Z. Kostova

发表

Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation.

A. Weissman, Y. Tsai, Z. Kostova, 2007, Seminars in cell & developmental biology.

A Ubc7p-binding domain in Cue1p activates ER-associated protein degradation

A. Weissman, S. Scholz, Z. Kostova, 2009, Journal of Cell Science.

Temperature-sensitive Yeast GPI Anchoring Mutants gpi2 and gpi3 Are Defective in the Synthesis of N-Acetylglucosaminyl Phosphatidylinositol.

J. Fassler, P. Orlean, W. Gray, 1995, The Journal of Biological Chemistry.

Comparative importance in vivo of conserved glutamate residues in the EX7E motif retaining glycosyltransferase Gpi3p, the UDP-GlcNAc-binding subunit of the first enzyme in glycosylphosphatidylinositol assembly.

P. Orlean, A. Menon, S. Vainauskas, 2003, European journal of biochemistry.

The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system.

P. Coffino, D. Wolf, F. Eisele, 2006, Molecular biology of the cell.

Protein Quality Control in the Export Pathway: The Endoplasmic Reticulum and its Cytoplasmic Proteasome Connection

D. Wolf, Z. Kostova, Zlatka Kostova, 2002 .

Endoplasmic Reticulum Protein Quality Control and Degradation

D. Wolf, Z. Kostova, A. Schäfer, 2007 .

A genomic screen identifies Dsk2p and Rad23p as essential components of ER‐associated degradation

D. Wolf, A. Schaefer, Z. Kostova, 2004, EMBO reports.

For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin–proteasome connection

D. Wolf, Z. Kostova, Zlatka Kostova, 2003, The EMBO journal.

The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation

T. Veenstra, S. Hewitt, A. Weissman, 2007, Nature Medicine.

Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78.

Yien Che Tsai, Ranabir Das, X. Ji, 2009, Molecular cell.

Photoaffinity labelling with P3-(4-azidoanilido)uridine 5'-triphosphate identifies gpi3p as the UDP-GlcNAc-binding subunit of the enzyme that catalyses formation of GlcNAc-phosphatidylinositol, the first glycolipid intermediate in glycosylphosphatidylinositol synthesis.

P. Orlean, A. Menon, D. Rancour, 2000, The Biochemical journal.

Use of Modular Substrates Demonstrates Mechanistic Diversity and Reveals Differences in Chaperone Requirement of ERAD*

R. Hitt, C. Taxis, D. Wolf, 2003, Journal of Biological Chemistry.

A genome‐wide screen identifies Yos9p as essential for ER‐associated degradation of glycoproteins

D. Wolf, Bettina A. Buschhorn, Z. Kostova, 2004, FEBS letters.

A structurally unique E2-binding domain activates ubiquitination by the ERAD E2, Ubc7p, through multiple mechanisms.

X. Ji, A. Weissman, Jess Li, 2013, Molecular cell.

Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation

D. Wolf, Z. Kostova, Zlatka Kostova, 2005, Journal of Cell Science.