about
SM-protein-controlled ER-associated degradation discriminates between different SNAREs.A comprehensive strategy enabling high-resolution functional analysis of the yeast genome.Shaping the landscape: mechanistic consequences of ubiquitin modification of chromatin.Sensitive and Quantitative Three-Color Protein Imaging in Fission Yeast Using Spectrally Diverse, Recoded Fluorescent Proteins with Experimentally-Characterized In Vivo Maturation Kinetics.Beyond Tethering and the LEM domain: MSCellaneous functions of the inner nuclear membrane Lem2.The Histone Acetyltransferase Mst2 Protects Active Chromatin from Epigenetic Silencing by Acetylating the Ubiquitin Ligase Brl1.Global regulation of heterochromatin spreading by Leo1.Chromatin binding and silencing: Two roles of the same protein Lem2.Control of heterochromatin localization and silencing by the nuclear membrane protein Lem2.Relationship between genome and epigenome--challenges and requirements for future researchThe fission yeast nucleoporin Alm1 is required for proteasomal degradation of kinetochore components.Glutathione and a UV light-induced glutathione S-transferase are involved in signaling to chalcone synthase in cell culturesA series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targetingThe euchromatic histone mark H3K36me3 preserves heterochromatin through sequestration of an acetyltransferase complex in fission yeastSet1/COMPASS repels heterochromatin invasion at euchromatic sites by disrupting Suv39/Clr4 activity and nucleosome stabilityTASks for subtelomeres: when nucleosome loss and genome instability are favoredNeutral epigenetic inheritance: being prepared for future generationsShelterin and subtelomeric DNA sequences control nucleosome maintenance and genome stability
P50
Q27932266-B7AD71E2-6270-4C13-8C50-1B6203A8A162Q33351293-C9C8A541-0E59-41ED-8854-4D89AB86C64CQ36073403-36CEE9F6-B6BA-4652-B8B1-8C872405ECE8Q36091815-F9233B71-A5C5-46BB-B4D3-B87A681AF7DBQ36178359-5E8031E9-105E-4D3B-8FA6-69D1119EDD09Q41123075-4938A8BB-5B4B-43BC-8197-5A06DECFFDD8Q41461673-B9B5F174-0F5B-4322-A040-F37B2161FF25Q42316628-529CCEC5-3A49-4BA9-A4CE-6FE57C6DB1A4Q42687369-13DE7969-176C-4CAF-A8F4-B35CCBCCC46CQ42712507-C72802F2-5289-48EB-806E-A929FF3B30D9Q47703993-71D80CFF-E132-41EE-BA39-A67DB7BD8BDAQ73102578-FD5D7D96-1424-4A2C-9BF3-1C942A1DC199Q81277350-80AFD722-5897-430A-AC5A-F320B2774AA7Q90249962-D3C365D5-D6B2-4C2A-9666-389934A6CCFEQ91725529-E0311207-892D-4E91-9F1B-1A65096619B7Q91839272-C2FDB34E-BC54-4750-A5BC-35C58A49C6ACQ92173238-67427160-DCF9-4E59-A3A0-5B0D996E8843Q93016092-3430EEE9-09ED-4DAF-89A8-303696A20A3C
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Sigurd Braun
@ast
Sigurd Braun
@en
Sigurd Braun
@es
Sigurd Braun
@nl
type
label
Sigurd Braun
@ast
Sigurd Braun
@en
Sigurd Braun
@es
Sigurd Braun
@nl
prefLabel
Sigurd Braun
@ast
Sigurd Braun
@en
Sigurd Braun
@es
Sigurd Braun
@nl
P106
P31
P496
0000-0001-6399-8574