P3373
Exonuclease hDIS3L2 specifies an exosome-independent 3'-5' degradation pathway of human cytoplasmic mRNAC16orf57, a gene mutated in poikiloderma with neutropenia, encodes a putative phosphodiesterase responsible for the U6 snRNA 3' end modificationProteomic analysis identifies a new complex required for nuclear pre-mRNA retention and splicingThe human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3LLocalisation of the human hSuv3p helicase in the mitochondrial matrix and its preferential unwinding of dsDNARNA channelling by the archaeal exosomeProteins involved in the degradation of cytoplasmic mRNA in the major eukaryotic model systemsStructure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease familyStructure of the yeast Pml1 splicing factor and its integration into the RES complexStructural and biochemical insights to the role of the CCR4-NOT complex and DDX6 ATPase in microRNA repressionThe yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitochondrial degradosome in processing and turnover of RNA.Endonucleolytic RNA cleavage by a eukaryotic exosome.Rbs1, a new protein implicated in RNA polymerase III biogenesis in yeast Saccharomyces cerevisiae.The yeast mitochondrial degradosome. Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism.RNA channelling by the eukaryotic exosome.Subunit architecture of multimeric complexes isolated directly from cells.A single subunit, Dis3, is essentially responsible for yeast exosome core activity.Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome.Probabilistic approach to predicting substrate specificity of methyltransferasesIdentification of a novel human mitochondrial endo-/exonuclease Ddk1/c20orf72 necessary for maintenance of proper 7S DNA levels.Linear mtDNA fragments and unusual mtDNA rearrangements associated with pathological deficiency of MGME1 exonuclease.Identification of protein partners in mycobacteria using a single-step affinity purification method.Characterization of the mycobacterial acyl-CoA carboxylase holo complexes reveals their functional expansion into amino acid catabolismRecent developments in the analysis of protein complexes.hUTP24 is essential for processing of the human rRNA precursor at site A1, but not at site A0DIS3 shapes the RNA polymerase II transcriptome in humans by degrading a variety of unwanted transcripts.Two novel C-terminal frameshift mutations in the β-globin gene lead to rapid mRNA decay.The architecture of the Schizosaccharomyces pombe CCR4-NOT complexHuman mitochondrial RNA decay mediated by PNPase-hSuv3 complex takes place in distinct fociFilaggrin inhibits generation of CD1a neolipid antigens by house dust mite-derived phospholipase.A new strategy for gene targeting and functional proteomics using the DT40 cell line.Perlman syndrome nuclease DIS3L2 controls cytoplasmic non-coding RNAs and provides surveillance pathway for maturing snRNAsMultiple myeloma-associated hDIS3 mutations cause perturbations in cellular RNA metabolism and suggest hDIS3 PIN domain as a potential drug target.Identification of a novel human nuclear-encoded mitochondrial poly(A) polymerase.Mechanisms of RNA degradation by the eukaryotic exosome.Novel endoribonucleases as central players in various pathways of eukaryotic RNA metabolism.The eukaryotic RNA exosome: same scaffold but variable catalytic subunits.Catalytic properties of the eukaryotic exosome.The yeast THO complex forms a 5-subunit assembly that directly interacts with active chromatin.RNA decay machines: the exosome.
P50
Q24294915-E8758C63-0D8D-4BCB-991D-9176D71DD676Q24296749-4C06B651-0EBF-4E91-B071-A0832EA3AE4FQ24317157-29EE3C68-E6C7-4DE3-B55A-E066816C8830Q24317597-0FF68F73-6F8F-44AD-A625-D6E2A293C7BEQ24323324-E378576B-877C-4639-9648-221DDDD3982FQ24671892-C2A5B33C-9225-4B48-B2E5-26671ED43B01Q26864165-FD4515E0-2A70-4F6B-88BB-EED2C4BA010CQ27650186-F5F98CDC-491D-47FC-A163-980AE37886C6Q27652991-ECBACADC-EFB2-4BF6-8AC8-7A3F39FBC34AQ27690102-0E2204CC-16B3-46BB-86CF-254CA40DEC95Q27929755-AE4CAE5B-5F16-44B5-8898-9A51B5819759Q27930673-3D2B04B1-D2B9-4633-A198-4BB53AA0F003Q27931809-A39976B5-6C17-4D55-8E19-84CEA222FE3AQ27933081-7A5D1BFD-DCC8-47CE-A89B-416EF457D849Q27933474-F3F786BB-F363-4DBE-B347-9BC4B3F0741DQ27933735-A68448C6-7241-42D4-8076-C0DA87B4E81AQ27935552-E15AB5B6-DD03-4899-B58F-DC409955DA6EQ27936839-F9BE1A31-08B9-4018-86A6-3FA57C97DD05Q27940324-491D1C44-47CE-4858-870C-11AF9C3D3688Q34324975-C34E1183-73DB-40F4-B6EA-95B230AD7057Q34427479-9E47204A-FC9C-45F5-AAEE-AC118FC10F39Q35130200-CED032EC-D58A-4AC1-A33F-618D6C49D646Q35141658-1F9E0ABF-8290-472A-B3E1-BA32323F4F86Q35620982-9D1D0A9D-B50B-45AE-A483-D5FCC90DD3F1Q36190916-C5134678-193B-4412-B64E-9B4BB0E93317Q36199560-627FFD34-7FD2-4B67-8BDB-AE837FAB5642Q36396254-F24558E7-80FC-41FE-9998-03C3A4C1DBE0Q36534273-8513A457-C229-4A82-960B-7E66C859ECADQ36559213-005F31E5-854E-4A8C-8DA4-D6E57078CB0FQ36916564-AC9AC7E1-C290-4D40-B995-501F5C0750B2Q37197853-E4688CEC-BF82-48F4-AE77-4D3C8AF9D69EQ37472950-08866344-52BE-456C-B307-F3099E18BAF8Q37518637-5A62EBD5-71AC-4FA0-BD3B-6ED2532DA4F9Q37693914-D7B5CC85-96F8-4534-8A93-005ED46C6975Q37714460-B7815B2A-E49C-41FC-B787-995C8A686B74Q37776952-760390B2-9691-4F0B-AC43-7F76EA69581DQ37834909-DDFF15B9-AC02-4FBB-829E-28F9CEDB92B9Q37895568-7C46C111-AC8E-4AFC-A16B-5850837D226FQ38042310-316E0DA3-4845-46EA-8836-0DF00D63F5E5Q38077004-00B2660E-24D4-41DA-A2CD-E45589A574A7
P50
description
Polish researcher, molecular biologist
@en
Pools onderzoeker
@nl
investigador polacu
@ast
polnischer Forscher
@de
polski naukowiec, biolog molekularny
@pl
name
Andrzej Dziembowski
@ast
Andrzej Dziembowski
@ca
Andrzej Dziembowski
@cs
Andrzej Dziembowski
@de
Andrzej Dziembowski
@en
Andrzej Dziembowski
@es
Andrzej Dziembowski
@fr
Andrzej Dziembowski
@ga
Andrzej Dziembowski
@gl
Andrzej Dziembowski
@hr
type
label
Andrzej Dziembowski
@ast
Andrzej Dziembowski
@ca
Andrzej Dziembowski
@cs
Andrzej Dziembowski
@de
Andrzej Dziembowski
@en
Andrzej Dziembowski
@es
Andrzej Dziembowski
@fr
Andrzej Dziembowski
@ga
Andrzej Dziembowski
@gl
Andrzej Dziembowski
@hr
altLabel
Andrzej Stanisław Dziembowski
@pl
prefLabel
Andrzej Dziembowski
@ast
Andrzej Dziembowski
@ca
Andrzej Dziembowski
@cs
Andrzej Dziembowski
@de
Andrzej Dziembowski
@en
Andrzej Dziembowski
@es
Andrzej Dziembowski
@fr
Andrzej Dziembowski
@ga
Andrzej Dziembowski
@gl
Andrzej Dziembowski
@hr
P8172
P106
P108
P1153
6602879453
P1412
P1559
Andrzej Dziembowski
@pl
P21
P214
72151110766937061436
P27
P31
P3124
P3373
P496
0000-0001-8492-7572
P569
1974-01-01T00:00:00Z
P734
P7859
lccn-n2019184427