Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Dennis L, Maeder"'
Autor:
Wirojne Kanoksilapatham, Juan M. González, Dennis L. Maeder, Jocelyne DiRuggiero, Frank T. Robb
Publikováno v:
Archaea, Vol 1, Iss 4, Pp 277-283 (2004)
Pyrococcus species are hyperthermophilic members of the order Thermococcales, with optimal growth temperatures approaching 100 °C. All species grow heterotrophically and produce H2 or, in the presence of elemental sulfur (S°), H2S. Pyrococcus woese
Externí odkaz:
https://doaj.org/article/9e3163ff45c8485db06a8842c65830db
Publikováno v:
The Journal of Nutritional Biochemistry. 20:1000-1012
We have demonstrated that zinc exposure induces apoptosis in human prostate cancer cells (PC-3) and benign hyperplasia cells (BPH), but not in normal prostate cells (HPR-1). However, the mechanisms underlying the effects of zinc on prostate cancer ce
Publikováno v:
Journal of Molecular Evolution. 60:409-416
Group II chaperonins belong to the Hsp60 family occurring in archaea and eukaryotes. The archaeal chaperonins build the thermosome, which is similar to the eukaryotic CCT (chaperonin-containing TCP-1). Eukaryotes have eight subunits, and up until now
Autor:
Frederick P. Schwarz, M. Ökvist, Lennart Sjölin, B. Göran Karlsson, Anna Katarina Tigerström, Dennis L. Maeder, Carmen Alvarez-Rúa, Frank T. Robb
Publikováno v:
Biochemistry. 43:12563-12574
Identification and evaluation of factors important for thermostability in proteins is a growing research field with many industrial applications. This study investigates the effects of introducing a novel disulfide bond and engineered electrostatic i
Autor:
Wirojne Kanoksilapatham, Jocelyne DiRuggiero, Dennis L. Maeder, Juan M. Gonzalez, Frank T. Robb
Publikováno v:
Archaea, Vol 1, Iss 4, Pp 277-283 (2004)
Pyrococcusspecies are hyperthermophilic members of the order Thermococcales, with optimal growth temperatures approaching 100 °C. All species grow heterotrophically and produce H2or, in the presence of elemental sulfur (S°), H2S.Pyrococcus woeseian
Autor:
David W. Rice, Dennis L. Maeder, Frank T. Robb, Kitty S. P. Yip, Svetlana E. Sedelnikova, Michael W. W. Adams, Nicola Tolliday, K.L. Britton, Costantino Vetriani, Kesen Ma, Timothy J. Stillman, Patrick J. Baker
Publikováno v:
Journal of Molecular Biology. 293:1121-1132
Glutamate dehydrogenase catalyses the oxidative deamination of glutamate to 2-oxoglutarate with concomitant reduction of NAD(P)+, and has been shown to be widely distributed in nature across species ranging from psychrophiles to hyperthermophiles. Ex
Autor:
Juan M. Gonzalez, Jocelyne DiRuggiero, Robert B. Weiss, Frank T. Robb, Dennis L. Maeder, Joshua L. Cherry, Diane M. Dunn
Publikováno v:
Europe PubMed Central
Divergence of the hyperthermophilic Archaea, Pyrococcus furiosus and Pyrococcus horikoshii, was assessed by analysis of complete genomic sequences of both species. The average nucleotide identity between the genomic sequences is 70-75% within ORFs. T
Autor:
David W. Rice, Frank T. Robb, Costantino Vetriani, Nicola Tolliday, Dennis L. Maeder, Kitty S. P. Yip, Timothy J. Stillman, K. Linda Britton, Horst H. Klump
Publikováno v:
Proceedings of the National Academy of Sciences. 95:12300-12305
The discovery of hyperthermophilic microorganisms and the analysis of hyperthermostable enzymes has established the fact that multisubunit enzymes can survive for prolonged periods at temperatures above 100°C. We have carried out homology-based mode
Autor:
Dennis L. Maeder, Willem M. de Vos, J.H.G. Lebbink, Kitty S. P. Yip, K. Linda Britton, David W. Rice, Timothy J. Stillman, Frank T. Robb, Constantino Vetriani
Publikováno v:
Scopus-Elsevier
European Journal of Biochemistry, 255, 336-346
European Journal of Biochemistry 255 (1998)
European Journal of Biochemistry, 255, 336-346
European Journal of Biochemistry 255 (1998)
The recent structure determination of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus and the comparison of this structure with its counterparts from the mesophiles Clostridium symbiosum and Escherichia coli has highlighted the
Publikováno v:
Seed Science Research. 5:137-144
An LEA-like protein has been isolated and characterized from pea (Pisum sativum) embryos. It is the most prevalent protein in a homogenate of pea axes heated for 10 min at 80°C and then centifuged for 10 min at 17000g(80°C supernatant fraction). It