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K Strub

Showing results (1-10 of 29) with videos related to

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Biological Chemistry|April 9, 1999
New insights into signal recognition and elongation arrest activities of the signal recognition particleN Bui, K Strub
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactionsK Strub, P Walter
Molecular and Cellular Biology|February 1, 1990
Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNAK Strub, P Walter
Journal of Cell Science|November 1, 1996
The signal recognition particle and related small cytoplasmic ribonucleoprotein particlesF Bovia, K Strub
The EMBO Journal|July 1, 1986
Genetic complementation in the Xenopus oocyte: co-expression of sea urchin histone and U7 RNAs restores 3' processing of H3 pre-mRNA in the oocyteK Strub, M L Birnstiel
Cellular and Molecular Life Sciences : CMLS|May 22, 2007
Useful 'junk': Alu RNAs in the human transcriptomeJ Häsler, T Samuelsson, K Strub
Nucleic Acids Research|May 15, 1997
A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particleY Thomas, N Bui, K Strub
Molecular and Cellular Biology|August 1, 1991
Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolutionK Strub, J Moss, P Walter
RNA (New York, N.Y.)|November 26, 1999
The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structureK Strub, M Fornallaz, N Bui
Nucleic Acids Research|June 11, 1994
The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chainF Bovia, N Bui, K Strub
Pageof 3

Showing results (1-10 of 29) with videos related to

Sort By:
Pageof 3
Biological Chemistry|April 9, 1999
New insights into signal recognition and elongation arrest activities of the signal recognition particleN Bui, K Strub
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactionsK Strub, P Walter
Molecular and Cellular Biology|February 1, 1990
Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNAK Strub, P Walter
Journal of Cell Science|November 1, 1996
The signal recognition particle and related small cytoplasmic ribonucleoprotein particlesF Bovia, K Strub
The EMBO Journal|July 1, 1986
Genetic complementation in the Xenopus oocyte: co-expression of sea urchin histone and U7 RNAs restores 3' processing of H3 pre-mRNA in the oocyteK Strub, M L Birnstiel
Cellular and Molecular Life Sciences : CMLS|May 22, 2007
Useful 'junk': Alu RNAs in the human transcriptomeJ Häsler, T Samuelsson, K Strub
Nucleic Acids Research|May 15, 1997
A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particleY Thomas, N Bui, K Strub
Molecular and Cellular Biology|August 1, 1991
Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolutionK Strub, J Moss, P Walter
RNA (New York, N.Y.)|November 26, 1999
The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structureK Strub, M Fornallaz, N Bui
Nucleic Acids Research|June 11, 1994
The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chainF Bovia, N Bui, K Strub
Pageof 3