathways. Despite clear evidence that ribosome collision occurs stochastically at a cellular and ... ...

Abstract	Impairment of protein translation can cause stalling and collision of ribosomes and is a signal for the activation of ribosomal surveillance and rescue pathways. Despite clear evidence that ribosome collision occurs stochastically at a cellular and organismal level, physiologically relevant sources of such aberrations are poorly understood. Here we show that a burst of the cellular signaling molecule nitric oxide (NO) reduces translational activity and causes ribosome collision in human cell lines. This is accompanied by activation of the ribotoxic stress response, resulting in ZAKα-mediated activation of p38 and JNK kinases. In addition, NO production is associated with ZNF598-mediated ubiquitination of the ribosomal protein RPS10 and GCN2-mediated activation of the integrated stress response, which are well-described responses to the collision of ribosomes. In sum, our work implicates a novel role of NO as an inducer of ribosome collision and activation of ribosomal surveillance mechanisms in human cells.
MeSH term(s)	Humans ; Nitric Oxide/metabolism ; Ribosomes/metabolism ; Protein Biosynthesis ; Ribosomal Proteins/genetics ; Ribosomal Proteins/metabolism ; Ubiquitination ; Carrier Proteins/metabolism
Chemical Substances	Nitric Oxide (31C4KY9ESH) ; Ribosomal Proteins ; ZNF598 protein, human ; Carrier Proteins
Language	English
Publishing date	2023-07-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-023-05997-5
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