Distinct activation of an E2 ubiquitin-conjugating enzyme by its cognate E3 ligases von Cohen, Itamar, Wiener, Reuven, Reiss, Yuval, Ravid, Tommer

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The Hunt for Degrons of the 26S Proteasome von Ella, Hadar, Reiss, Yuval, Ravid, Tommer

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Releasing the Lockdown: An Emerging Role for the Ubiquitin-Proteasome System in the Breakdown of Transient Protein Inclusions von Reiss, Yuval, Gur, Elisheva, Ravid, Tommer

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Ubiquitin Ligase Activity and Tyrosine Phosphorylation Underlie Suppression of Growth Factor Signaling by c-Cbl/Sli-1 von Levkowitz, Gil, Waterman, Hadassa, Ettenberg, Seth A, Katz, Menachem, Tsygankov, Alexander Y, Alroy, Iris, Lavi, Sara, Iwai, Kazuhiro, Reiss, Yuval, Ciechanover, Aaron, Lipkowitz, Stanley, Yarden, Yosef

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Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding von Amit, Ido, Yakir, Liat, Katz, Menachem, Zwang, Yaara, Marmor, Mina D, Citri, Ami, Shtiegman, Keren, Alroy, Iris, Tuvia, Shmuel, Reiss, Yuval, Roubini, Eli, Cohen, Maya, Wides, Ron, Bacharach, Eran, Schubert, Ullrich, Yarden, Yosef

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ubiquitin E3 ligase POSH regulates calcium homeostasis through spatial control of Herp von Tuvia, Shmuel, Taglicht, Daniel, Erez, Omri, Alroy, Iris, Alchanati, Iris, Bicoviski, Vivian, Dori-Bachash, Mally, Ben-Avraham, Danny, Reiss, Yuval

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Sequential Poly-ubiquitylation by Specialized Conjugating Enzymes Expands the Versatility of a Quality Control Ubiquitin Ligase von Weber, Annika, Cohen, Itamar, Popp, Oliver, Dittmar, Gunnar, Reiss, Yuval, Sommer, Thomas, Ravid, Tommer, Jarosch, Ernst

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The Trans-Golgi Network-Associated Human Ubiquitin-Protein Ligase POSH Is Essential for HIV Type 1 Production von Alroy, Iris, Tuvia, Shmuel, Greener, Tsvika, Gordon, Daphna, Barr, Haim M., Taglicht, Daniel, Mandil-Levin, Revital, Ben-Avraham, Danny, Konforty, Dalit, Nir, Anat, Levius, Orit, Bicoviski, Vivian, Dori, Mally, Cohen, Shenhav, Yaar, Liora, Erez, Omri, Propheta-Meiran, Oshrat, Koskas, Mordechai, Caspi-Bachar, Elanite, Alchanati, Iris, Sela-Brown, Alin, Moskowitz, Haim, Tessmer, Uwe, Schubert, Ulrich, Reiss, Yuval, Hershko, Avram

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The Mouse and Human Genes Encoding the Recognition Component of the N-End Rule Pathway von Kwon, Yong Tae, Reiss, Yuval, Fried, Victor A., Hershko, Avram, Yoon, Jeong Kyo, Gonda, David K., Sangan, Pitchai, Copeland, Neal G., Jenkins, Nancy A., Varshavsky, Alexander

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Inhibition of purified p21ras farnesyl : protein transferase by Cys-AAX tetrapeptides von REISS, Y, GOLDSTEIN, J. L, SEABRA, M. C, CASEY, P. J, BROWN, M. S

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A Role for a Novel Luminal Endoplasmic Reticulum Aminopeptidase in Final Trimming of 26 S Proteasome-generated Major Histocompatability Complex Class I Antigenic Peptides von Komlosh, Arthur, Momburg, Frank, Weinschenk, Toni, Emmerich, Niels, Schild, Hansjörg, Nadav, Eran, Shaked, Isabella, Reiss, Yuval

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Exploring the functional interaction between POSH and ALIX and the relevance to HIV-1 release von Votteler, Jörg, Iavnilovitch, Elena, Fingrut, Orit, Shemesh, Vivian, Taglicht, Daniel, Erez, Omri, Sörgel, Stefan, Walther, Torsten, Bannert, Norbert, Schubert, Ulrich, Reiss, Yuval

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26 S Proteasome-mediated Production of an Authentic Major Histocompatibility Class I-restricted Epitope from an Intact Protein Substrate von Ben-Shahar, Sary, Komlosh, Arthur, Nadav, Eran, Shaked, Isabella, Ziv, Tamar, Admon, Arie, DeMartino, George N., Reiss, Yuval

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Placing a Disrupted Degradation Motif at the C Terminus of Proteasome Substrates Attenuates Degradation without Impairing Ubiquitylation von Alfassy, Omri S., Cohen, Itamar, Reiss, Yuval, Tirosh, Boaz, Ravid, Tommer

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Assays for dissecting the in vitro enzymatic activity of yeast Ubc7 von Mashahreh, Bayan, Reiss, Yuval, Wiener, Reuven, Ravid, Tommer

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Efficient presentation of exogenous antigen by liver endothelial cells to CD8 + T cells results in antigen-specific T-cell tolerance von Knolle, Percy A, Limmer, Andreas, Ohl, Jutta, Kurts, Christian, Ljunggren, Hans-Gustaf, Reiss, Yuval, Groettrup, Marcus, Momburg, Frank, Arnold, Bernd

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The E3 Ubiquitin-Ligase Bmi1/Ring1A Controls the Proteasomal Degradation of Top2α Cleavage Complex – A Potentially New Drug Target von Alchanati, Iris, Teicher, Carmit, Cohen, Galit, Shemesh, Vivian, Barr, Haim M., Nakache, Philippe, Ben-Avraham, Danny, Idelevich, Anna, Angel, Itzchak, Livnah, Nurit, Tuvia, Shmuel, Reiss, Yuval, Taglicht, Daniel, Erez, Omri

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Degradation of Ndd1 by APC/C(Cdh1) generates a feed forward loop that times mitotic protein accumulation von Sajman, Julia, Zenvirth, Drora, Nitzan, Mor, Margalit, Hanah, Simpson-Lavy, Kobi J, Reiss, Yuval, Cohen, Itamar, Ravid, Tommer, Brandeis, Michael

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Degradation of Ndd1 by APC/CCdh1 generates a feed forward loop that times mitotic protein accumulation von Sajman, Julia, Zenvirth, Drora, Nitzan, Mor, Margalit, Hanah, Simpson-Lavy, Kobi J., Reiss, Yuval, Cohen, Itamar, Ravid, Tommer, Brandeis, Michael

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The E3 ubiquitin-ligase Bmi1/Ring1A controls the proteasomal degradation of Top2alpha cleavage complex - a potentially new drug target von Alchanati, Iris, Teicher, Carmit, Cohen, Galit, Shemesh, Vivian, Barr, Haim M, Nakache, Philippe, Ben-Avraham, Danny, Idelevich, Anna, Angel, Itzchak, Livnah, Nurit, Tuvia, Shmuel, Reiss, Yuval, Taglicht, Daniel, Erez, Omri

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