Proteasome activation during cardiac hypertrophy by the chaperone H11 Kinase/Hsp22 (2008)
Hedhli, Nadia, Wang, Li, Wang, Qian, Rashed, Eman, Tian, Yimin, Sui, Xiangzhen, ...
Aims The regulation of protein degradation by the proteasome during cardiac hypertrophy remains largely unknown. Also, the proteasome translocates to the nuclear periphery in response to cellular...
Proteasome Activation7during Cardiac Hypertrophy by the chaperone H11 Kinase/Hsp22 (2007)
Hedhli, Nadia, Wang, Li, Wang, Qian, Rashed, Eman, Tian, Yimin, Sui, Xiangzhen, ...
Aims The regulation of protein degradation by the proteasome during cardiac hypertrophy remains largely unknown. Also, the proteasome translocates to the nuclear periphery in response to cellular...
Proteasome activation during cardiac hypertrophy by the chaperone H11 Kinase/Hsp22 (2007)
Hedhli, Nadia, Wang, Li, Wang, Qian, Rashed, Eman, Tian, Yimin, Sui, Xiangzhen, ...
Aims The regulation of protein degradation by the proteasome during cardiac hypertrophy remains largely unknown. Also, the proteasome translocates to the nuclear periphery in response to cellular...
Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway (2004)
Ortolan, Tatiana G., Chen, Li, Tongaonkar, Prasad, Madura, Kiran
Rad23 protein interacts with the nucleotide excision-repair (NER) factor Rad4, and the dimer can bind damaged DNA. Rad23 also binds ubiquitinated proteins and promotes their degradation by the...
Lommel, Lori, Chen, Li, Madura, Kiran, Sweder, Kevin
Regulation of protein expression can be achieved through destruction of proteins by the 26S proteasome. Cellular processes that are regulated by proteolysis include cell cycle progression, stress...
The N-End Rule is Mediated by the UBC2(RAD6) Ubiquitin-Conjugating Enzyme (1991)
Dohmen, R. Jurgen, Madura, Kiran, Bartel, Bonnie, Varshavsky, Alexander
The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all organisms examined, from mammals to...
Madura, Kiran, Prakash, Satya, Prakash, Louise
The RAD6 gene of Saccharomyces cerevisiae encodes a ubiquitin-conjugating (E2) enzyme and is required for the repair of damaged DNA, mutagenesis, and sporulation. Here, we report our studies on the...
The RAD23 gene of Saccharomyces cerevisiae is required for excision-repair of UV damaged DNA. In this paper, we determine the location of the RAD23 genein a cloned DNA fragment, identify the 1.6 kb...
Long internal inverted repeat in a yeast viral double-stranded RNA (1985)
Bruenn, Jeremy, Madura, Kiran, Siegel, Alan, Miner, Zoe, Lee, Myunghee
The Saccharomyces cerevisiae viruses are non-infectious double-stranded (ds) RNA viruses present in most laboratory strains of yeast. Their genome consists of one or more dsRNAs separately...
Evidence for an Interaction between Ubiquitin-Conjugating Enzymes and the 26S Proteasome
Tongaonkar, Prasad, Chen, Li, Lambertson, David, Ko, Bom, Madura, Kiran
The targeting of proteolytic substrates is accomplished by a family of ubiquitin-conjugating (E2) enzymes and a diverse set of substrate recognition (E3) factors. The ligation of a multiubiquitin...
The 26S proteasome negatively regulates the level of overall genomic nucleotide excision repair
Lommel, Lori, Chen, Li, Madura, Kiran, Sweder, Kevin
Regulation of protein expression can be achieved through destruction of proteins by the 26S proteasome. Cellular processes that are regulated by proteolysis include cell cycle progression, stress...
Rad23 Promotes the Targeting of Proteolytic Substrates to the Proteasome
Rad23 contains a ubiquitin-like domain (UbLR23) that interacts with catalytically active proteasomes and two ubiquitin (Ub)-associated (UBA) sequences that bind Ub. The UBA domains can bind Ub in...
Doss-Pepe, Ellen W., Stenroos, Edward S., Johnson, William G., Madura, Kiran
Machado-Joseph disease is caused by an expansion of a trinucleotide CAG repeat in the gene encoding the protein ataxin-3. We investigated if ataxin-3 was a proteasome-associated factor that...
Chuang, Show-Mei, Chen, Li, Lambertson, David, Anand, Monika, Kinzy, Terri Goss, Madura, Kiran
Rad23 and Rpn10 play synergistic roles in the recognition of ubiquitinated proteins by the proteasome, and loss of both proteins causes growth and proteolytic defects. However, the physiological...
Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway
Ortolan, Tatiana G., Chen, Li, Tongaonkar, Prasad, Madura, Kiran
Rad23 protein interacts with the nucleotide excision-repair (NER) factor Rad4, and the dimer can bind damaged DNA. Rad23 also binds ubiquitinated proteins and promotes their degradation by the...
Chen, Li, Shinde, Ujwal, Ortolan, Tatiana G., Madura, Kiran
Rad23 is a DNA repair protein that promotes the assembly of the nucleotide excision repair complex. Rad23 can interact with the 26S proteasome through an N-terminal ubiquitin-like domain, and...
Chuang, Show-Mei, Madura, Kiran
Surveillance mechanisms that monitor protein synthesis can promote rapid elimination of misfolded nascent proteins. We showed that the translation elongation factor eEF1A and the proteasome subunit...
Evidence for an Interaction between Ubiquitin-Conjugating Enzymes and the 26S Proteasome
Tongaonkar, Prasad, Chen, Li, Lambertson, David, Ko, Bom, Madura, Kiran
The targeting of proteolytic substrates is accomplished by a family of ubiquitin-conjugating (E2) enzymes and a diverse set of substrate recognition (E3) factors. The ligation of a multiubiquitin...
The 26S proteasome negatively regulates the level of overall genomic nucleotide excision repair
Lommel, Lori, Chen, Li, Madura, Kiran, Sweder, Kevin
Regulation of protein expression can be achieved through destruction of proteins by the 26S proteasome. Cellular processes that are regulated by proteolysis include cell cycle progression, stress...
Rad23 Promotes the Targeting of Proteolytic Substrates to the Proteasome
Rad23 contains a ubiquitin-like domain (UbLR23) that interacts with catalytically active proteasomes and two ubiquitin (Ub)-associated (UBA) sequences that bind Ub. The UBA domains can bind Ub in...
Doss-Pepe, Ellen W., Stenroos, Edward S., Johnson, William G., Madura, Kiran
Machado-Joseph disease is caused by an expansion of a trinucleotide CAG repeat in the gene encoding the protein ataxin-3. We investigated if ataxin-3 was a proteasome-associated factor that...
Chuang, Show-Mei, Chen, Li, Lambertson, David, Anand, Monika, Kinzy, Terri Goss, Madura, Kiran
Rad23 and Rpn10 play synergistic roles in the recognition of ubiquitinated proteins by the proteasome, and loss of both proteins causes growth and proteolytic defects. However, the physiological...
Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway
Ortolan, Tatiana G., Chen, Li, Tongaonkar, Prasad, Madura, Kiran
Rad23 protein interacts with the nucleotide excision-repair (NER) factor Rad4, and the dimer can bind damaged DNA. Rad23 also binds ubiquitinated proteins and promotes their degradation by the...
Chen, Li, Shinde, Ujwal, Ortolan, Tatiana G., Madura, Kiran
Rad23 is a DNA repair protein that promotes the assembly of the nucleotide excision repair complex. Rad23 can interact with the 26S proteasome through an N-terminal ubiquitin-like domain, and...
Chuang, Show-Mei, Madura, Kiran
Surveillance mechanisms that monitor protein synthesis can promote rapid elimination of misfolded nascent proteins. We showed that the translation elongation factor eEF1A and the proteasome subunit...
Centrin/Cdc31 Is a Novel Regulator of Protein Degradation▿
Rad23 is required for efficient protein degradation and performs an important role in nucleotide excision repair. Saccharomyces cerevisiae Rad23, and its human counterpart (hHR23), are present in a...
Proteasome inhibition decreases cardiac remodeling after initiation of pressure overload
Hedhli, Nadia, Lizano, Paulo, Hong, Chull, Fritzky, Luke F., Dhar, Sunil K., Liu, Huasheng, ...
We tested the possibility that proteasome inhibition may reverse preexisting cardiac hypertrophy and improve remodeling upon pressure overload. Mice were submitted to aortic banding and followed up...