about
Reconstituting the kinetochore–microtubule interface: what, why, and howMad1 kinetochore recruitment by Mps1-mediated phosphorylation of Bub1 signals the spindle checkpoint.Glc7/protein phosphatase 1 regulatory subunits can oppose the Ipl1/aurora protein kinase by redistributing Glc7.Direct interaction between yeast spindle pole body components: Kar1p is required for Cdc31p localization to the spindle pole bodyMutation of YCS4, a budding yeast condensin subunit, affects mitotic and nonmitotic chromosome behavior.An E3 ubiquitin ligase prevents ectopic localization of the centromeric histone H3 variant via the centromere targeting domainQuantitative proteomic analysis of purified yeast kinetochores identifies a PP1 regulatory subunitThe budding yeast protein kinase Ipl1/Aurora allows the absence of tension to activate the spindle checkpointDe novo kinetochore assembly requires the centromeric histone H3 variant.Tension directly stabilizes reconstituted kinetochore-microtubule attachments.Kinetochores require oligomerization of Dam1 complex to maintain microtubule attachments against tension and promote biorientation.The FACT complex interacts with the E3 ubiquitin ligase Psh1 to prevent ectopic localization of CENP-A.Sister kinetochores are mechanically fused during meiosis I in yeast.The Mub1/Ubr2 ubiquitin ligase complex regulates the conserved Dsn1 kinetochore protein.Phosphoregulation promotes release of kinetochores from dynamic microtubules via multiple mechanismsKinetochore function and chromosome segregation rely on critical residues in histones H3 and H4 in budding yeast.Measuring kinetochore-microtubule interaction in vitro.Captivating capture: how microtubules attach to kinetochores.Under Tension: Kinetochores and Basic ResearchRegulation of Budding Yeast CENP-A levels Prevents Misincorporation at Promoter Nucleosomes and Transcriptional Defects.The spindle checkpoint: tension versus attachment.Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing centerMicrotubule capture: a concerted effort.The composition, functions, and regulation of the budding yeast kinetochorePericentromeric sister chromatid cohesion promotes kinetochore biorientation.Signalling dynamics in the spindle checkpoint response.Histone H4 Facilitates the Proteolysis of the Budding Yeast CENP-ACse4 Centromeric Histone Variant.An efficient purification system for native minichromosome from Saccharomyces cerevisiae.The structure of purified kinetochores reveals multiple microtubule-attachment sites.A TOG Protein Confers Tension Sensitivity to Kinetochore-Microtubule Attachments.Stochastic Modeling Yields a Mechanistic Framework for Spindle Attachment Error Correction in Budding Yeast Mitosis.Correcting SYNful attachments.Design principles of a microtubule polymerase.An assay for de novo kinetochore assembly reveals a key role for the CENP-T pathway in budding yeastSister chromatid cohesion in mitosisAn Mtw1 complex promotes kinetochore biorientation that is monitored by the Ipl1/Aurora protein kinaseProteolysis contributes to the exclusive centromere localization of the yeast Cse4/CENP-A histone H3 variantEditorial overview: Cell architecture: Cellular organization and functionH3K4 methylation at active genes mitigates transcription-replication conflicts during replication stressKinetochore-associated Stu2 promotes chromosome biorientation in vivo
P50
Q27007105-A9EE9C3E-A2B0-4C9D-8C6F-F480487B7B58Q27930798-9DFF51F6-BE80-41BF-988E-1AAA3287C489Q27931042-9F1DA909-0CAC-497F-8969-CEE1C3D2304BQ27933029-A3AE4C1F-35E2-431C-8E44-543560E65CACQ27934947-25889416-9291-4F9D-A84B-B281DF410CB5Q27936898-92794C16-EBBE-4BC0-A2B1-54A5150C753CQ27939587-0184AE33-CB6D-4786-B839-2940DCA480F4Q28365645-6F6D01C2-CA1A-4982-A94B-5F01A85B97DAQ28941168-BA8B10D0-DAE1-4FA7-B0C9-3ECF2BB8877BQ30500849-938B6FBF-CD99-4F6C-B2EA-DBCDC5831616Q30592344-AC90AA83-DA7F-44D3-ABC9-27774A23B7F8Q34342927-4CC50325-B12D-4862-ADE5-9862B2583DCCQ34482668-B3240722-C7AC-42CC-8F80-656E46DA8557Q34585694-7ED99F5C-B75E-4AFB-A436-4EC0C7104BCDQ34670084-7DBAD423-18F6-4F80-893B-388531104600Q34987501-3CF2A855-575C-47D4-BDB1-A17A3EE9937EQ35121046-29EBE8BE-287B-4D54-83D9-CF719379FBA6Q35142905-CD0FA2DF-01B5-438A-A926-70C9B2354F91Q35882315-71A097F3-D9C7-46E9-B9EF-62AFCCD61ADBQ35959575-2C598363-A650-4542-9888-787A3D8C6C31Q36220221-9B9DB63D-46C8-412D-ACC4-13500EC498A3Q36237090-2F622975-0DA9-4A2A-8700-8473D1711B6AQ36686601-4D365C3F-F762-4FAE-B22D-C777FAEEC843Q37063126-346AA0F7-77E0-496B-A8C6-8E7F9A5AC5BDQ37327282-50C385AD-CB7A-4E6E-B401-9ACF6F1AED4BQ38258850-9FE7EE15-568C-45EF-B07B-807C9DB82398Q39236417-C1875581-C4FF-4B49-A2E6-23104337C0ABQ39946677-0CC026A5-E1CD-4688-A33E-176731065122Q42198473-D55B996D-A149-495E-9D4F-A8A2710E0C49Q42741776-DF1BBAFE-ACE7-4DBE-9862-BFDE52EBB7E5Q47807712-60D25866-FCB2-4A7B-8DE0-BA54E7D1E18DQ47895637-24519212-975A-49B0-8BCD-99A4E5C15098Q55155335-C64540CA-21C6-40AF-BCE3-904F5B348A8FQ56529576-4316985B-582E-47E9-BA70-BAF178352006Q77891942-5FD05D2A-3B73-49D9-9B5C-AF18C5F8ED9DQ79258734-14A253FE-F64E-4E89-A251-AEEEED97AB0EQ80972424-0736C586-1F7C-40E9-B998-DDA7ECC92974Q87121713-673D4CD4-63F0-4652-921D-1B6081A52A5EQ89636837-DF8F5C3C-4BAC-411F-810B-56E4629AC4FAQ90482853-17DE86E2-9918-421A-9559-F1794BF138AA
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Sue Biggins
@ast
Sue Biggins
@en
Sue Biggins
@es
Sue Biggins
@nl
Sue Biggins
@sl
type
label
Sue Biggins
@ast
Sue Biggins
@en
Sue Biggins
@es
Sue Biggins
@nl
Sue Biggins
@sl
prefLabel
Sue Biggins
@ast
Sue Biggins
@en
Sue Biggins
@es
Sue Biggins
@nl
Sue Biggins
@sl
P106
P1153
6701837141
P21
P31
P4012
P496
0000-0002-4499-6319