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Article ; Online: RNA binding protein-mediated post-transcriptional gene regulation in medulloblastoma.

Bish, Rebecca / Vogel, Christine

2014 Volume 37, Issue 5, Page(s) 357–364

Abstract: Medulloblastoma, the most common malignant brain tumor in children, is a disease whose mechanisms are now beginning to be uncovered by high-throughput studies of somatic mutations, mRNA expression patterns, and epigenetic profiles of patient tumors. One ... ...

Abstract	Medulloblastoma, the most common malignant brain tumor in children, is a disease whose mechanisms are now beginning to be uncovered by high-throughput studies of somatic mutations, mRNA expression patterns, and epigenetic profiles of patient tumors. One emerging theme from studies that sequenced the tumor genomes of large cohorts of medulloblastoma patients is frequent mutation of RNA binding proteins. Proteins which bind multiple RNA targets can act as master regulators of gene expression at the post-transcriptional level to co-ordinate cellular processes and alter the phenotype of the cell. Identification of the target genes of RNA binding proteins may highlight essential pathways of medulloblastomagenesis that cannot be detected by study of transcriptomics alone. Furthermore, a subset of RNA binding proteins are attractive drug targets. For example, compounds that are under development as anti-viral targets due to their ability to inhibit RNA helicases could also be tested in novel approaches to medulloblastoma therapy by targeting key RNA binding proteins. In this review, we discuss a number of RNA binding proteins, including Musashi1 (MSI1), DEAD (Asp-Glu-Ala-Asp) box helicase 3 X-linked (DDX3X), DDX31, and cell division cycle and apoptosis regulator 1 (CCAR1), which play potentially critical roles in the growth and/or maintenance of medulloblastoma.
MeSH term(s)	Animals ; Apoptosis Regulatory Proteins/physiology ; Cell Cycle Proteins/physiology ; Cerebellar Neoplasms/genetics ; Cerebellar Neoplasms/metabolism ; DEAD-box RNA Helicases/physiology ; Gene Expression Regulation, Neoplastic ; Humans ; Medulloblastoma/genetics ; Medulloblastoma/metabolism ; Nerve Tissue Proteins/physiology ; Protein Biosynthesis ; RNA Interference ; RNA-Binding Proteins/physiology
Chemical Substances	Apoptosis Regulatory Proteins ; CCAR1 protein, human ; Cell Cycle Proteins ; MSI1 protein, human ; Nerve Tissue Proteins ; RNA-Binding Proteins ; DDX31 protein, human (EC 3.6.1.-) ; DDX3X protein, human (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2014-03-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1148964-9
ISSN	0219-1032 ; 1016-8478
ISSN (online)	0219-1032
ISSN	1016-8478
DOI	10.14348/molcells.2014.0008
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Article ; Online: Surface Charge Measurements with Scanning Ion Conductance Microscopy Provide Insights into Nitrous Acid Speciation at the Kaolin Mineral-Air Interface.

Zhu, Cheng / Jagdale, Gargi / Gandolfo, Adrien / Alanis, Kristen / Abney, Rebecca / Zhou, Lushan / Bish, David / Raff, Jonathan D / Baker, Lane A

Environmental science & technology

2021 Volume 55, Issue 18, Page(s) 12233–12242

Abstract: Unique surface properties of aluminosilicate clay minerals arise from anisotropic distribution of surface charge across their layered structures. Yet, a molecular-level understanding of clay mineral surfaces has been hampered by the lack of analytical ... ...

Abstract	Unique surface properties of aluminosilicate clay minerals arise from anisotropic distribution of surface charge across their layered structures. Yet, a molecular-level understanding of clay mineral surfaces has been hampered by the lack of analytical techniques capable of measuring surface charges at the nanoscale. This is important for understanding the reactivity, colloidal stability, and ion-exchange capacity properties of clay minerals, which constitute a major fraction of global soils. In this work, scanning ion conductance microscopy (SICM) is used for the first time to visualize the surface charge and topography of dickite, a well-ordered member of the kaolin subgroup of clay minerals. Dickite displayed a pH-independent negative charge on basal surfaces whereas the positive charge on edges increased from pH 6 to 3. Surface charges responded to malonate addition, which promoted dissolution/precipitation reactions. Results from SICM were used to interpret heterogeneous reactivity studies showing that gas-phase nitrous acid (HONO) is released from the protonation of nitrite at Al-OH
MeSH term(s)	Clay ; Kaolin ; Microscopy ; Minerals ; Nitrous Acid
Chemical Substances	Minerals ; Kaolin (24H4NWX5CO) ; Clay (T1FAD4SS2M) ; Nitrous Acid (T2I5UM75DN)
Language	English
Publishing date	2021-08-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1520-5851
ISSN (online)	1520-5851
DOI	10.1021/acs.est.1c03455
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Article: Surface Charge Measurements with Scanning Ion Conductance Microscopy Provide Insights into Nitrous Acid Speciation at the Kaolin Mineral–Air Interface

Zhu, Cheng / Jagdale, Gargi / Gandolfo, Adrien / Alanis, Kristen / Abney, Rebecca / Zhou, Lushan / Bish, David / Raff, Jonathan D. / Baker, Lane A.

Environmental science & technology. 2021 Aug. 27, v. 55, no. 18

2021

Abstract	Unique surface properties of aluminosilicate clay minerals arise from anisotropic distribution of surface charge across their layered structures. Yet, a molecular-level understanding of clay mineral surfaces has been hampered by the lack of analytical techniques capable of measuring surface charges at the nanoscale. This is important for understanding the reactivity, colloidal stability, and ion-exchange capacity properties of clay minerals, which constitute a major fraction of global soils. In this work, scanning ion conductance microscopy (SICM) is used for the first time to visualize the surface charge and topography of dickite, a well-ordered member of the kaolin subgroup of clay minerals. Dickite displayed a pH-independent negative charge on basal surfaces whereas the positive charge on edges increased from pH 6 to 3. Surface charges responded to malonate addition, which promoted dissolution/precipitation reactions. Results from SICM were used to interpret heterogeneous reactivity studies showing that gas-phase nitrous acid (HONO) is released from the protonation of nitrite at Al–OH₂⁺ groups on dickite edges at pH well above the aqueous pKₐ of HONO. This study provides nanoscale insights into mineral surface processes that affect environmental processes on the local and global scale.
Keywords	anisotropy ; clay ; environmental science ; ion exchange capacity ; kaolin ; microscopy ; nitrites ; nitrous acid ; pH ; protonation ; topography
Language	English
Dates of publication	2021-0827
Size	p. 12233-12242.
Publishing place	American Chemical Society
Document type	Article
ISSN	1520-5851
DOI	10.1021/acs.est.1c03455
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Article: Werner helicase-interacting protein 1 binds polyubiquitin via its zinc finger domain.

Bish, Rebecca A / Myers, Michael P

The Journal of biological chemistry

2007 Volume 282, Issue 32, Page(s) 23184–23193

Abstract: DNA repair is regulated on many levels by ubiquitination. In order to identify novel connections between DNA repair pathways and ubiquitin signaling, we used mass spectrometry to identify proteins that interact with lysine 6-linked polyubiquitin chains. ... ...

Abstract	DNA repair is regulated on many levels by ubiquitination. In order to identify novel connections between DNA repair pathways and ubiquitin signaling, we used mass spectrometry to identify proteins that interact with lysine 6-linked polyubiquitin chains. From this proteomic screen, we identified the DNA repair protein WRNIP1 (Werner helicase-interacting protein 1), along with nucleosome assembly protein 1, as novel ubiquitin-interacting proteins. We found that a small zinc finger domain at the N terminus of WRNIP1 is sufficient and necessary for noncovalent ubiquitin binding. This ubiquitin-binding zinc finger (UBZ) domain binds polyubiquitin but not monoubiquitin and appears to show no specificity for polyubiquitin chain linkage. A homologous zinc finger domain in RAD18 also binds polyubiquitin, suggesting a wider role for the UBZ domain in DNA repair. The WRNIP1 ubiquitin-binding function, along with its previously established ATPase activity, suggests that WRNIP1 plays a role in the metabolism of ubiquitinated proteins. Supporting this model, deletion of MGS1, the yeast homolog of WRNIP1, slows the rate of ubiquitin turnover, rendering yeast resistant to cycloheximide. We also find that WRNIP1 is heavily modified with ubiquitin and SUMO, revealing complex layers in the involvement of ubiquitin pathway proteins in the regulation of DNA repair. The novel ubiquitin-binding ability of WRNIP1 sheds light on the role of UBZ domain-containing proteins in postreplication DNA repair.
MeSH term(s)	ATPases Associated with Diverse Cellular Activities ; Amino Acid Sequence ; Carrier Proteins/metabolism ; Carrier Proteins/physiology ; Cycloheximide/chemistry ; DNA Repair ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/physiology ; Humans ; Lysine/chemistry ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Protein Synthesis Inhibitors/pharmacology ; Signal Transduction ; Ubiquitin/chemistry ; Zinc Fingers
Chemical Substances	Carrier Proteins ; DNA-Binding Proteins ; Protein Synthesis Inhibitors ; Ubiquitin ; Cycloheximide (98600C0908) ; WRNIP1 protein, human (EC 3.6.1.3) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2007-06-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.M701042200
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Article ; Online: Comprehensive Protein Interactome Analysis of a Key RNA Helicase: Detection of Novel Stress Granule Proteins.

Bish, Rebecca / Cuevas-Polo, Nerea / Cheng, Zhe / Hambardzumyan, Dolores / Munschauer, Mathias / Landthaler, Markus / Vogel, Christine

Biomolecules

2015 Volume 5, Issue 3, Page(s) 1441–1466

Abstract: DDX6 (p54/RCK) is a human RNA helicase with central roles in mRNA decay and translation repression. To help our understanding of how DDX6 performs these multiple functions, we conducted the first unbiased, large-scale study to map the DDX6-centric ... ...

Abstract	DDX6 (p54/RCK) is a human RNA helicase with central roles in mRNA decay and translation repression. To help our understanding of how DDX6 performs these multiple functions, we conducted the first unbiased, large-scale study to map the DDX6-centric protein-protein interactome using immunoprecipitation and mass spectrometry. Using DDX6 as bait, we identify a high-confidence and high-quality set of protein interaction partners which are enriched for functions in RNA metabolism and ribosomal proteins. The screen is highly specific, maximizing the number of true positives, as demonstrated by the validation of 81% (47/58) of the RNA-independent interactors through known functions and interactions. Importantly, we minimize the number of indirect interaction partners through use of a nuclease-based digestion to eliminate RNA. We describe eleven new interactors, including proteins involved in splicing which is an as-yet unknown role for DDX6. We validated and characterized in more detail the interaction of DDX6 with Nuclear fragile X mental retardation-interacting protein 2 (NUFIP2) and with two previously uncharacterized proteins, FAM195A and FAM195B (here referred to as granulin-1 and granulin-2, or GRAN1 and GRAN2). We show that NUFIP2, GRAN1, and GRAN2 are not P-body components, but re-localize to stress granules upon exposure to stress, suggesting a function in translation repression in the cellular stress response. Using a complementary analysis that resolved DDX6's multiple complex memberships, we further validated these interaction partners and the presence of splicing factors. As DDX6 also interacts with the E3 SUMO ligase TIF1β, we tested for and observed a significant enrichment of sumoylation amongst DDX6's interaction partners. Our results represent the most comprehensive screen for direct interaction partners of a key regulator of RNA life cycle and localization, highlighting new stress granule components and possible DDX6 functions-many of which are likely conserved across eukaryotes.
MeSH term(s)	Cytosol/metabolism ; DEAD-box RNA Helicases/metabolism ; HEK293 Cells ; Heat-Shock Response ; Humans ; Oxidative Stress ; Protein Interaction Mapping ; Protein Transport ; Proto-Oncogene Proteins/metabolism
Chemical Substances	Proto-Oncogene Proteins ; DDX6 protein, human (EC 3.6.1.-) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2015-07-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom5031441
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Article: Conjugation of complex polyubiquitin chains to WRNIP1.

Bish, Rebecca A / Fregoso, Oliver I / Piccini, Antonella / Myers, Michael P

Journal of proteome research

2008 Volume 7, Issue 8, Page(s) 3481–3489

Abstract: Werner helicase interacting protein 1 (WRNIP1) is a ubiquitin-binding protein that undergoes extensive post-translational modification including ubiquitination, sumoylation, and phosphorylation. These post-translational modifications are expected to ... ...

Abstract	Werner helicase interacting protein 1 (WRNIP1) is a ubiquitin-binding protein that undergoes extensive post-translational modification including ubiquitination, sumoylation, and phosphorylation. These post-translational modifications are expected to regulate the function of WRNIP1 in the DNA damage response. In this study, we use a denaturing tandem affinity purification technique along with mass spectrometry to show that, unlike most ubiquitin-binding proteins, WRNIP1 is polyubiquitinated. WRNIP1 polyubiquitination is reminiscent of the well-characterized phenomenon of the coupled monoubiquitination of ubiquitin-binding proteins in that this polyubiquitination is dependent on the presence of an intact ubiquitin-binding domain. The polyubiquitin chains conjugated to WRNIP1 are linked through lysines 11, 48, and 63. This study presents the first evidence for the conjugation of K11-K48-K63 polyubiquitin chains to a specific substrate in vivo. Polyubiquitination is likely to regulate WRNIP1's function in the DNA damage response, as UV radiation induces the hyperubiquitination of WRNIP1. Polyubiquitination with noncanonical intraubiquitin linkages may represent a unique mode of regulation of UBZ domain-containing proteins.
MeSH term(s)	ATPases Associated with Diverse Cellular Activities ; Animals ; Carrier Proteins/metabolism ; Cell Line ; Chromatography, Liquid ; DNA Damage ; DNA-Binding Proteins/metabolism ; Humans ; Mice ; Polyubiquitin/metabolism ; Protein Conformation ; Protein Processing, Post-Translational ; Spectrometry, Mass, Electrospray Ionization ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Ubiquitination ; Ultraviolet Rays
Chemical Substances	Carrier Proteins ; DNA-Binding Proteins ; Polyubiquitin (120904-94-1) ; WRNIP1 protein, human (EC 3.6.1.3) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-)
Language	English
Publishing date	2008-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2078618-9
ISSN	1535-3893
ISSN	1535-3893
DOI	10.1021/pr800217q
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Zs.A 6189: Show issues

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Article ; Online: Comprehensive Protein Interactome Analysis of a Key RNA Helicase

Rebecca Bish / Nerea Cuevas-Polo / Zhe Cheng / Dolores Hambardzumyan / Mathias Munschauer / Markus Landthaler / Christine Vogel

Biomolecules, Vol 5, Iss 3, Pp 1441-

Detection of Novel Stress Granule Proteins

2015 Volume 1466

Abstract	DDX6 (p54/RCK) is a human RNA helicase with central roles in mRNA decay and translation repression. To help our understanding of how DDX6 performs these multiple functions, we conducted the first unbiased, large-scale study to map the DDX6-centric protein-protein interactome using immunoprecipitation and mass spectrometry. Using DDX6 as bait, we identify a high-confidence and high-quality set of protein interaction partners which are enriched for functions in RNA metabolism and ribosomal proteins. The screen is highly specific, maximizing the number of true positives, as demonstrated by the validation of 81% (47/58) of the RNA-independent interactors through known functions and interactions. Importantly, we minimize the number of indirect interaction partners through use of a nuclease-based digestion to eliminate RNA. We describe eleven new interactors, including proteins involved in splicing which is an as-yet unknown role for DDX6. We validated and characterized in more detail the interaction of DDX6 with Nuclear fragile X mental retardation-interacting protein 2 (NUFIP2) and with two previously uncharacterized proteins, FAM195A and FAM195B (here referred to as granulin-1 and granulin-2, or GRAN1 and GRAN2). We show that NUFIP2, GRAN1, and GRAN2 are not P-body components, but re-localize to stress granules upon exposure to stress, suggesting a function in translation repression in the cellular stress response. Using a complementary analysis that resolved DDX6’s multiple complex memberships, we further validated these interaction partners and the presence of splicing factors. As DDX6 also interacts with the E3 SUMO ligase TIF1β, we tested for and observed a significant enrichment of sumoylation amongst DDX6’s interaction partners. Our results represent the most comprehensive screen for direct interaction partners of a key regulator of RNA life cycle and localization, highlighting new stress granule components and possible DDX6 functions—many of which are likely conserved across eukaryotes.
Keywords	DDX6 ; post-transcriptional regulation ; protein interactions ; SUMOylation ; NUFIP2 ; FAM195A ; FAM195B ; stress granules ; P bodies ; mRNA degradation ; Biology (General) ; QH301-705.5 ; Science ; Q
Subject code	580
Language	English
Publishing date	2015-07-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Comprehensive Protein Interactome Analysis of a Key RNA Helicase

Rebecca Bish / Nerea Cuevas-Polo / Zhe Cheng / Dolores Hambardzumyan / Mathias Munschauer / Markus Landthaler / Christine Vogel

Biomolecules, Vol 5, Iss 3, Pp 1441-

Detection of Novel Stress Granule Proteins

2015 Volume 1466

Abstract	DDX6 (p54/RCK) is a human RNA helicase with central roles in mRNA decay and translation repression. To help our understanding of how DDX6 performs these multiple functions, we conducted the first unbiased, large-scale study to map the DDX6-centric protein-protein interactome using immunoprecipitation and mass spectrometry. Using DDX6 as bait, we identify a high-confidence and high-quality set of protein interaction partners which are enriched for functions in RNA metabolism and ribosomal proteins. The screen is highly specific, maximizing the number of true positives, as demonstrated by the validation of 81% (47/58) of the RNA-independent interactors through known functions and interactions. Importantly, we minimize the number of indirect interaction partners through use of a nuclease-based digestion to eliminate RNA. We describe eleven new interactors, including proteins involved in splicing which is an as-yet unknown role for DDX6. We validated and characterized in more detail the interaction of DDX6 with Nuclear fragile X mental retardation-interacting protein 2 (NUFIP2) and with two previously uncharacterized proteins, FAM195A and FAM195B (here referred to as granulin-1 and granulin-2, or GRAN1 and GRAN2). We show that NUFIP2, GRAN1, and GRAN2 are not P-body components, but re-localize to stress granules upon exposure to stress, suggesting a function in translation repression in the cellular stress response. Using a complementary analysis that resolved DDX6’s multiple complex memberships, we further validated these interaction partners and the presence of splicing factors. As DDX6 also interacts with the E3 SUMO ligase TIF1β, we tested for and observed a significant enrichment of sumoylation amongst DDX6’s interaction partners. Our results represent the most comprehensive screen for direct interaction partners of a key regulator of RNA life cycle and localization, highlighting new stress granule components and possible DDX6 functions—many of which are likely conserved across eukaryotes.
Keywords	DDX6 ; post-transcriptional regulation ; protein interactions ; SUMOylation ; NUFIP2 ; FAM195A ; FAM195B ; stress granules ; P bodies ; mRNA degradation ; Biology (General) ; QH301-705.5 ; Science ; Q
Subject code	580
Language	English
Publishing date	2015-07-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Comprehensive Protein Interactome Analysis of a Key RNA Helicase

Rebecca Bish / Nerea Cuevas-Polo / Zhe Cheng / Dolores Hambardzumyan / Mathias Munschauer / Markus Landthaler / Christine Vogel

Biomolecules, Vol 5, Iss 3, Pp 1441-

Detection of Novel Stress Granule Proteins

2015 Volume 1466

Abstract	DDX6 (p54/RCK) is a human RNA helicase with central roles in mRNA decay and translation repression. To help our understanding of how DDX6 performs these multiple functions, we conducted the first unbiased, large-scale study to map the DDX6-centric protein-protein interactome using immunoprecipitation and mass spectrometry. Using DDX6 as bait, we identify a high-confidence and high-quality set of protein interaction partners which are enriched for functions in RNA metabolism and ribosomal proteins. The screen is highly specific, maximizing the number of true positives, as demonstrated by the validation of 81% (47/58) of the RNA-independent interactors through known functions and interactions. Importantly, we minimize the number of indirect interaction partners through use of a nuclease-based digestion to eliminate RNA. We describe eleven new interactors, including proteins involved in splicing which is an as-yet unknown role for DDX6. We validated and characterized in more detail the interaction of DDX6 with Nuclear fragile X mental retardation-interacting protein 2 (NUFIP2) and with two previously uncharacterized proteins, FAM195A and FAM195B (here referred to as granulin-1 and granulin-2, or GRAN1 and GRAN2). We show that NUFIP2, GRAN1, and GRAN2 are not P-body components, but re-localize to stress granules upon exposure to stress, suggesting a function in translation repression in the cellular stress response. Using a complementary analysis that resolved DDX6’s multiple complex memberships, we further validated these interaction partners and the presence of splicing factors. As DDX6 also interacts with the E3 SUMO ligase TIF1β, we tested for and observed a significant enrichment of sumoylation amongst DDX6’s interaction partners. Our results represent the most comprehensive screen for direct interaction partners of a key regulator of RNA life cycle and localization, highlighting new stress granule components and possible DDX6 functions—many of which are likely conserved across eukaryotes.
Keywords	DDX6 ; post-transcriptional regulation ; protein interactions ; SUMOylation ; NUFIP2 ; FAM195A ; FAM195B ; stress granules ; P bodies ; mRNA degradation ; Biology (General) ; QH301-705.5 ; Science ; Q
Subject code	580
Language	English
Publishing date	2015-07-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Cognitive skills, student achievement tests, and schools.

Finn, Amy S / Kraft, Matthew A / West, Martin R / Leonard, Julia A / Bish, Crystal E / Martin, Rebecca E / Sheridan, Margaret A / Gabrieli, Christopher F O / Gabrieli, John D E

Psychological science

2014 Volume 25, Issue 3, Page(s) 736–744

Abstract: Cognitive skills predict academic performance, so schools that improve academic performance might also improve cognitive skills. To investigate the impact schools have on both academic performance and cognitive skills, we related standardized achievement- ...

Abstract	Cognitive skills predict academic performance, so schools that improve academic performance might also improve cognitive skills. To investigate the impact schools have on both academic performance and cognitive skills, we related standardized achievement-test scores to measures of cognitive skills in a large sample (N = 1,367) of eighth-grade students attending traditional, exam, and charter public schools. Test scores and gains in test scores over time correlated with measures of cognitive skills. Despite wide variation in test scores across schools, differences in cognitive skills across schools were negligible after we controlled for fourth-grade test scores. Random offers of enrollment to oversubscribed charter schools resulted in positive impacts of such school attendance on math achievement but had no impact on cognitive skills. These findings suggest that schools that improve standardized achievement-test scores do so primarily through channels other than improving cognitive skills.
MeSH term(s)	Achievement ; Adolescent ; Adolescent Development ; Child ; Child Development ; Cognition ; Education ; Educational Measurement ; Female ; Humans ; Male ; Schools
Language	English
Publishing date	2014-01-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2022256-7
ISSN	1467-9280 ; 0956-7976
ISSN (online)	1467-9280
ISSN	0956-7976
DOI	10.1177/0956797613516008
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