Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1 (Q27637899)

ORCID Public Data File 2021

Christopher D. Lima

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ORCID Public Data File 2021

author name string

Victor Bernier-Villamor

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Deborah A Sampson

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Michael J Matunis

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Christopher D Lima

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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language of work or name

English

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publication date

8 February 2002

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published in

Cell

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volume

108

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issue

3

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page(s)

345-56

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cites work

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Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha

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Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1.

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Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail

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SP-RING for SUMO: new functions bloom for a ubiquitin-like protein

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Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade

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Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p

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Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins

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An E3-like factor that promotes SUMO conjugation to the yeast septins

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A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

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A novel factor required for the SUMO1/Smt3 conjugation of yeast septins

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