Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes.
about
ribonuclease P/MRP protein subunit RPP1, putativeribonucleases P/MRP protein subunit POP1, putativeribonuclease P protein subunit RPR2, putativeribonuclease P/MRP protein subunit RPP1, putativeribonucleases P/MRP protein subunit POP1, putativeribonuclease P protein subunit RPR2, putativeribonucleases P/MRP protein subunit POP1, putativeribonuclease P protein subunit RPR2, putativeribonuclease P/MRP protein subunit RPP1, putativeribonucleases P/MRP protein subunit POP1, putativeribonuclease P protein subunit RPR2, putativeribonucleases P/MRP protein subunit POP1, putativeribonucleases P/MRP protein subunit POP1, putativeribonuclease P/MRP protein subunit RPP1, putativeribonucleases P/MRP protein subunit POP1, putativeribonuclease P protein subunit RPR2, putativeribonuclease P/MRP protein subunit RPP1, putativeribonuclease P/MRP protein subunit RPP1, putativeribonuclease P protein subunit RPR2, putativeribonucleases P/MRP protein subunit POP1, putativeribonuclease P protein subunit RPR2, putativeribonuclease P/MRP protein subunit RPP1, putativeribonuclease P protein subunit RPR2, putativeribonuclease P protein subunit RPR2, putativeribonuclease P/MRP protein subunit RPP1, putativeribonucleases P/MRP protein subunit POP1, putativeribonuclease P protein subunit RPR2, putative
P1343
Human RNase P: a tRNA-processing enzyme and transcription factorInteractions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture.Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrateConservation and losses of non-coding RNAs in avian genomesAlba-domain proteins of Trypanosoma brucei are cytoplasmic RNA-binding proteins that interact with the translation machineryArchaeal/eukaryal RNase P: subunits, functions and RNA diversificationRNase MRP and disease3' terminal diversity of MRP RNA and other human noncoding RNAs revealed by deep sequencing.Targeted CRISPR disruption reveals a role for RNase MRP RNA in human preribosomal RNA processingBcheck: a wrapper tool for detecting RNase P RNA genes.Of proteins and RNA: the RNase P/MRP family.Ribosomal protein L7Ae is a subunit of archaeal RNase P.GAMETOPHYTE DEFECTIVE 1, a putative subunit of RNases P/MRP, is essential for female gametogenesis and male competence in Arabidopsis.Molecular characterization of three PRORP proteins in the moss Physcomitrella patens: nuclear PRORP protein is not essential for moss viability.Substrate recognition by ribonucleoprotein ribonuclease MRP.The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA.Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.RNase MRP cleaves pre-tRNASer-Met in the tRNA maturation pathway.Assembly of the complex between archaeal RNase P proteins RPP30 and Pop5Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAsFidelity of tRNA 5'-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactorsOf P and Z: mitochondrial tRNA processing enzymes.Nuclear RNase P of Trypanosoma brucei: a single protein in place of the multicomponent RNA-protein complex.Proteomic analysis of bovine nucleolus.Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects.Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopyRNase P enzymes: divergent scaffolds for a conserved biological reaction.The evolution of the ribosome biogenesis pathway from a yeast perspectiveEvolution of the iron-responsive element.A structural module in RNase P expands the variety of RNA kinks.Dynamic interactions within sub-complexes of the H/ACA pseudouridylation guide RNP.Distribution of Ribonucleoprotein and Protein-Only RNase P in Eukarya.Mitochondrial Genome Engineering: The Revolution May Not Be CRISPR-Ized.Minimal and RNA-free RNase P in Aquifex aeolicus.
P2860
Q56562313-38DBD8D1-4B59-434C-9BDB-3F719EE7AA2FQ56562847-8D67A54D-5206-47BB-B7AE-41C8A31E4768Q56586949-4B6EC81D-6D46-43DE-8EC8-00D102C33B95Q56717665-7AC32983-32F1-4D6A-8DC7-900C3826445CQ56719679-6B4A0A33-501B-4BE1-AA6A-B18FA73DB5C9Q56737798-10BCFC01-9193-44B7-B827-E6D94499B555Q59725632-40179446-1B50-41F1-B1FF-8499E55D9A96Q59883856-D2D807AC-C432-4588-B74E-26AB9B307B27Q59916998-B300472C-19E2-4EF8-8B03-420ADC1E4C71Q59918571-C1FB1E73-7308-4926-88D0-52F0B4F9F69BQ59921005-5B52D845-8472-44EC-84B7-D7872AB2B43BQ59948225-86CD48F4-E9E3-438C-8F73-1471161CB18EQ59951904-516B8A8E-08FA-45FD-9C41-2A0D4F855E7BQ59959928-539F8B2F-C5D1-4E0A-BAA0-96E086C7ABB7Q59966336-7FB4F9B5-B685-4980-B223-62A09FAB43C7Q59970457-8FF106CC-EDC4-4AD6-8F0D-BC1C5998C5ADQ59982578-003B8251-C3A7-43E6-AABA-E92A0A04819DQ59982586-22E84157-E9EA-45AC-BAA4-4C6D3CB919FCQ59985691-093F5261-3A68-4E2A-8E43-8078A970612EQ59990034-3ED580C0-1E2F-484A-81F0-01CBE96910D7Q59999241-5B02A421-2A11-4A7B-97E1-2540D996E32AQ60000099-E995BA4A-C085-401B-A624-5DB17B1CC709Q60002169-089FC526-2E4E-4C96-8828-9CF4BFB64045Q60010876-6C9FC695-F320-4856-A51E-4A25C7BC09EAQ61617020-8F32B9F5-BCCC-4654-B467-D2CC8C26B96AQ61618298-B6C6A518-0DA1-498A-B045-C5DD19AE33B4Q61620211-65A12FBB-3F1A-4E74-8787-6743C3A7BE39
P1343
Q24671877-60626E1A-1578-48FF-B5C0-E2741B6E7EEEQ27905699-9246504C-11D4-4E8F-AB7E-5F7ABD7CC798Q27905710-AA79C1B0-7F1C-4CEA-A001-6BB19993EC37Q28651058-0A338D6E-2220-41CB-8DC8-3F20A549531EQ28742336-64570131-45FF-4934-93E0-50F0FF8A12A3Q28744300-3E3B8F1C-10D3-4A60-8F4F-CF209E40C7FBQ30048481-68FC15FF-34F6-4E04-9214-7DD19402C131Q30457001-A37A6F84-4F7E-40F4-94E5-B1D7B63F80DCQ30460576-1238B4F7-48AA-4AE2-86F5-EA2830738D06Q33631756-F31B594F-ED59-4EF8-B08B-E6D2071B7EEDQ34075899-3828A770-1ACC-46AA-9CAB-D7B8762EBF03Q34093284-78671DDE-3A67-4C58-9038-F0964B54C07BQ34235015-FFA998E1-4805-4C89-95A2-423E85FA7A20Q34361039-14D11DEA-C558-4EBE-8AF2-9D32657DFCC2Q34497413-F4CB1EEF-CA19-46B5-89E9-B5C5B9742D69Q34579824-38537B4A-D3A1-4FC8-894C-9B26A7A641EFQ35262654-F649BE5A-AD1F-4465-84F5-7D0190B1CAB7Q35425781-03E1DD27-65FF-4951-9456-63676F201BE0Q35582312-207A44F4-3951-4D42-B5C6-B5008B3AE3B2Q36003399-0D819B22-4FE8-4DDF-9237-598842CCA79BQ36044708-F7B886EB-B8A1-4474-88CB-6E3E7D045D8AQ37216231-03DA9B0A-80BE-4BEA-B581-7F95A9F24F5AQ37254038-B1589CDC-2770-413B-BA33-33E6697AB492Q37318391-B4A1FB1F-BE8D-48FF-9529-C0BD42ABD409Q37636822-C61E60A2-6C15-4946-BA99-C5FAD217E428Q41871063-293686C0-279B-4CEF-86EC-543167D77293Q41895901-659C2114-975E-4FAE-9AD5-C70583B41F09Q41941227-6AC2A9C3-3E55-4923-B265-5493E35BCE3AQ42159338-8271A081-95BD-4CEF-9B61-13D8ACDD1CE7Q42636430-ACBE4469-489E-4B3A-8E3F-A6BD18BAFCE2Q42734613-AE08A3D2-B601-4855-9E02-98E715A542CFQ44434425-38C65241-EBC7-44CB-8C82-4E8119BA2F88Q47309962-EB18272A-8399-4B93-9FE8-74DA5994813BQ47600756-DA92BCDE-2AE8-486C-821B-66AA1E88877B
P2860
Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Inventory and analysis of the ...... n the yeast and human enzymes.
@en
Inventory and analysis of the ...... n the yeast and human enzymes.
@nl
type
label
Inventory and analysis of the ...... n the yeast and human enzymes.
@en
Inventory and analysis of the ...... n the yeast and human enzymes.
@nl
prefLabel
Inventory and analysis of the ...... n the yeast and human enzymes.
@en
Inventory and analysis of the ...... n the yeast and human enzymes.
@nl
P2093
P2860
P921
P356
P1476
Inventory and analysis of the ...... n the yeast and human enzymes.
@en
P2093
Magnus Alm Rosenblad
Marcela Dávila López
Paul Piccinelli
Tore Samuelsson
P2860
P304
P356
10.1093/NAR/GKL626
P407
P577
2006-09-22T00:00:00Z