Results 11 to 20 of about 3,152 (182)

Dissociation and reconstitution of the Thermoplasma proteasome

European Journal of Biochemistry, 1994
The proteasome from the thermoacidophilic archaeon Thermoplasma acidophilum in its native state represents a 20S particle with significant secondary structure (approximately 35% alpha helix) of its subunits.
Grziwa, A., Jaenicke, R., Wiegand, G., Pühler, G., Baumeister, W., Maack, S.   +5 more
core   +4 more sources

Ubiquitin found in the archaebacterium Thermoplasma acidophilum

FEBS Letters, 1993
Systematic N-terminal sequencing of the low molecular weight proteins from Thermoplasma acidophilum separated by two-dimensional poly-acrylamide gel electrophoresis led to the discovery of a polypeptide with an apparent M(r) of 4.5 kDa identical as its ...
Lottspeich, Friedrich, Stefan Wolf, Baumeister, Wolfgang, Wolf, S., Wolfgang Baumeister, Baumeister, W., Friedrich Lottspeich, Lottspeich, F., Wolf, Stefan   +8 more
core   +4 more sources

Proteomics Analysis of Thermoplasma Quinone Droplets.

PROTEOMICS, 2019
A novel type of lipid droplet/lipoprotein (LD/LP) particle from Thermoplasma acidophilum has been identified recently, and based on biochemical evidences, it was named Thermoplasma Quinone Droplet (TaQD).
Varga, S., Nagy, I., Zinzula, L., Boicu, M., Kukolya, J., Sun, N.   +5 more
core   +4 more sources

The chaperones of the archaeon Thermoplasma acidophilum

Journal of Structural Biology, 2001
Chaperones are an essential component of a cell's ability to respond to environmental challenges. Chaperones have been studied primarily in bacteria, but in recent years it has become apparent that some classes of chaperones either are very divergent in ...
Gutsche, I., Lupas, A. ; https://orcid.org/, Ruepp, A., Baumeister, W., Rockel, B.   +4 more
core   +5 more sources

Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum.

PLoS ONE, 2015
Thermoplasma acidophilum is a thermophilic archaeon that uses both non-phosphorylative Entner-Doudoroff (ED) pathway and Embden-Meyerhof-Parnas (EMP) pathway for glucose degradation.
Sang Ho Park, Hyoun Sook Kim, Mi Seul Park, Sojin Moon, Mi Kyung Song, Han Su Park, Hyunggu Hahn, Soon-Jong Kim, Euiyoung Bae, Hyun-Jung Kim, Byung Woo Han   +10 more
doaj   +2 more sources

Proteasome from thermoplasma acidophilum - a threonine protease

Science, 1995
The catalytic mechanism of the 20S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the beta subunit and by inhibitor studies.
Stock, D., Jan Löwe, Andrei Lupas, Daniela Stock, Wolfgang Baumeister, Erika Seemüller, Lupas, A., Baumeister, W., Löwe, J., Robert Huber, Huber, R., Seemüller, E.   +11 more
core   +5 more sources

Crystal structure of the Thermoplasma acidophilum protein Ta1207 [PDF]

Acta Crystallographica Section F Structural Biology Communications, 2017
The crystal structure of the Ta1207 protein from Thermoplasma acidophilum is reported. Ta1207 was identified in a screen for high-molecular-weight protein complexes in T. acidophilum. In solution, Ta1207 forms homopentamers of 188 kDa.
Hubert, A., Nagy, I., Pathare, G., Thomas, D., Bracher, A.   +4 more
core   +4 more sources

Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaebacterium Thermoplasma acidophilum

PROTEOMICS, 1986
It has been found that the thermoacidophilic archaebacterium, Thermoplasma acidophilum, can metabolise glucose via a modified Entner-Doudoroff pathway involving non-phosphorylated intermediates.
Nigel Budgen, Budgen, Nigel, Michael J. Danson, Danson, Michael J.   +3 more
core   +4 more sources

Lipids of Thermoplasma acidophilum [PDF]

Journal of Bacteriology, 1972
Cells of Thermoplasma acidophilum contain about 3% total lipid on a dry weight basis. Total lipid was found to contain 17.5% neutral lipid, 25.1% glycolipid, and 56.6% phospholipid by chromatography on silicic acid.
T A, Langworthy, P F, Smith, W R, Mayberry   +2 more
  +12 more sources

Primary structure of the thermosome from thermoplasma acidophilum

Biological Chemistry Hoppe-Seyler, 1995
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subunits (M(r) 58 000 and 60 000) which assemble into a cylindrical complex of pseudo eight-fold rotational symmetry.
Kellermann, J., Thomas Waldmann, Jürgen Peters, Waldmann, T., Andrei Lupas, Wolfgang Baumeister, Lupas, A., Baumeister, W., Josef Kellermann, Peters, J.   +9 more
core   +5 more sources