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1 |
Material Type: Artigo
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Inhibition of mitochondrial LonP1 protease by allosteric blockade of ATP binding and hydrolysis via CDDO and its derivativesLee, Jae ; Pandey, Ashutosh K. ; Venkatesh, Sundararajan ; Thilagavathi, Jayapalraja ; Honda, Tadashi ; Singh, Kamal ; Suzuki, Carolyn K.The Journal of biological chemistry, 2022-03, Vol.298 (3), p.101719-101719, Article 101719 [Periódico revisado por pares]United States: Elsevier IncTexto completo disponível |
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Material Type: Artigo
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DNA and RNA Binding by the Mitochondrial Lon Protease Is Regulated by Nucleotide and Protein SubstrateLiu, Tong ; Lu, Bin ; Lee, Irene ; Ondrovicová, Gabriela ; Kutejová, Eva ; Suzuki, Carolyn KThe Journal of biological chemistry, 2004-04, Vol.279 (14), p.13902-13910 [Periódico revisado por pares]United States: American Society for Biochemistry and Molecular BiologyTexto completo disponível |
3 |
Material Type: Artigo
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Roles for the Human ATP-dependent Lon Protease in Mitochondrial DNA MaintenanceLu, Bin ; Yadav, Swati ; Shah, Parul G. ; Liu, Tong ; Tian, Bin ; Pukszta, Sebastian ; Villaluna, Nerissa ; Kutejovaé, Eva ; Newlon, Carol S. ; Santos, Janine H. ; Suzuki, Carolyn K.The Journal of biological chemistry, 2007-06, Vol.282 (24), p.17363-17374 [Periódico revisado por pares]United States: Elsevier IncTexto completo disponível |
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Material Type: Artigo
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Tid1 Isoforms Are Mitochondrial DnaJ-like Chaperones with Unique Carboxyl Termini That Determine Cytosolic FateLu, Bin ; Garrido, Nuria ; Spelbrink, Johannes N. ; Suzuki, Carolyn K.The Journal of biological chemistry, 2006-05, Vol.281 (19), p.13150-13158 [Periódico revisado por pares]United States: Elsevier IncTexto completo disponível |
5 |
Material Type: Artigo
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Cleavage Site Selection within a Folded Substrate by the ATP-dependent Lon ProteaseOndrovičová, Gabriela ; Liu, Tong ; Singh, Kamalendra ; Tian, Bin ; Li, Hong ; Gakh, Oleksandr ; Perečko, Dusan ; Janata, Jiří ; Granot, Zvi ; Orly, Joseph ; Kutejová, Eva ; Suzuki, Carolyn K.The Journal of biological chemistry, 2005-07, Vol.280 (26), p.25103-25110 [Periódico revisado por pares]United States: Elsevier IncTexto completo disponível |
6 |
Material Type: Artigo
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Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscleSorimachi, H. ; Toyama-Sorimachi, N. ; Saido, T.C. ; Kawasaki, H. ; Sugita, H. ; Miyasaka, M. ; Arahata, K. ; Ishiura, S. ; Suzuki, K.The Journal of biological chemistry, 1993-05, Vol.268 (14), p.10593-10605 [Periódico revisado por pares]Bethesda, MD: Elsevier IncTexto completo disponível |
7 |
Material Type: Artigo
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Matrix metalloproteinases degrade insulin-like growth factor-binding protein-3 in dermal fibroblast culturesFowlkes, J L ; Enghild, J J ; Suzuki, K ; Nagase, HThe Journal of biological chemistry, 1994-10, Vol.269 (41), p.25742-25746 [Periódico revisado por pares]United States: Elsevier IncTexto completo disponível |
8 |
Material Type: Artigo
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Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectinWATANABE, T ; SUZUKI, K ; OYANAGI, W ; OHNISHI, K ; TANAKA, HThe Journal of biological chemistry, 1990-09, Vol.265 (26), p.15659-15665 [Periódico revisado por pares]Bethesda, MD: American Society for Biochemistry and Molecular BiologyTexto completo disponível |
9 |
Material Type: Artigo
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Suppression of antioxidative enzyme expression by transforming growth factor-beta 1 in rat hepatocytesKayanoki, Y ; Fujii, J ; Suzuki, K ; Kawata, S ; Matsuzawa, Y ; Taniguchi, NThe Journal of biological chemistry, 1994-06, Vol.269 (22), p.15488-15492 [Periódico revisado por pares]United States: American Society for Biochemistry and Molecular BiologyTexto completo disponível |
10 |
Material Type: Artigo
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Spatial resolution of fodrin proteolysis in postischemic brainSaido, T C ; Yokota, M ; Nagao, S ; Yamaura, I ; Tani, E ; Tsuchiya, T ; Suzuki, K ; Kawashima, SThe Journal of biological chemistry, 1993-11, Vol.268 (33), p.25239-25243 [Periódico revisado por pares]United States: Elsevier IncTexto completo disponível |