about
Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexesSPOP promotes tumorigenesis by acting as a key regulatory hub in kidney cancerBuilding and remodelling Cullin-RING E3 ubiquitin ligasesAtomistic autophagy: the structures of cellular self-digestionStructure of a Glomulin-RBX1-CUL1 Complex: Inhibition of a RING E3 Ligase through Masking of Its E2-Binding SurfaceMechanism of ubiquitin ligation and lysine prioritization by a HECT E3A cascading activity-based probe sequentially targets E1-E2-E3 ubiquitin enzymesCryo-EM of Mitotic Checkpoint Complex-Bound APC/C Reveals Reciprocal and Conformational Regulation of Ubiquitin LigationTwo Distinct Types of E3 Ligases Work in Unison to Regulate Substrate UbiquitylationProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical spaceStructural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.Protein neddylation: beyond cullin-RING ligases.Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis.RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complexDefining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy.System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes.Mutation in ATG5 reduces autophagy and leads to ataxia with developmental delay.biGBac enables rapid gene assembly for the expression of large multisubunit protein complexes.Mechanism of APC/CCDC20 activation by mitotic phosphorylation.Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.Insights into links between autophagy and the ubiquitin system from the structure of LC3B bound to the LIR motif from the E3 ligase NEDD4.Structure of an APC3-APC16 complex: insights into assembly of the anaphase-promoting complex/cyclosome.APC15 mediates CDC20 autoubiquitylation by APC/C(MCC) and disassembly of the mitotic checkpoint complex.Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C.A role of autophagy in spinocerebellar ataxia-Rare exception or general principle?Binding to E1 and E3 is mutually exclusive for the human autophagy E2 Atg3.Mechanism of polyubiquitination by human anaphase-promoting complex: RING repurposing for ubiquitin chain assembly.Structural biology: A protein engagement RING.Crystallographic Characterization of ATG Proteins and Their Interacting Partners.Production of Human ATG Proteins for Lipidation Assays.Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated CompartmentsDiscovery of an Orally Bioavailable Inhibitor of Defective in Cullin Neddylation 1 (DCN1)-Mediated Cullin NeddylationPiperidinyl Ureas Chemically Control Defective in Cullin Neddylation 1 (DCN1)-Mediated Cullin NeddylationParadoxical mitotic exit induced by a small molecule inhibitor of APC/CCdc20Allosteric regulation through a switch element in the autophagy E2, Atg3Molecular glue concept solidifiesQuantifying the heterogeneity of macromolecular machines by mass photometryDual-color pulse-chase ubiquitination assays to simultaneously monitor substrate priming and extensionA switch element in the autophagy E2 Atg3 mediates allosteric regulation across the lipidation cascade
P50
Q24299638-473E5E3D-48B1-4957-8DF0-47475E70E20FQ24337489-8D24CB96-AC4A-4E9B-89B1-20825E257545Q24339492-BF152A4D-7981-4EC6-A932-0CB530C45F4AQ27027816-E694797F-C4CE-4FD2-B5B0-093ACE168C95Q27028021-4C7F3BC7-8BD9-4836-901C-322F906F15EEQ27670574-462DF4C0-8D88-4F5E-B32A-A74FE55489BFQ27679532-76F5CA23-BC71-451C-A894-B2D578146BB6Q27704870-58E69332-6923-40F8-8F9A-C8C11A7D6482Q27727603-4D4E65AE-C3FC-448E-955B-C11FC29F5028Q28115944-411A9DB9-BF07-456E-B0C2-238748DBF64DQ28817986-D4684958-560B-49A0-9D57-A85F98833630Q33773468-63350ADA-F21B-4301-BF08-1A08BB034C42Q34042816-BF92BD4D-5F41-4EFE-A5BC-A4A905DF4D5AQ34622632-23C44F38-79DF-447C-834A-A1D2E03C6467Q35567086-95109B8C-7454-48BE-B0CF-B6F54161570BQ35669194-755E3FF4-FF23-4077-917E-E514C8E93C4DQ35947378-21F70C94-1B0A-4E70-A4A4-9C48519894A1Q36673666-98E514DF-F36A-4FEA-A4ED-128441154B21Q36905027-730144D5-6553-4A1A-AB27-C6B0AF23A403Q36905102-13CF5109-CCEC-48F9-89A0-B16FE09289B8Q38701253-343EDCD4-00E4-4E63-9743-893D7AB37907Q38704902-950CE38A-0F47-46F6-9FDB-34513E93F3FFQ41100050-DEB5E4B9-C9F1-4635-97A9-458B730D5245Q41154841-43EFC3C4-AF8E-404D-848D-BE8D4C43D116Q41546924-8C026BC0-8D4B-4795-83A0-5277AB932F76Q41557084-A252EF20-4055-46C4-8E2D-F13F009AFF5EQ42860953-DD4E2684-778A-48A8-B576-3050F35FDF87Q43074598-DAF153CE-0D48-43DC-90D5-44405608FDA6Q43148089-32395DE1-D359-478F-832C-4A2FA53402DEQ49208739-820BB87E-E1DA-4379-9288-9A557874615CQ50982268-49F88097-DBB7-4592-B8D5-84E50F70A6BFQ57029699-BD900F28-445C-4F51-9CAF-EDEDEDEDE7AEQ88080886-C56D32B6-31B6-4CC8-84F6-A163C425C87DQ88080896-B53E0703-640E-42B8-9038-F80466780357Q90171686-E7B68653-7AD2-4180-A716-7E32F4E0D5C0Q91127372-3F72B349-5473-44F6-A4B8-F2120C7E7578Q91826901-B63E946F-9E56-4C18-97DD-3CE44BB67576Q91891947-236088CD-BB62-4463-B08D-0E588B3C0AC4Q92233296-3664018E-18D5-4E76-8362-7059811901B4Q92534284-79426EAD-C472-409D-8A84-F85338BF4962
P50
description
Forscher
@de
investigador
@es
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
研究者
@zh
name
Brenda A Schulman
@ast
Brenda A Schulman
@en
Brenda A Schulman
@es
Brenda A Schulman
@nl
type
label
Brenda A Schulman
@ast
Brenda A Schulman
@en
Brenda A Schulman
@es
Brenda A Schulman
@nl
prefLabel
Brenda A Schulman
@ast
Brenda A Schulman
@en
Brenda A Schulman
@es
Brenda A Schulman
@nl
P106
P31
P496
0000-0002-3083-1126