The recombinational enhancer for DNA inversion functions independent of its orientation as a consequence of dyad symmetry in the Fis-DNA complex

Nucleic Acids Research ◽

10.1093/nar/17.15.6043 ◽

1989 ◽

Vol 17 (15) ◽

pp. 6043-6054 ◽

Author(s):

Ronald Kanaar ◽

Jochem P. van Hal ◽

Pieter van de Putte

Keyword(s):

Dna Inversion ◽

Dyad Symmetry ◽

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883: The Anticancer Activity of Mycobacterial Cell Wall-DNA Complex (MCC) Against Human Bladder Cancer Cell Lines is Different to BCG

The Journal of Urology ◽

10.1016/s0022-5347(18)31111-x ◽

2007 ◽

Vol 177 (4S) ◽

pp. 294-294

Author(s):

Nigel C. Phillips ◽

Sonia Ménard ◽

David S. Surprenant ◽

Danbing Ke ◽

Mario C. Filion

Keyword(s):

Bladder Cancer ◽

Cell Wall ◽

Anticancer Activity ◽

Cancer Cell ◽

Human Bladder Cancer ◽

Human Bladder ◽

Human Bladder Cancer Cell ◽

Mycobacterial Cell Wall ◽

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714: Inhibition of Bladder Cancer Cell Proliferation by Mycobacterial Cell Wall-DNA Complex (MCC) in Combination with Chemotherapeutic Agents

The Journal of Urology ◽

10.1016/s0022-5347(18)37963-1 ◽

2004 ◽

Vol 171 (4S) ◽

pp. 190-190

Author(s):

Myriam Labelle ◽

Mario C. Filion ◽

Nigel C. Phillips

Keyword(s):

Cell Proliferation ◽

Bladder Cancer ◽

Cell Wall ◽

Cancer Cell ◽

Chemotherapeutic Agents ◽

Bladder Cancer Cell ◽

Cancer Cell Proliferation ◽

Mycobacterial Cell ◽

Mycobacterial Cell Wall ◽

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Faculty Opinions recommendation of Structural basis of transcription activation: the CAP-alpha CTD-DNA complex.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1009129.122661 ◽

2002 ◽

Author(s):

Richard Gourse

Keyword(s):

Transcription Activation ◽

Structural Basis ◽

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Faculty Opinions recommendation of Structural basis of transcription activation: the CAP-alpha CTD-DNA complex.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1009129.119157 ◽

2002 ◽

Author(s):

Stephen Busby

Keyword(s):

Transcription Activation ◽

Structural Basis ◽

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Faculty Opinions recommendation of Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.717964305.793465848 ◽

2012 ◽

Author(s):

Gottfried Otting

Keyword(s):

Nmr Spectroscopy ◽

Full Length ◽

Domain Interactions ◽

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Faculty Opinions recommendation of Structure of an 'open' clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transport.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.718083460.793485958 ◽

2013 ◽

Author(s):

Anthony Maxwell

Keyword(s):

Type Ii ◽

Dna Capture ◽

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Faculty Opinions recommendation of Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.8827956.9362054 ◽

2011 ◽

Author(s):

Yamini Dalal

Keyword(s):

Dna Methylation ◽

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Cleavage of phi X174 single-stranded DNA by gene A protein and formation of a tight protein-DNA complex.

Journal of Virology ◽

10.1128/jvi.35.2.409-413.1980 ◽

1980 ◽

Vol 35 (2) ◽

pp. 409-413 ◽

Author(s):

S Eisenberg

Keyword(s):

Single Stranded Dna ◽

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Identification of a domain of the herpes simplex virus trans-activator Vmw65 required for protein-DNA complex formation through the use of protein A fusion proteins.

Journal of Virology ◽

10.1128/jvi.63.12.5509-5513.1989 ◽

1989 ◽

Vol 63 (12) ◽

pp. 5509-5513 ◽

Author(s):

G Werstuck ◽

J P Capone

Keyword(s):

Herpes Simplex Virus ◽

Herpes Simplex ◽

Complex Formation ◽

Fusion Proteins ◽

Protein A ◽

Simplex Virus ◽

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The Solution Structure of the Human ETS1-DNA Complex Reveals a Novel Mode of Binding and True Side Chain Intercalation

Cell ◽

10.1016/s0092-8674(00)81354-9 ◽

1996 ◽

Vol 87 (2) ◽

pp. 358 ◽

Author(s):

Milton H Werner ◽

G.Marius Clore ◽

Constance L Fisher ◽

Robert J Fisher ◽

Loc Trinh ◽

...

Keyword(s):

Solution Structure ◽

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