sameAs
P185
An N-terminal domain of Dbf4p mediates interaction with both origin recognition complex (ORC) and Rad53p and can deregulate late origin firing.Histones and histone modifications in perinuclear chromatin anchoring: from yeast to manChromatin states and nuclear organization in development--a view from the nuclear laminaStructural basis for the role of the Sir3 AAA+ domain in silencing: interaction with Sir4 and unmethylated histone H3K79Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formationRedistribution of silencing proteins from telomeres to the nucleolus is associated with extension of life span in S. cerevisiae.Distortion of the DNA double helix by RAP1 at silencers and multiple telomeric binding sites.An N-terminal acidic region of Sgs1 interacts with Rpa70 and recruits Rad53 kinase to stalled forks.Distinct roles for SWR1 and INO80 chromatin remodeling complexes at chromosomal double-strand breaks.Sif2p interacts with Sir4p amino-terminal domain and antagonizes telomeric silencing in yeast.PolySUMOylation by Siz2 and Mms21 triggers relocation of DNA breaks to nuclear pores through the Slx5/Slx8 STUbL.Semi-conservative replication in yeast nuclear extracts requires Dna2 helicase and supercoiled template.Chromatin organization and dynamics in double-strand break repairHistone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeastRecruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repairReplication foci dynamics: replication patterns are modulated by S-phase checkpoint kinases in fission yeast.Lte1, Cdc14 and MEN-controlled Cdk inactivation in yeast coordinate rDNA decompaction with late telophase progression.Promoter- and RNA polymerase II-dependent hsp-16 gene association with nuclear pores in Caenorhabditis elegansA game of musical chairs: Pro- and anti-resection factors compete for TOPBP1 binding after DNA damage.Heterochromatin Protein 1β (HP1β) has distinct functions and distinct nuclear distribution in pluripotent versus differentiated cells.Automatic tracking of individual fluorescence particles: application to the study of chromosome dynamics.The processing of double-strand breaks and binding of single-strand-binding proteins RPA and Rad51 modulate the formation of ATR-kinase foci in yeast.Actin-related protein Arp6 influences H2A.Z-dependent and -independent gene expression and links ribosomal protein genes to nuclear pores.Nuclear compartments and gene regulation.Targeting Sir proteins to sites of action: a general mechanism for regulated repression.Ku-deficient yeast strains exhibit alternative states of silencing competenceMechanistically distinct roles for Sgs1p in checkpoint activation and replication fork maintenance.The organisation of chromatin loops: characterization of a scaffold attachment site.A sense of the end.The budding yeast nucleus.TORC2-a new player in genome stabilityPositions of potential: nuclear organization and gene expression.Measuring limits of telomere movement on nuclear envelopeSIR proteins and the assembly of silent chromatin in budding yeast.Subtelomeric factors antagonize telomere anchoring and Tel1-independent telomere length regulationFrom snapshots to moving pictures: new perspectives on nuclear organization.On TADs and LADs: Spatial Control Over Gene Expression.The origin recognition complex functions in sister-chromatid cohesion in Saccharomyces cerevisiae.Analysis of Sir2p domains required for rDNA and telomeric silencing in Saccharomyces cerevisiae.Open questions: epigenetics and the role of heterochromatin in development
P50
Q24541493-6204FA39-E089-42C9-A445-4D2B8E9267EDQ26770526-6A41BFD7-773B-46C0-81FC-36423A013E05Q26798007-8D885103-18CD-4113-B047-071B33BE3EF4Q27673259-D3EFEBA0-E070-46F7-BD58-5DB429DABF6DQ27675824-34A598A4-0A3D-4DA6-A94F-E0ED697F586BQ27931333-CA7CC64D-CEAF-46B3-9D49-65AE8081140DQ27931439-CD7D03D6-2B34-4FB5-96DE-74AB80E9E87EQ27933571-9009D17E-401E-4CDA-B8A5-2EE062E943D6Q27934708-5C5754A9-C927-497D-987B-3E556FA840F7Q27934734-D2E19F18-FB29-4053-9A7E-EF120D097CCBQ27935500-3FBE0F5B-3386-40FD-9A86-733947E14257Q27935820-955540E6-8978-4F44-B61F-995097DC7852Q28069283-FB281DE9-9371-4833-9740-9BF4F7657718Q29614857-3F0669B9-B04D-4F23-9096-13129D3ABDF7Q29620305-73AD7A18-6CAE-47C7-A63C-398BC76FD138Q30479065-A82F13E2-09AE-4653-BE7E-2D62B08DBAC6Q30488070-520CD74E-E0EA-4274-B64D-5A8ECCD9FE91Q30537180-C9FF8704-D057-46D9-BC32-FC1D25C69508Q30572330-852C2309-9594-4AC8-93F7-F307ED91C6EBQ30666181-E01FD89D-C9E0-40C4-B6E4-370ED0694EB3Q33224137-B6394956-B12D-4EA3-955B-1A50B83FE408Q33305607-6E33A1BE-52C5-42D1-BF46-8B2EA50E4018Q33564388-560BD0A0-0F0A-4F62-9D91-EC697134CCCFQ33632367-07020B3A-97FC-4F53-B9A1-1DE74AACE91CQ33671486-C5999280-57D8-4E27-875C-580D385BCF46Q33757235-78651B28-1368-4E2F-B222-977FCA517BD6Q33761161-F62FB0F9-FB3F-40C6-8739-450632DF88D5Q33879560-A73B215B-9E1F-4003-AD88-DF50D013CAC8Q33927541-9CB1C101-04D4-438B-8734-2B52DE3472B7Q34014665-8F963CE6-004C-4813-A98E-6985709C1091Q34131149-47EF2104-57F4-4687-A419-3B31C02F0B89Q34189097-CA861348-A5FB-4316-9763-F42DAAF5D1EEQ34353272-B9B18200-6AF3-48CA-9AE7-7F6DF3B04F42Q34369656-761B17A5-B34B-4F27-BC7B-1ADAC234DFDFQ34410987-E0ED2BC4-6EB4-4D46-970F-4B14AB703B52Q34446338-B10C391F-9680-499D-8BC1-0D7B616E5EEAQ34531125-157708FC-E892-4D76-8668-852B591487BEQ34600944-AE6E139B-B752-4B3C-B171-00C1A35A9D1CQ34609028-ADFD9E3F-BCA5-496B-85A1-C1DFB71EC2C8Q34622533-4B5386C0-4E6E-4AB7-B53B-9DCDD94512F3
P50
description
US-amerikanische Molekularbiologin
@de
biologiste moléculaire
@fr
bióloga molecular suiza
@ast
moleculair biologe uit Zwitserland
@nl
molecular biologist
@en
عالمة أحياء جزيئية سويسرية
@ar
name
Susan Gasser
@ca
Susan Gasser
@es
Susan Gasser
@fr
Susan M Gasser
@ast
Susan M. Gasser
@bar
Susan M. Gasser
@de
Susan M. Gasser
@en
Susan M. Gasser
@ga
Susan M. Gasser
@it
Susan M. Gasser
@nl
type
label
Susan Gasser
@ca
Susan Gasser
@es
Susan Gasser
@fr
Susan M Gasser
@ast
Susan M. Gasser
@bar
Susan M. Gasser
@de
Susan M. Gasser
@en
Susan M. Gasser
@ga
Susan M. Gasser
@it
Susan M. Gasser
@nl
altLabel
Susan M Gasser
@en
Susan M Gasser
@nl
Susan M Gasser
@sl
prefLabel
Susan Gasser
@ca
Susan Gasser
@es
Susan Gasser
@fr
Susan M Gasser
@ast
Susan M. Gasser
@bar
Susan M. Gasser
@de
Susan M. Gasser
@en
Susan M. Gasser
@ga
Susan M. Gasser
@it
Susan M. Gasser
@nl
P108
P166
P1006
P214
P227
P244
P269
P1006
P1321
P1412
P166
P184
P2080
P21
P213
0000 0001 2351 7844