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A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

http://www.wikidata.org/entity/Q24301555

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Drugging the unfolded protein response in acute leukemias Drosophila as a model for unfolded protein response research Endoplasmic reticulum quality control and systemic amyloid disease: Impacting protein stability from the inside out Molecular Pathways: Immunosuppressive Roles of IRE1α-XBP1 Signaling in Dendritic Cells of the Tumor Microenvironment Tumorigenic and Immunosuppressive Effects of Endoplasmic Reticulum Stress in Cancer Unfolding anti-tumor immunity: ER stress responses sculpt tolerogenic myeloid cells in cancer New Concepts in Alpha-1 Antitrypsin Deficiency Disease Mechanisms.Identification of human short introns.RTCB-1 mediates neuroprotection via XBP-1 mRNA splicing in the unfolded protein response pathway.The RtcB RNA ligase is an essential component of the metazoan unfolded protein response.The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA and controls antibody secretion in plasma cells A novel role for protein kinase Kin2 in regulating HAC1 mRNA translocation, splicing, and translation.Cutting, dicing, healing and sealing: the molecular surgery of tRNA RNA ligation in neurons by RtcB inhibits axon regeneration.Coevolution of RtcB and Archease created a multiple-turnover RNA ligase Characterization of 3'-Phosphate RNA Ligase Paralogs RtcB1, RtcB2, and RtcB3 from Myxococcus xanthus Highlights DNA and RNA 5'-Phosphate Capping Activity of RtcB3.PERK regulated miR-424(322)-503 cluster fine-tunes activation of IRE1 and ATF6 during Unfolded Protein Response.A conformational RNA zipper promotes intron ejection during non-conventional XBP1 mRNA splicing.Autonomous translational pausing is required for XBP1u mRNA recruitment to the ER via the SRP pathway.Prostate cancer and the unfolded protein response.Multiple Mechanisms of Unfolded Protein Response-Induced Cell Death Proteostasis control by the unfolded protein response Regulation of the unfolded protein response by noncoding RNA.The Unfolded Protein Response in the Immune Cell Development: Putting the Caretaker in the Driving Seat.Cellular and molecular phenotypes depending upon the RNA repair system RtcAB of Escherichia coli.Divergence and Conservation of the Major UPR Branch IRE1-bZIP Signaling Pathway across Eukaryotes.Structural and Functional Analysis of the Allosteric Inhibition of IRE1α with ATP-Competitive Ligands.Novel mechanism of enhancing IRE1α-XBP1 signalling via the PERK-ATF4 pathway.Cleavage of 3'-terminal adenosine by archaeal ATP-dependent RNA ligase.A functional link between the co-translational protein translocation pathway and the UPR.Physiological/pathological ramifications of transcription factors in the unfolded protein response.Ire1 has distinct catalytic mechanisms for XBP1/HAC1 splicing and RIDD.Endoplasmic reticulum stress signaling and chemotherapy resistance in solid cancers.Making ends meet: a role of RNA ligase RTCB in unfolded protein response.Functional analysis of the mammalian RNA ligase for IRE1 in the unfolded protein response.Erratum: Proteostasis control by the unfolded protein response.Dual IRE1 RNase functions dictate glioblastoma development.Genetic bypass of essential RNA repair enzymes in budding yeast.Homology model of the human tRNA splicing ligase RtcB.Profiling the Dual Enzymatic Activities of the Serine/Threonine Kinase IRE1α.

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A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

http://www.wikidata.org/entity/Q24301555

description

2014 nî lūn-bûn

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2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

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2014年論文

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2014年論文

@zh-tw

2014年论文

@wuu

name

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@ast

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@en

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@en-gb

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@nl

type

label

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@ast

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@en

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@en-gb

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@nl

prefLabel

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@ast

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@en

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

@en-gb

A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

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J.MOLCEL.2014.06.032

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A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB

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Feng-Xia Liang

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Xiaozhong Wang

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Yanyan Lu

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P2860

A conditional knockout resource for the genome-wide study of mouse gene function

XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

HSPC117 is the essential subunit of a human tRNA splicing ligase complex

Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response

pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response

The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts

Analysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism.

The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule

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RNA 2',3'-cyclic phosphate and 5'-OH ligase

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4156904

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