about
Selecting one of several mating types through gene segment joining and deletion in Tetrahymena thermophilaBasal body stability and ciliogenesis requires the conserved component Poc1Mus81 nuclease and Sgs1 helicase are essential for meiotic recombination in a protist lacking a synaptonemal complexDeletion of the Tetrahymena thermophila rDNA replication fork barrier region disrupts macronuclear rDNA excision and creates a fragile site in the micronuclear genomeMethylation of histone H3K23 blocks DNA damage in pericentric heterochromatin during meiosis.Nested genes CDA12 and CDA13 encode proteins associated with membrane trafficking in the ciliate Tetrahymena thermophila.Role of ATG8 and autophagy in programmed nuclear degradation in Tetrahymena thermophilaThe recombinases Rad51 and Dmc1 play distinct roles in DNA break repair and recombination partner choice in the meiosis of Tetrahymena.CCTalpha and CCTdelta chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena.Class I histone deacetylase Thd1p affects nuclear integrity in Tetrahymena thermophila.Basal body duplication and maintenance require one member of the Tetrahymena thermophila centrin gene familyThe conjugation-specific Die5 protein is required for development of the somatic nucleus in both Paramecium and Tetrahymena.A robust inducible-repressible promoter greatly facilitates gene knockouts, conditional expression, and overexpression of homologous and heterologous genes in Tetrahymena thermophila.Germ line transcripts are processed by a Dicer-like protein that is essential for developmentally programmed genome rearrangements of Tetrahymena thermophila.LIA4 encodes a chromoshadow domain protein required for genomewide DNA rearrangements in Tetrahymena thermophilaThe CNA1 histone of the ciliate Tetrahymena thermophila is essential for chromosome segregation in the germline micronucleusMsh4 and Msh5 function in SC-independent chiasma formation during the streamlined meiosis of TetrahymenaThe two SAS-6 homologs in Tetrahymena thermophila have distinct functions in basal body assembly.The condensin complex is essential for amitotic segregation of bulk chromosomes, but not nucleoli, in the ciliate Tetrahymena thermophilaLIA5 is required for nuclear reorganization and programmed DNA rearrangements occurring during tetrahymena macronuclear differentiationSUMOylation is developmentally regulated and required for cell pairing during conjugation in Tetrahymena thermophilaA domesticated PiggyBac transposase interacts with heterochromatin and catalyzes reproducible DNA elimination in Tetrahymena.The germ line limited M element of Tetrahymena is targeted for elimination from the somatic genome by a homology-dependent mechanism.The Tetrahymena thermophila phagosome proteome.Vacuolar protein sorting protein 13A, TtVPS13A, localizes to the tetrahymena thermophila phagosome membrane and is required for efficient phagocytosisZygotic expression of the double-stranded RNA binding motif protein Drb2p is required for DNA elimination in the ciliate Tetrahymena thermophila.Lia1p, a novel protein required during nuclear differentiation for genome-wide DNA rearrangements in Tetrahymena thermophila.An essential role for the DNA breakage-repair protein Ku80 in programmed DNA rearrangements in Tetrahymena thermophila.Tudor nuclease genes and programmed DNA rearrangements in Tetrahymena thermophila.Bld10/Cep135 stabilizes basal bodies to resist cilia-generated forces.Sfr13, a member of a large family of asymmetrically localized Sfi1-repeat proteins, is important for basal body separation and stability in Tetrahymena thermophila.Nucleus-specific importin alpha proteins and nucleoporins regulate protein import and nuclear division in the binucleate Tetrahymena thermophila.Dynein-2 affects the regulation of ciliary length but is not required for ciliogenesis in Tetrahymena thermophilaBasal body components exhibit differential protein dynamics during nascent basal body assemblyDifferential targeting of Tetrahymena ORC to ribosomal DNA and non-rDNA replication origins.Sfr1, a Tetrahymena thermophila Sfi1 Repeat Protein, Modulates the Production of Cortical Row Basal Bodies.Asymmetrically localized proteins stabilize basal bodies against ciliary beating forces.DRH1, a p68-related RNA helicase gene, is required for chromosome breakage in Tetrahymena.Tetrahymena in the laboratory: strain resources, methods for culture, maintenance, and storage.An evolutionarily conserved phosphatidate phosphatase maintains lipid droplet number and endoplasmic reticulum morphology but not nuclear morphology.
P2860
Q21092706-F6948672-8E49-4920-9F47-9D98247D8F2DQ22001530-2E10C81F-AF83-4461-B23C-602DE0F33DBAQ24603667-2E5CE6DB-C443-4586-AFEE-851DA391F223Q25257785-476D6D16-4452-458A-BD85-CF3995BAA6C2Q30411151-8C5D8DBB-3EA6-40CD-AB26-61A191C0BE9BQ30488290-5146F3CA-B528-4441-9626-0711DAB9A547Q30512687-136248BC-8C11-437F-BE5B-6DC98E8B5678Q33350963-B2DFC7EE-5CC1-4074-8157-2981807A5103Q33587559-4C5BFB3E-4F55-4291-905A-A1123CF60B89Q33836008-40B2AE11-6521-4927-A927-8C1CEC7764AEQ33911099-5A3DF567-59CD-4773-B9F9-D1AB90123350Q33983213-42620145-3486-407A-AF43-98E97AE2CC0CQ34019993-3914F514-5589-477D-9B16-A26A5C8EB8E6Q34097228-B09A1B4F-1088-4EEC-9D46-32B9C1A10F84Q34297686-436EA1FD-1B38-4DB5-A214-4989FA4506B8Q34298429-94C1B396-1613-4E08-BA54-B7A950302A61Q34471736-1A759967-5F67-439E-A411-629CEFB3CA15Q34603390-995EF6E8-42CB-4329-A6FE-20C87AA4D429Q34718111-37F52136-C507-4AEE-B2EF-7D82B1EF0E6FQ34999545-9CA47713-2CBB-4139-941C-50E4EDD53CDBQ35031726-CECF1FBC-EE22-41C1-A665-0C02742613B1Q35069227-132D2AC2-FDC3-4F56-A2BC-32C246A46A7FQ35128100-E7604164-8A79-40BF-A41E-36069CB13BFEQ35216748-7992F9DD-098A-4470-92B7-059D001B62E3Q35271290-8031A339-5088-48E3-AD0B-412A103281EBQ35598273-3217D635-B4F3-46CC-9055-6838F2A99D1BQ35947117-2C38DD86-D97D-4D73-AF55-329B53492D7BQ35998613-DD65EE53-FA30-45CF-9ADE-A8E3A176524EQ36095315-00677EE5-1478-4C02-8CF3-A195154778BBQ36465096-B0990698-11F3-4E5E-8BF4-CBC2020C7E78Q36825253-14623C26-E73D-478B-94BC-45A27BE8F3CCQ36899105-AA4B2EF9-1FC7-44F5-AC3A-E54F6A8D1C47Q37061540-A259EA56-D585-4D17-9804-870EA6D185A7Q37078593-A4F1E298-5A5B-4821-808D-28D3A81566D2Q37087250-EEF35D07-6AAC-4D38-A386-4DEBD43C3200Q37418858-D0081C5F-54B6-4B0C-918E-D3B3E7E0CDC7Q37429836-39D28F65-379D-4705-99CA-2DCE8A0B0D16Q37545456-4F8903BD-A7E5-4D42-B2AE-3D58423D6529Q39307970-E87822AC-A784-490F-AEEE-86C2849FB146Q47103627-02212537-ABED-46B6-93FE-2D93550F3430
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Biolistic transformation of macro- and micronuclei.
@ast
Biolistic transformation of macro- and micronuclei.
@en
type
label
Biolistic transformation of macro- and micronuclei.
@ast
Biolistic transformation of macro- and micronuclei.
@en
prefLabel
Biolistic transformation of macro- and micronuclei.
@ast
Biolistic transformation of macro- and micronuclei.
@en
P1476
Biolistic transformation of macro- and micronuclei
@en
P2093
D Cassidy-Hanley
P304
P356
10.1016/S0091-679X(08)61553-8
P577
2000-01-01T00:00:00Z