A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB
about
Classification of intrinsically disordered regions and proteinsGlycine-alanine repeats impair proper substrate unfolding by the proteasomeFunctions of the 19S complex in proteasomal degradationRatcheting up protein translocation with anthrax toxinAdaptor-Dependent Degradation of a Cell-Cycle Regulator Uses a Unique Substrate ArchitectureSubstrate selection by the proteasome during degradation of protein complexesMitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.Targeting proteins for degradationAutocatalytic processing of m-AAA protease subunits in mitochondriaDisordered proteinaceous machinesRecognition and processing of ubiquitin-protein conjugates by the proteasomeStepwise unfolding of a β barrel protein by the AAA+ ClpXP protease.Capping Enzyme mRNA-cap/RNGTT Regulates Hedgehog Pathway Activity by Antagonizing Protein Kinase ARad23 escapes degradation because it lacks a proteasome initiation regionDefining the geometry of the two-component proteasome degronParadigms of protein degradation by the proteasome.Slipping up: partial substrate degradation by ATP-dependent proteases.Intrinsically disordered segments affect protein half-life in the cell and during evolution.Pri sORF peptides induce selective proteasome-mediated protein processing.Pathogenic polyglutamine expansion length correlates with polarity of the flanking sequences.Increased proteolytic processing of full-length Gli2 transcription factor reduces the hedgehog pathway activity in vivo.Yeast SREBP cleavage activation requires the Golgi Dsc E3 ligase complex.The contributions of protein kinase A and smoothened phosphorylation to hedgehog signal transduction in Drosophila melanogaster.A truncated, activin-induced Smad3 isoform acts as a transcriptional repressor of FSHβ expression in mouse pituitaryRegulated protein turnover: snapshots of the proteasome in action.Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization.A three-part signal governs differential processing of Gli1 and Gli3 proteins by the proteasome.Gates, Channels, and Switches: Elements of the Proteasome MachineProtein unfolding and degradation by the AAA+ Lon protease.Coarse-Grained Simulations of Topology-Dependent Mechanisms of Protein Unfolding and Translocation Mediated by ClpY ATPase NanomachinesFused-Costal2 protein complex regulates Hedgehog-induced Smo phosphorylation and cell-surface accumulationSubstrate Ubiquitination Controls the Unfolding Ability of the Proteasome.Sequence- and species-dependence of proteasomal processivity.Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.Slippery substrates impair function of a bacterial protease ATPase by unbalancing translocation versus exitProtein targeting to ATP-dependent proteases.Gly-Ala repeats induce position- and substrate-specific regulation of 26 S proteasome-dependent partial processingATP-dependent proteases differ substantially in their ability to unfold globular proteinsCritical clamp loader processing by an essential AAA+ protease in Caulobacter crescentus.Truncated ErbB2 expressed in tumor cell nuclei contributes to acquired therapeutic resistance to ErbB2 kinase inhibitors.
P2860
Q22061736-82CE934F-D5C5-49E9-8542-632F6A93147AQ24543904-9A85E54B-64A3-4BC8-9D75-D7373AD32671Q26996345-BA14CF33-3C72-4649-A642-941747E56A48Q27023964-0D04E99A-4FF5-4748-8AA1-8CF102901CCEQ27681031-39F6722A-A62C-4BA1-BC24-CF092DADBDA7Q27932156-0EFDB4C6-B418-4BE1-B9C9-69A83289A81AQ27933616-92762328-F0F4-4060-BDBD-04195238A7DDQ28261886-1A834C6A-76E8-43B0-8075-CDB6BAE2C8C4Q28586518-642F3D9B-20A0-4791-AAED-0431C148DABCQ28652765-34601E4B-D280-4D82-B352-12CC9F7662E2Q29547616-4967CBB8-A1CA-42A7-9190-D7F8B0F3C9C0Q30155499-6C13EDE9-8CAA-4F7E-A61D-434EF25A55C1Q33767227-8140100A-30AC-4CFC-AF73-F4B28EAE1A36Q33801171-1C2786E2-8498-4F67-B2B5-C4928D7BB5F8Q34161503-ADF0081A-B1E0-412A-A7DB-308F60358156Q34410240-FC2FA5DB-0023-4832-B5ED-7E31EB94ECBFQ34419828-B60C7A64-7478-4705-B22E-03D5C775ED50Q34438593-E1349812-525A-41DE-A958-03EFAEB8F25BQ34494721-0A8C566F-D2BD-4EA2-8D41-E66F0D92BF02Q34544146-BB3CC131-2B2A-4C50-9EA8-3EF67CBA308DQ34764658-922E48BA-90E8-4CE9-A5B2-10C686F9DAA4Q34874112-F32FA7A4-2DEC-4534-A0F2-910031515420Q35038489-36AA4463-A9BA-4A84-97FA-B1A8C764D0EEQ35189000-39B3EE9B-9DC1-46E8-A85B-70051E67FC98Q35257872-A602B3B8-BB8A-4E30-9F8F-DF089F450008Q35420913-8C588ADA-7DC3-46B9-BB12-47D026536C65Q35604264-A02D9927-7E1F-4FA1-8113-A800E326458DQ35862786-9D1EADCC-E44B-48AC-8A01-9382C54218DCQ35884522-9AAB3868-1FD6-4BA9-8C95-D9DD8A7EE6E6Q35886561-935964E3-1F16-4D7E-A7F7-AC07BB8F8BAFQ35917072-18C38214-8576-4076-B378-C29925A45BEDQ36074198-91B962B3-F7F0-4419-B084-4D2986373494Q36177085-6B3507A6-AA18-4818-A086-9CCF72686649Q36182814-B5984396-CB06-461A-A8FD-1FD5884B4605Q36832564-B823A7B9-61F2-4A28-9673-E90576F3D388Q37085193-B1F4DF02-FFFC-44E3-8119-26A4AA7825ECQ37142562-01D8F771-A1BB-4427-97AF-4818C9A3F668Q37254059-F4DE612C-E22D-425A-AA95-B6064230A89DQ37318075-B92A3A5D-DC1B-4B52-A9D0-D9DB5E3DEE8AQ37332545-3E1990CA-3209-477E-BDDF-5669B969B259
P2860
A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB
description
article
@en
im November 2005 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в листопаді 2005
@uk
name
A conserved processing mechani ...... Cubitus interruptus and NF-κB
@en
A conserved processing mechani ...... Cubitus interruptus and NF-κB
@nl
type
label
A conserved processing mechani ...... Cubitus interruptus and NF-κB
@en
A conserved processing mechani ...... Cubitus interruptus and NF-κB
@nl
prefLabel
A conserved processing mechani ...... Cubitus interruptus and NF-κB
@en
A conserved processing mechani ...... Cubitus interruptus and NF-κB
@nl
P2860
P356
P1476
A conserved processing mechani ...... Cubitus interruptus and NF-κB
@en
P2093
Robert A Holmgren
P2860
P2888
P304
P356
10.1038/NSMB1018
P577
2005-11-20T00:00:00Z