Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation

Search Page

My NCBI Filters
Text availability
Article attribute
Article type
Publication date

Search Results

120 results
Filters applied: . Clear all Results are displayed in a computed author sort order. Results by year timeline is unavailable
Page 1
The HHpred interactive server for protein homology detection and structure prediction.
Söding J, Biegert A, Lupas AN. Söding J, et al. Nucleic Acids Res. 2005 Jul 1;33(Web Server issue):W244-8. doi: 10.1093/nar/gki408. Nucleic Acids Res. 2005. PMID: 15980461 Free PMC article.
Do G protein subunits associate via a three-stranded coiled coil?
Lupas AN, Lupas JM, Stock JB. Lupas AN, et al. FEBS Lett. 1992 Dec 14;314(2):105-8. doi: 10.1016/0014-5793(92)80952-d. FEBS Lett. 1992. PMID: 1459238
Model structure of the Omp alpha rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima.
Lupas A, Müller S, Goldie K, Engel AM, Engel A, Baumeister W. Lupas A, et al. J Mol Biol. 1995 Apr 21;248(1):180-9. doi: 10.1006/jmbi.1995.0210. J Mol Biol. 1995. PMID: 7731042
Omp alpha is an outer-membrane protein that spans the periplasmic space of the hyperthermophilic eubacterium Thermotoga maritima. ...The Omp alpha rod is a tetramer with an unusual periodicity of hydrophobic residues close to 3.6 that differs from the 3.5 periodicit …
Omp alpha is an outer-membrane protein that spans the periplasmic space of the hyperthermophilic eubacterium Thermotoga maritima. ... …
The Thermoplasma acidophilum rpl15 gene encodes a homologue of eukaryotic ribosomal proteins L15/YL10.
Zwickl P, Lupas A, Baumeister W. Zwickl P, et al. Biochem Biophys Res Commun. 1995 Apr 17;209(2):684-8. doi: 10.1006/bbrc.1995.1553. Biochem Biophys Res Commun. 1995. PMID: 7733938
This gene, rpl15, was identified as an open reading frame (ORF) located 2.3 kb upstream of the gene encoding the alpha-subunit of the T. acidophilum proteasome. ...
This gene, rpl15, was identified as an open reading frame (ORF) located 2.3 kb upstream of the gene encoding the alpha-subunit of the …
Tetrabrachion: a filamentous archaebacterial surface protein assembly of unusual structure and extreme stability.
Peters J, Nitsch M, Kühlmorgen B, Golbik R, Lupas A, Kellermann J, Engelhardt H, Pfander JP, Müller S, Goldie K, et al. Peters J, et al. J Mol Biol. 1995 Jan 27;245(4):385-401. doi: 10.1006/jmbi.1994.0032. J Mol Biol. 1995. PMID: 7837271
The unique structure of tetrabrachion is reflected in an extreme thermal stability in the presence of strong denaturants (1% (w/v) SDS of 6M guanidine): the arms, which are stabilized by intramolecular disulphide bridges, melt around 115 degrees C under non-reducing condit …
The unique structure of tetrabrachion is reflected in an extreme thermal stability in the presence of strong denaturants (1% (w/v) SD …
Prediction and analysis of coiled-coil structures.
Lupas A. Lupas A. Methods Enzymol. 1996;266:513-25. doi: 10.1016/s0076-6879(96)66032-7. Methods Enzymol. 1996. PMID: 8743703 No abstract available.
Coiled coils: new structures and new functions.
Lupas A. Lupas A. Trends Biochem Sci. 1996 Oct;21(10):375-82. Trends Biochem Sci. 1996. PMID: 8918191 Review.
Predicting coiled-coil regions in proteins.
Lupas A. Lupas A. Curr Opin Struct Biol. 1997 Jun;7(3):388-93. doi: 10.1016/s0959-440x(97)80056-5. Curr Opin Struct Biol. 1997. PMID: 9204281 Review.
120 results
Jump to page
Feedback