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Article: DNA helicases associated with genetic instability, cancer, and aging.

Suhasini, Avvaru N / Brosh, Robert M

Advances in experimental medicine and biology

2012 Volume 767, Page(s) 123–144

Abstract: DNA helicases have essential roles in the maintenance of genomic -stability. They have achieved even greater prominence with the discovery that mutations in human helicase genes are responsible for a variety of genetic disorders and are associated with ... ...

Abstract	DNA helicases have essential roles in the maintenance of genomic -stability. They have achieved even greater prominence with the discovery that mutations in human helicase genes are responsible for a variety of genetic disorders and are associated with tumorigenesis. A number of missense mutations in human helicase genes are linked to chromosomal instability diseases characterized by age-related disease or associated with cancer, providing incentive for the characterization of molecular defects underlying aberrant cellular phenotypes. In this chapter, we discuss some examples of clinically relevant missense mutations in various human DNA helicases, particularly those of the Iron-Sulfur cluster and RecQ families. Clinically relevant mutations in the XPD helicase can lead to Xeroderma pigmentosum, Cockayne's syndrome, Trichothiodystrophy, or COFS syndrome. FANCJ mutations are associated with Fanconi anemia or breast cancer. Mutations of the Fe-S helicase ChlR1 (DDX11) are linked to Warsaw Breakage syndrome. Mutations in the RecQ helicases BLM and WRN are linked to the cancer-prone disorder Bloom's syndrome and premature aging condition Werner syndrome, respectively. RECQL4 mutations can lead to Rothmund-Thomson syndrome, Baller-Gerold syndrome, or RAPADILINO. Mutations in the Twinkle mitochondrial helicase are responsible for several neuromuscular degenerative disorders. We will discuss some insights gained from biochemical and genetic studies of helicase variants, and highlight some hot areas of helicase research based on recent developments.
MeSH term(s)	DNA Helicases ; Genomic Instability ; Humans ; Mutation ; Neoplasms/genetics ; Rothmund-Thomson Syndrome/genetics ; Werner Syndrome ; Xeroderma Pigmentosum/genetics
Chemical Substances	DNA Helicases (EC 3.6.4.-)
Language	English
Publishing date	2012-11-17
Publishing country	United States
Document type	Journal Article
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-1-4614-5037-5_6
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Article ; Online: Protein degradation pathways regulate the functions of helicases in the DNA damage response and maintenance of genomic stability.

Sommers, Joshua A / Suhasini, Avvaru N / Brosh, Robert M

Biomolecules

2015 Volume 5, Issue 2, Page(s) 590–616

Abstract: Degradation of helicases or helicase-like proteins, often mediated by ubiquitin-proteasomal pathways, plays important regulatory roles in cellular mechanisms that respond to DNA damage or replication stress. The Bloom's syndrome helicase (BLM) provides ... ...

Abstract	Degradation of helicases or helicase-like proteins, often mediated by ubiquitin-proteasomal pathways, plays important regulatory roles in cellular mechanisms that respond to DNA damage or replication stress. The Bloom's syndrome helicase (BLM) provides an example of how helicase degradation pathways, regulated by post-translational modifications and protein interactions with components of the Fanconi Anemia (FA) interstrand cross-link (ICL) repair pathway, influence cell cycle checkpoints, DNA repair, and replication restart. The FANCM DNA translocase can be targeted by checkpoint kinases that exert dramatic effects on FANCM stability and chromosomal integrity. Other work provides evidence that degradation of the F-box DNA helicase (FBH1) helps to balance translesion synthesis (TLS) and homologous recombination (HR) repair at blocked replication forks. Degradation of the helicase-like transcription factor (HLTF), a DNA translocase and ubiquitylating enzyme, influences the choice of post replication repair (PRR) pathway. Stability of the Werner syndrome helicase-nuclease (WRN) involved in the replication stress response is regulated by its acetylation. Turning to transcription, stability of the Cockayne Syndrome Group B DNA translocase (CSB) implicated in transcription-coupled repair (TCR) is regulated by a CSA ubiquitin ligase complex enabling recovery of RNA synthesis. Collectively, these studies demonstrate that helicases can be targeted for degradation to maintain genome homeostasis.
MeSH term(s)	Animals ; DNA Damage ; DNA Helicases/genetics ; DNA Helicases/metabolism ; DNA Repair ; Genetic Diseases, Inborn/genetics ; Genomic Instability ; Humans ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis
Chemical Substances	Proteasome Endopeptidase Complex (EC 3.4.25.1) ; DNA Helicases (EC 3.6.4.-)
Language	English
Publishing date	2015-04-21
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom5020590
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Article ; Online: Disease-causing missense mutations in human DNA helicase disorders.

Suhasini, Avvaru N / Brosh, Robert M

Mutation research

2012 Volume 752, Issue 2, Page(s) 138–152

Abstract: Helicases have important roles in nucleic acid metabolism, and their prominence is marked by the discovery of genetic disorders arising from disease-causing mutations. Missense mutations can yield unique insight to molecular functions and basis for ... ...

Abstract	Helicases have important roles in nucleic acid metabolism, and their prominence is marked by the discovery of genetic disorders arising from disease-causing mutations. Missense mutations can yield unique insight to molecular functions and basis for disease pathology. XPB or XPD missense mutations lead to Xeroderma pigmentosum, Cockayne's syndrome, Trichothiodystrophy, or COFS syndrome, suggesting that DNA repair and transcription defects are responsible for clinical heterogeneity. Complex phenotypes are also observed for RECQL4 helicase mutations responsible for Rothmund-Thomson syndrome, Baller-Gerold syndrome, or RAPADILINO. Bloom's syndrome causing missense mutations are found in the conserved helicase and RecQ C-terminal domain of BLM that interfere with helicase function. Although rare, patient-derived missense mutations in the exonuclease or helicase domain of Werner syndrome protein exist. Characterization of WRN separation-of-function mutants may provide insight to catalytic requirements for suppression of phenotypes associated with the premature aging disorder. Characterized FANCJ missense mutations associated with breast cancer or Fanconi anemia interfere with FANCJ helicase activity required for DNA repair and the replication stress response. For example, a FA patient-derived mutation in the FANCJ Iron-Sulfur domain was shown to uncouple its ATPase and translocase activity from DNA unwinding. Mutations in DDX11 (ChlR1) are responsible for Warsaw Breakage syndrome, a recently discovered autosomal recessive cohesinopathy. Ongoing and future studies will address clinically relevant helicase mutations and polymorphisms, including those that interfere with key protein interactions or exert dominant negative phenotypes (e.g., certain mutant alleles of Twinkle mitochondrial DNA helicase). Chemical rescue may be an approach to restore helicase activity in loss-of-function helicase disorders. Genetic and biochemical analyses of disease-causing missense mutations in human helicase disorders have led to new insights to the molecular defects underlying aberrant cellular and clinical phenotypes.
MeSH term(s)	Bloom Syndrome/enzymology ; Bloom Syndrome/genetics ; Bloom Syndrome/pathology ; Cockayne Syndrome/enzymology ; Cockayne Syndrome/genetics ; Cockayne Syndrome/pathology ; DNA Helicases/genetics ; Fanconi Anemia/enzymology ; Fanconi Anemia/genetics ; Fanconi Anemia/pathology ; Humans ; Mutation, Missense/genetics ; Xeroderma Pigmentosum/enzymology ; Xeroderma Pigmentosum/genetics ; Xeroderma Pigmentosum/pathology
Chemical Substances	DNA Helicases (EC 3.6.4.-)
Language	English
Publishing date	2012-12-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	206607-5
ISSN	1873-135X ; 1383-5718 ; 0027-5107 ; 0165-1110 ; 0165-1161 ; 0165-7992 ; 0921-8777 ; 0165-1218 ; 1383-5726 ; 0167-8817 ; 0921-8734 ; 1383-5742
ISSN (online)	1873-135X
ISSN	1383-5718 ; 0027-5107 ; 0165-1110 ; 0165-1161 ; 0165-7992 ; 0921-8777 ; 0165-1218 ; 1383-5726 ; 0167-8817 ; 0921-8734 ; 1383-5742
DOI	10.1016/j.mrrev.2012.12.004
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Article: Fanconi anemia and Bloom's syndrome crosstalk through FANCJ-BLM helicase interaction.

Suhasini, Avvaru N / Brosh, Robert M

Trends in genetics : TIG

2011 Volume 28, Issue 1, Page(s) 7–13

Abstract: Fanconi anemia (FA) and Bloom's syndrome (BS) are rare hereditary chromosomal instability disorders. FA displays bone marrow failure, acute myeloid leukemia, and head and neck cancers, whereas BS is characterized by growth retardation, immunodeficiency, ... ...

Abstract	Fanconi anemia (FA) and Bloom's syndrome (BS) are rare hereditary chromosomal instability disorders. FA displays bone marrow failure, acute myeloid leukemia, and head and neck cancers, whereas BS is characterized by growth retardation, immunodeficiency, and a wide spectrum of cancers. The BLM gene mutated in BS encodes a DNA helicase that functions in a protein complex to suppress sister-chromatid exchange. Of the 15 FA genetic complementation groups implicated in interstrand crosslink repair, FANCJ encodes a DNA helicase involved in recombinational repair and replication stress response. Based on evidence that BLM and FANCJ interact we suggest that crosstalk between BLM and FA pathways is more complex than previously thought. We propose testable models for how FANCJ and BLM coordinate to help cells deal with stalled replication forks or double-strand breaks (DSB). Understanding how BLM and FANCJ cooperate will help to elucidate an important pathway for maintaining genomic stability.
MeSH term(s)	Basic-Leucine Zipper Transcription Factors/genetics ; Basic-Leucine Zipper Transcription Factors/metabolism ; Bloom Syndrome/enzymology ; Bloom Syndrome/genetics ; Chromosomal Instability ; Fanconi Anemia/enzymology ; Fanconi Anemia/genetics ; Fanconi Anemia Complementation Group Proteins/genetics ; Fanconi Anemia Complementation Group Proteins/metabolism ; Humans ; Protein Binding ; RecQ Helicases/genetics ; RecQ Helicases/metabolism
Chemical Substances	BACH1 protein, human ; Basic-Leucine Zipper Transcription Factors ; Fanconi Anemia Complementation Group Proteins ; Bloom syndrome protein (EC 3.6.1.-) ; RecQ Helicases (EC 3.6.4.12)
Language	English
Publishing date	2011-10-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	619240-3
ISSN	1362-4555 ; 0168-9525 ; 0168-9479
ISSN (online)	1362-4555
ISSN	0168-9525 ; 0168-9479
DOI	10.1016/j.tig.2011.09.003
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Article: Safety and Pharmacodynamics of the PDE4 Inhibitor Roflumilast in Advanced B-cell Malignancies.

Kelly, Kevin / Mejia, Alex / Suhasini, Avvaru N / Lin, An-Ping / Kuhn, John / Karnad, Anand B / Weitman, Steven / Aguiar, Ricardo C T

Clinical cancer research : an official journal of the American Association for Cancer Research

2017 Volume 23, Issue 5, Page(s) 1186–1192

Abstract: Purpose: ...

Abstract	Purpose:
Language	English
Publishing date	2017-03-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	1225457-5
ISSN	1557-3265 ; 1078-0432
ISSN (online)	1557-3265
ISSN	1078-0432
DOI	10.1158/1078-0432.CCR-16-1207
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Article ; Online: Mechanistic and biological aspects of helicase action on damaged DNA.

Suhasini, Avvaru N / Brosh, Robert M

Cell cycle (Georgetown, Tex.)

2010 Volume 9, Issue 12, Page(s) 2317–2329

Abstract: Helicases catalytically unwind structured nucleic acids in a nucleoside-triphosphate-dependent and directionally specific manner, and are essential for virtually all aspects of nucleic acid metabolism. ATPase-driven helicases which translocate along ... ...

Abstract	Helicases catalytically unwind structured nucleic acids in a nucleoside-triphosphate-dependent and directionally specific manner, and are essential for virtually all aspects of nucleic acid metabolism. ATPase-driven helicases which translocate along nucleic acids play a role in damage recognition or unwinding of a DNA tract containing the lesion. Although classical biochemical experiments provided evidence that bulky covalent adducts inhibit DNA unwinding catalyzed by certain DNA helicases in a strand-specific manner (i.e., block to DNA unwinding restricted to adduct residence in the strand the helicase translocates), recent studies suggest more complex arrangements that may depend on the helicase under study, its assembly in a protein complex, and the type of structural DNA perturbation. Moreover, base and sugar phosphate backbone modifications exert effects on DNA helicases that suggest specialized tracking mechanisms. As a component of the replication stress response, the single-stranded DNA binding protein Replication Protein A (RPA) may serve to enable eukaryotic DNA helicases to overcome certain base lesions. Helicases play important roles in DNA damage signaling which also involve their partnership with RPA. In this review, we will discuss our current understanding of mechanistic and biological aspects of helicase action on damaged DNA.
MeSH term(s)	DNA/chemistry ; DNA/genetics ; DNA/metabolism ; DNA Damage ; DNA Helicases/genetics ; DNA Helicases/metabolism ; DNA Repair ; DNA Replication ; DNA, Single-Stranded/chemistry ; DNA, Single-Stranded/genetics ; Humans
Chemical Substances	DNA, Single-Stranded ; DNA (9007-49-2) ; DNA Helicases (EC 3.6.4.-)
Language	English
Publishing date	2010-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.4161/cc.9.12.11902
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Article ; Online: Protein Degradation Pathways Regulate the Functions of Helicases in the DNA Damage Response and Maintenance of Genomic Stability

Joshua A. Sommers / Avvaru N. Suhasini / Robert M. Brosh

Biomolecules, Vol 5, Iss 2, Pp 590-

2015 Volume 616

Abstract	Degradation of helicases or helicase-like proteins, often mediated by ubiquitin-proteasomal pathways, plays important regulatory roles in cellular mechanisms that respond to DNA damage or replication stress. The Bloom’s syndrome helicase (BLM) provides an example of how helicase degradation pathways, regulated by post-translational modifications and protein interactions with components of the Fanconi Anemia (FA) interstrand cross-link (ICL) repair pathway, influence cell cycle checkpoints, DNA repair, and replication restart. The FANCM DNA translocase can be targeted by checkpoint kinases that exert dramatic effects on FANCM stability and chromosomal integrity. Other work provides evidence that degradation of the F-box DNA helicase (FBH1) helps to balance translesion synthesis (TLS) and homologous recombination (HR) repair at blocked replication forks. Degradation of the helicase-like transcription factor (HLTF), a DNA translocase and ubiquitylating enzyme, influences the choice of post replication repair (PRR) pathway. Stability of the Werner syndrome helicase-nuclease (WRN) involved in the replication stress response is regulated by its acetylation. Turning to transcription, stability of the Cockayne Syndrome Group B DNA translocase (CSB) implicated in transcription-coupled repair (TCR) is regulated by a CSA ubiquitin ligase complex enabling recovery of RNA synthesis. Collectively, these studies demonstrate that helicases can be targeted for degradation to maintain genome homeostasis.
Keywords	helicase ; DNA damage response ; proteasome ; ubiquitin ; phosphorylation ; acetylation ; post-translational modification ; Bloom’s syndrome ; Fanconi Anemia ; Cockayne syndrome ; Werner syndrome ; Biology (General) ; QH301-705.5 ; Science ; Q
Subject code	570 ; 612
Language	English
Publishing date	2015-04-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article: Fanconi anemia and Bloom's syndrome crosstalk through FANCJ–BLM helicase interaction

Suhasini, Avvaru N / Brosh, Robert M., Jr

Trends in genetics. 2012 Jan., v. 28, no. 1

2012

Abstract	Fanconi anemia (FA) and Bloom's syndrome (BS) are rare hereditary chromosomal instability disorders. FA displays bone marrow failure, acute myeloid leukemia, and head and neck cancers, whereas BS is characterized by growth retardation, immunodeficiency, and a wide spectrum of cancers. The BLM gene mutated in BS encodes a DNA helicase that functions in a protein complex to suppress sister-chromatid exchange. Of the 15 FA genetic complementation groups implicated in interstrand crosslink repair, FANCJ encodes a DNA helicase involved in recombinational repair and replication stress response. Based on evidence that BLM and FANCJ interact we suggest that crosstalk between BLM and FA pathways is more complex than previously thought. We propose testable models for how FANCJ and BLM coordinate to help cells deal with stalled replication forks or double-strand breaks (DSB). Understanding how BLM and FANCJ cooperate will help to elucidate an important pathway for maintaining genomic stability.
Keywords	anemia ; immunosuppression ; stress response ; models ; head ; neck ; bone marrow ; genetic complementation ; genes ; growth retardation ; DNA helicases ; myeloid leukemia
Language	English
Dates of publication	2012-01
Size	p. 7-13.
Publishing place	Elsevier Ltd
Document type	Article
Note	2019-12-04
ZDB-ID	619240-3
ISSN	1362-4555 ; 0168-9525 ; 0168-9479
ISSN (online)	1362-4555
ISSN	0168-9525 ; 0168-9479
DOI	10.1016/j.tig.2011.09.003
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Article: Onconase action on tRNA(Lys3), the primer for HIV-1 reverse transcription.

Suhasini, Avvaru N / Sirdeshmukh, Ravi

Biochemical and biophysical research communications

2007 Volume 363, Issue 2, Page(s) 304–309

Abstract: Onconase, a cytotoxic and antitumor RNase inhibits viral replication in chronically HIV-1-infected human cells under sub lethal concentrations. Cellular tRNA has been implicated as the target for onconase action. We have recently shown that onconase ... ...

Abstract	Onconase, a cytotoxic and antitumor RNase inhibits viral replication in chronically HIV-1-infected human cells under sub lethal concentrations. Cellular tRNA has been implicated as the target for onconase action. We have recently shown that onconase cleaves selectively at GG residues in the UGG context in the variable loop and D-arm of the tRNA substrates. We therefore examined onconase cleavage specificity in in vitro transcribed tRNA(Lys3), which is the primer for HIV-1 reverse transcription but does not have UGG anywhere in its sequence. Onconase was found to cleave tRNA(Lys3) predominantly at the GG residues in the GGG triplet present in the variable loop. Mutations at this site did not effect onconase cleavages. Interestingly thus, onconase seems to cleave predominantly in the variable loop of tRNA(Lys3) regardless of the sequence context implying possible contribution of even structural determinants for its selective cleavages.
MeSH term(s)	Binding Sites ; DNA Primers/chemistry ; DNA Primers/metabolism ; HIV Reverse Transcriptase/chemistry ; HIV Reverse Transcriptase/metabolism ; HIV Reverse Transcriptase/ultrastructure ; Models, Chemical ; Models, Molecular ; Protein Binding ; RNA, Transfer/chemistry ; RNA, Transfer/metabolism ; RNA, Transfer/ultrastructure ; Reverse Transcription/physiology ; Ribonucleases/chemistry ; Ribonucleases/metabolism ; Ribonucleases/ultrastructure ; Substrate Specificity
Chemical Substances	DNA Primers ; RNA, Transfer (9014-25-9) ; HIV Reverse Transcriptase (EC 2.7.7.49) ; Ribonucleases (EC 3.1.-) ; ranpirnase (ZE15FIT23E)
Language	English
Publishing date	2007-11-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2007.08.157
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Article: Transfer RNA cleavages by onconase reveal unusual cleavage sites.

Suhasini, Avvaru N / Sirdeshmukh, Ravi

The Journal of biological chemistry

2006 Volume 281, Issue 18, Page(s) 12201–12209

Abstract: Onconase, a protein from amphibian eggs and a homologue of pancreatic ribonuclease (RNase) superfamily, is cytotoxic, exhibits antitumor and antiviral activity, and is in phase III clinical trials. It has been shown to predominantly target cellular tRNA ... ...

Abstract	Onconase, a protein from amphibian eggs and a homologue of pancreatic ribonuclease (RNase) superfamily, is cytotoxic, exhibits antitumor and antiviral activity, and is in phase III clinical trials. It has been shown to predominantly target cellular tRNA on its entry into mammalian cells (Saxena, S. K., Sirdeshmukh, R., Ardelt, W., Mikulski, S. M., Shogen, K., and Youle, R. J. (2002) J. Biol. Chem. 277, 15142-15146). Cleavage site mapping using natural tRNA substrates, in vitro, revealed predominant cleavage sites at UG and GG residues. Cleavages at UG or the less intense cleavages at CG sites are consistent with the known base specificity of onconase. However, predominance of cleavages at selected G-G bonds is unusual for a homologue of pancreatic RNases. Interestingly, in at least three of the four tRNA substrates studied, the predominant cleavages mapped in the triplet UGG located in the context of the variable loop or the D-arm of the tRNA. The cleavage specificity of onconase observed by us thus indicates another special feature of this enzyme, which may be relevant to its cellular actions.
MeSH term(s)	Animals ; Base Sequence ; Escherichia coli/metabolism ; Male ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Synthesis Inhibitors/metabolism ; RNA/chemistry ; RNA, Transfer/chemistry ; RNA, Transfer/metabolism ; Rabbits ; Reticulocytes/metabolism ; Ribonuclease, Pancreatic/chemistry ; Ribonucleases/chemistry ; Ribonucleases/physiology
Chemical Substances	Protein Synthesis Inhibitors ; RNA (63231-63-0) ; RNA, Transfer (9014-25-9) ; Ribonucleases (EC 3.1.-) ; Ribonuclease, Pancreatic (EC 3.1.27.5) ; ranpirnase (ZE15FIT23E)
Language	English
Publishing date	2006-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M504488200
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