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Items: 8

1.
2.

Activation processing of cathepsin H impairs recognition by its propeptide.

Horn M, Dolecková-Maresová L, Rulísek L, Mása M, Vasiljeva O, Turk B, Gan-Erdene T, Baudys M, Mares M.

Biol Chem. 2005 Sep;386(9):941-7.

PMID:
16164419
3.

Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins.

Hemelaar J, Borodovsky A, Kessler BM, Reverter D, Cook J, Kolli N, Gan-Erdene T, Wilkinson KD, Gill G, Lima CD, Ploegh HL, Ovaa H.

Mol Cell Biol. 2004 Jan;24(1):84-95.

4.

DEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1.

Wu K, Yamoah K, Dolios G, Gan-Erdene T, Tan P, Chen A, Lee CG, Wei N, Wilkinson KD, Wang R, Pan ZQ.

J Biol Chem. 2003 Aug 1;278(31):28882-91. Epub 2003 May 19.

5.

Identification and characterization of DEN1, a deneddylase of the ULP family.

Gan-Erdene T, Nagamalleswari K, Yin L, Wu K, Pan ZQ, Wilkinson KD.

J Biol Chem. 2003 Aug 1;278(31):28892-900. Epub 2003 May 19.

6.

Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family.

Borodovsky A, Ovaa H, Kolli N, Gan-Erdene T, Wilkinson KD, Ploegh HL, Kessler BM.

Chem Biol. 2002 Oct;9(10):1149-59.

7.
8.

Disulfide bridges of bovine spleen cathepsin B.

Baudys M, Meloun B, Gan-Erdene T, Pohl J, Kostka V.

Biol Chem Hoppe Seyler. 1990 Jun;371(6):485-91.

PMID:
2390214

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