Incorporation of Non-natural Amino Acids Improves Cell Permeability and Potency of Specific Inhibitors of Proteasome Trypsin-like Sites
about
The 26S proteasome is a multifaceted target for anti-cancer therapiesAssessing subunit dependency of the Plasmodium proteasome using small molecule inhibitors and active site probesMulticolor monitoring of the proteasome's catalytic signature.The novel β2-selective proteasome inhibitor LU-102 decreases phosphorylation of I kappa B and induces highly synergistic cytotoxicity in combination with ibrutinib in multiple myeloma cells.Subunit specific inhibitors of proteasomes and their potential for immunomodulationThe novel β2-selective proteasome inhibitor LU-102 synergizes with bortezomib and carfilzomib to overcome proteasome inhibitor resistance of myeloma cells.Discovery of an Inhibitor of the Proteasome Subunit Rpn11.Template-constrained macrocyclic peptides prepared from native, unprotected precursorsBlockade of the malignant phenotype by β-subunit selective noncovalent inhibition of immuno- and constitutive proteasomes.Small-molecule control of intracellular protein levels through modulation of the ubiquitin proteasome systemApplications of copper-catalyzed click chemistry in activity-based protein profiling.Peptide-based proteasome inhibitors in anticancer drug design.Activity-based probes for the multicatalytic proteasome.Downregulation of 26S proteasome catalytic activity promotes epithelial-mesenchymal transition.Sulfur-Switch Ugi Reaction for Macrocyclic Disulfide-Bridged Peptidomimetics.Inhibition of the Proteasome β2 Site Sensitizes Triple-Negative Breast Cancer Cells to β5 Inhibitors and Suppresses Nrf1 Activation.A Set of Activity-Based Probes to Visualize Human (Immuno)proteasome Activities.
P2860
Q26795764-664A6B43-81E4-47BE-A530-1B0508E80165Q34061291-547372C7-8172-4629-A2A9-D5F35E1DFE7CQ35121111-C3989726-F16C-4F18-8AC4-C68BCA417DDAQ35889653-1F3D4907-EAA0-471A-BE6A-13684C9AA913Q36042649-B405B207-E3EE-4620-945F-438DE2579374Q36115692-A7096435-4386-4483-A319-974BB2E12457Q36278259-6EBF3186-B622-458B-BD2A-70A19C0C274EQ37218436-93B35385-7758-400A-91F2-0A8321F7B319Q37705854-0DF712C2-FAA1-4653-B8E3-9725846457DDQ38181445-91BFCACE-4123-4539-9940-49C22C8F6A8EQ38182819-2D2A89A9-368C-457B-A03B-10055A5A08CCQ38192572-27E703AD-DDAE-4951-AD7E-339E5E6968BEQ39096761-594172A9-61C0-4D6D-B031-34E4E83072B6Q40996336-7C2165D8-77F5-4055-AF70-94B9761ED1DDQ41092301-3B7347F8-E3BA-46C7-AB48-8456A070A2A9Q47987649-08919DE9-4151-41E4-8FC6-500E9D71728BQ53461880-6E9899CC-761B-4886-A9B1-BD903D8C6F06
P2860
Incorporation of Non-natural Amino Acids Improves Cell Permeability and Potency of Specific Inhibitors of Proteasome Trypsin-like Sites
description
2013 nî lūn-bûn
@nan
2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@ast
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@en
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@nl
type
label
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@ast
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@en
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@nl
prefLabel
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@ast
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@en
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@nl
P2093
P2860
P50
P356
P1476
Incorporation of Non-natural A ...... Proteasome Trypsin-like Sites
@en
P2093
Alexei F Kisselev
Anne C Mirabella
Annet E M Blom
Christoph Driessen
Elliot D Mock
Gerjan de Bruin
Gijs A van der Marel
Mario van der Stelt
Mathias J Voges
Nerea Gallastegui
P2860
P304
P356
10.1021/JM3016987
P407
P577
2013-02-14T00:00:00Z