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D M Freymann

Showing results (1-10 of 12) with videos related to

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Structure (London, England : 1993)|September 22, 2001
The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPaseS Padmanabhan, D M Freymann
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1993
Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homologH D Bernstein, D Zopf, D M Freymann, et al.
Nature|September 13, 1984
6 A-resolution X-ray structure of a variable surface glycoprotein from Trypanosoma bruceiD M Freymann, P Metcalf, M Turner, et al.
Nature Structural Biology|July 30, 1999
Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDPD M Freymann, R J Keenan, R M Stroud, et al.
Nature|January 23, 1997
Structure of the conserved GTPase domain of the signal recognition particleD M Freymann, R J Keenan, R M Stroud, et al.
Cell|August 8, 1998
Crystal structure of the signal sequence binding subunit of the signal recognition particleR J Keenan, D M Freymann, P Walter, et al.
Annual Review of Biochemistry|June 8, 2001
The signal recognition particleR J Keenan, D M Freymann, R M Stroud, et al.
Journal of Molecular Biology|March 25, 2000
The crystal structure of thymidylate synthase from Pneumocystis carinii reveals a fungal insert important for drug designA C Anderson, K M Perry, D M Freymann, et al.
Science (New York, N.Y.)|June 2, 2000
Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptorP Peluso, D Herschlag, S Nock, et al.
RNA (New York, N.Y.)|December 1, 1996
NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP)U Schmitz, D M Freymann, T L James, et al.
Pageof 2

Showing results (1-10 of 12) with videos related to

Sort By:
Pageof 2
Structure (London, England : 1993)|September 22, 2001
The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPaseS Padmanabhan, D M Freymann
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1993
Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homologH D Bernstein, D Zopf, D M Freymann, et al.
Nature|September 13, 1984
6 A-resolution X-ray structure of a variable surface glycoprotein from Trypanosoma bruceiD M Freymann, P Metcalf, M Turner, et al.
Nature Structural Biology|July 30, 1999
Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDPD M Freymann, R J Keenan, R M Stroud, et al.
Nature|January 23, 1997
Structure of the conserved GTPase domain of the signal recognition particleD M Freymann, R J Keenan, R M Stroud, et al.
Cell|August 8, 1998
Crystal structure of the signal sequence binding subunit of the signal recognition particleR J Keenan, D M Freymann, P Walter, et al.
Annual Review of Biochemistry|June 8, 2001
The signal recognition particleR J Keenan, D M Freymann, R M Stroud, et al.
Journal of Molecular Biology|March 25, 2000
The crystal structure of thymidylate synthase from Pneumocystis carinii reveals a fungal insert important for drug designA C Anderson, K M Perry, D M Freymann, et al.
Science (New York, N.Y.)|June 2, 2000
Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptorP Peluso, D Herschlag, S Nock, et al.
RNA (New York, N.Y.)|December 1, 1996
NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP)U Schmitz, D M Freymann, T L James, et al.
Pageof 2