User profiles for Frauke Melchior
Frauke MelchiorProfessor for Molecular Biology, Heidelberg University Verified email at zmbh.uni-heidelberg.de Cited by 18902 |
SUMO—nonclassical ubiquitin
F Melchior - Annual review of cell and developmental biology, 2000 - annualreviews.org
▪ Abstract SUMO (small ubiquitin-related modifier) is the best-characterized member of a
growing family of ubiquitin-related proteins. It resembles ubiquitin in its structure, its ability to be …
growing family of ubiquitin-related proteins. It resembles ubiquitin in its structure, its ability to be …
Sumo
E Meulmeester, F Melchior - Nature, 2008 - nature.com
A protein called small ubiquitin-related modifier (SUMO) can be coupled to other proteins to
control their function. This SUMOylation has been implicated in the regulation of a host of …
control their function. This SUMOylation has been implicated in the regulation of a host of …
[HTML][HTML] A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
R Mahajan, C Delphin, T Guan, L Gerace, F Melchior - Cell, 1997 - cell.com
We have found that the mammalian Ran GTPase–activating protein RanGAP1 is highly
concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it …
concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it …
Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
Nuclear pore complexes (NPCs) are gateways for nucleocytoplasmic exchange. To analyze
their structure in a close-to-life state, we studied transport-active, intact nuclei from …
their structure in a close-to-life state, we studied transport-active, intact nuclei from …
Concepts in sumoylation: a decade on
R Geiss-Friedlander, F Melchior - Nature reviews Molecular cell biology, 2007 - nature.com
A decade has passed since SUMO (small ubiquitin-related modifier) was discovered to be a
reversible post-translational protein modifier. During this time many enzymes that participate …
reversible post-translational protein modifier. During this time many enzymes that participate …
Sumoylation: a regulatory protein modification in health and disease
A Flotho, F Melchior - Annual review of biochemistry, 2013 - annualreviews.org
Posttranslational modification with small ubiquitin-related modifier (SUMO) proteins is now
established as one of the key regulatory protein modifications in eukaryotic cells. Hundreds of …
established as one of the key regulatory protein modifications in eukaryotic cells. Hundreds of …
[HTML][HTML] The nucleoporin RanBP2 has SUMO1 E3 ligase activity
A Pichler, A Gast, JS Seeler, A Dejean, F Melchior - Cell, 2002 - cell.com
Posttranslational modification with SUMO1 regulates protein/protein interactions, localization,
and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. …
and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. …
[HTML][HTML] SUMO: regulating the regulator
G Bossis, F Melchior - Cell division, 2006 - Springer
Post-translational modifiers of the SUMO (S mall U biquitin-related M odifier) family have
emerged as key regulators of protein function and fate. While the past few years have seen an …
emerged as key regulators of protein function and fate. While the past few years have seen an …
PIASy, a nuclear matrix–associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
…, L Bruhn, H Sieber, A Pichler, F Melchior… - Genes & …, 2001 - genesdev.cshlp.org
The Wnt-responsive transcription factor LEF1 can activate transcription in association with β-catenin
and repress transcription in association with Groucho. In search of additional …
and repress transcription in association with Groucho. In search of additional …
Structure determination of the small ubiquitin-related modifier SUMO-1
…, A Arndt, S Metzger, R Mahajan, F Melchior… - Journal of molecular …, 1998 - Elsevier
The recently discovered small ubiquitin-related modifier SUMO-1 belongs to the growing
family of ubiquitin-related proteins involved in postranslational protein modification. Unlike …
family of ubiquitin-related proteins involved in postranslational protein modification. Unlike …