The direction of protein entry into the proteasome determines the variety of products and depends on the force needed to unfold its two termini.
about
Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97Disordered proteinaceous machinesPA28αβ: the enigmatic magic ring of the proteasome?Protein unfolding by biological unfoldases: insights from modeling.Intrinsically disordered segments affect protein half-life in the cell and during evolution.The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins.Structural basis of antizyme-mediated regulation of polyamine homeostasis.Binding of interferon reduces the force of unfolding for interferon receptor 1.The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates.Prokaryotic proteasomes: nanocompartments of degradation.Structural disorder and its role in proteasomal degradation.The Logic of the 26S Proteasome.NADH binds and stabilizes the 26S proteasomes independent of ATP.Conformational dynamics is key to understanding loss-of-function of NQO1 cancer-associated polymorphisms and its correction by pharmacological ligands.Protein co-translocational unfolding depends on the direction of pulling.Enhanced vulnerability of human proteins towards disease-associated inactivation through divergent evolution.Rapid degradation of solid-phase bound peptides by the 20S proteasome.Folding-Degradation Relationship of a Membrane Protein Mediated by the Universally Conserved ATP-Dependent Protease FtsH.Experimental and computational evidence on conformational fluctuations as a source of catalytic defects in genetic diseases
P2860
Q28243388-644EB894-7420-42C3-9B1A-1ECEE2120493Q28652765-DA4133CD-FB50-47E6-B804-52C1C5BDA8D2Q33912635-F2C92ED6-1F56-4222-8339-34B8342A4A77Q34310114-F1777478-88F5-4472-B664-B27EAD8B08FAQ34438593-76BFB822-97FE-43C2-8FD7-C535F9B2BD2CQ35941678-257802F9-E98D-40FF-A008-4E01E3AFD1D4Q36056787-B42A8086-D015-4C85-8813-27A0F56174DAQ36344846-97104374-EF0F-4BA3-9431-5AAFEE165980Q37348923-580B40FA-2FDF-4807-8695-9844B2F9C971Q37606186-F0F9E685-585A-4637-9E05-51C98281F0F2Q38557562-0DEE93E2-9C21-4865-B31E-E50B7B13DACFQ39318404-F271D2EE-E216-437B-8296-F301FD33762DQ39997925-31FD4BC4-817D-4B4C-9C7F-A455A69FA648Q42546531-EDBEDC02-07D6-4F08-A263-D4BDC4E63E7CQ42878378-39952CC1-EA20-40A3-AB68-E342DE3981FBQ47801086-4DAE49A0-30DC-45B9-A009-38BD7E521496Q47916219-828DE165-90A6-4ADF-9B84-A1599294FE0DQ54975593-609D1318-A52F-406D-ADC5-D9195653DA95Q57578372-CC2A864C-E7FA-4FFB-9303-0FBED93E143A
P2860
The direction of protein entry into the proteasome determines the variety of products and depends on the force needed to unfold its two termini.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
The direction of protein entry ...... ded to unfold its two termini.
@en
The direction of protein entry ...... ded to unfold its two termini.
@nl
type
label
The direction of protein entry ...... ded to unfold its two termini.
@en
The direction of protein entry ...... ded to unfold its two termini.
@nl
prefLabel
The direction of protein entry ...... ded to unfold its two termini.
@en
The direction of protein entry ...... ded to unfold its two termini.
@nl
P2093
P2860
P1433
P1476
The direction of protein entry ...... eded to unfold its two termini
@en
P2093
Alfred L Goldberg
Boaz Tirosh
Dalit Shental-Bechor
Dikla Berko
Paolo Cascio
Shira Tabachnick-Cherny
Silvia Mioletti
Yaakov Levy
P2860
P304
P356
10.1016/J.MOLCEL.2012.08.029
P577
2012-10-04T00:00:00Z