Results 321 to 330 of about 1,734,521 (378)

An Aptamer Glue Enables Hyperefficient Targeted Membrane Protein Degradation. [PDF]

JACS Au
Zhang GR, Zhang C, Fu T, Tan W, Wang XQ.
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Protein destroyer: Inducible E3-DART for targeted protein degradation in plants. [PDF]

Plant Cell
Kamble NU.
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Leveraging Dual-Ligase Recruitment to Enhance Protein Degradation via a Heterotrivalent Proteolysis Targeting Chimera. [PDF]

J Am Chem Soc
Bond AG, Muñoz I Ordoño M, Bisbach CM, Craigon C, Makukhin N, Caine EA, Nagala M, Urh M, Winter GE, Riching KM, Ciulli A.   +10 more
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NFAT2 drives both Orai3 transcription and protein degradation by harnessing the differences in epigenetic landscape

Raju S, Sharma A, Ranjan G, Motiani RK.
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Identification of actionable targeted protein degradation effector sites through Site-specific Ligand Incorporation-induced Proximity (SLIP)

Xiao Z, Gavriil ES, Cao F, Zhang X, Li SX, Kotelnikov S, Michalska P, Marte F, Huang C, Lu Y, Zhang Y, Bernardini E, Kozakov D, Tate EW.   +13 more
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Degron tagging for rapid protein degradation in mice.

Dis Model Mech
Hernández-Morán BA, Taylor G, Lorente-Macías Á, Wood AJ.   +3 more
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Lysosomes and protein degradation [PDF]

Biochemical Society Transactions, 1977
Considerable evidence from studies with group-specific proteinase inhibitors, in particular pepstatin, the aspartic proteinase inhibitor, implicates lysosomes in turnover of endogenous cellular proteins. Recent experiments using a new group-specific inhibitor of thiol (cysteine) proteinases, Z-Phe-Ala-diazomethyl ketone, are described.
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Targeted protein degradation and the enzymology of degraders

Current Opinion in Chemical Biology, 2018
Targeted protein degradation is an emerging strategy for drug discovery that employs small molecules to catalyze the ubiquitination of target proteins, ultimately causing their degradation by the proteasome. Current degrader designs employ hetero-bivalent molecules to recruit E3 ubiquitin ligases such as VHL, Cereblon, and the IAPs to the target ...
Stewart L. Fisher, Andrew J. K. Phillips
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Protein folding and degradation in bacteria:¶To degrade or not to degrade? That is the question

Cellular and Molecular Life Sciences, 2002
In Escherichia coli protein quality control is carried out by a protein network, comprising chaperones and proteases. Central to this network are two protein families, the AAA+ and the Hsp70 family. The major Hsp70 chaperone. DnaK, efficiently prevents protein aggregation and supports the refolding of damaged proteins. In a special case, DnaK, together
Dougan, David A., Mogk, Axel, Bukau, Bernd   +2 more
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