(Q44870020)

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Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA I. Cryoelectron microscopic studies

scientific article published on October 20, 1991

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scholarly article

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Europe PubMed Central

7 December 2017

Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA I. Cryoelectron microscopic studies (English)

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10.1016/0022-2836(91)90923-T

https://api.crossref.org/works/10.1016/0022-2836(91)90923-T

7 November 2022

Structure and assembly of the Escherichia coli transcription termination factor rho and its interaction with RNA. I. Cryoelectron microscopic studies (English)

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1719215

7 November 2022

Escherichia coli

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structural biology

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10.1016/0022-2836(91)90923-T

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7 November 2022

Steven Seifried

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S. E. Seifried

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7 November 2022

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von Hippel PH

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7 December 2017

E. P. Gogol

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7 November 2022

P. H. von Hippel

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0000-0003-2512-8097

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Europe PubMed Central

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publication date

1 October 1991

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20 October 1991

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7 November 2022

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https://api.elsevier.com/content/article/PII:002228369190923T?httpAccept=text/xml

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10.1016/0022-2836(91)90923-T

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7 November 2022

https://api.elsevier.com/content/article/PII:002228369190923T?httpAccept=text/plain

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10.1016/0022-2836(91)90923-T

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7 November 2022

Journal of Molecular Biology

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7 December 2017

221

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7 December 2017

1127-1138

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7 December 2017

4

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7 December 2017

The E. coli Rho protein: an ATPase that terminates transcription

1

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7 November 2022

Escherichia coli transcription termination factor rho has a two-domain structure in its activated form

2

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10.1016/0022-2836(91)90923-T

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7 November 2022

Interactions of Escherichia coli transcription termination factor rho with RNA. II. Electron microscopy and nuclease protection experiments

3

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10.1016/0022-2836(91)90923-T

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7 November 2022

Cryo-electron microscopy of vitrified specimens

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10.1016/0022-2836(91)90923-T

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7 November 2022

Stabilization of the hexameric form of Escherichia coli protein rho under ATP hydrolysis conditions.

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10.1016/0022-2836(91)90923-T

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7 November 2022

Computer averaging of electron micrographs of 40S ribosomal subunits

8

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10.1016/0022-2836(91)90923-T

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7 November 2022

The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens

12

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10.1016/0022-2836(91)90923-T

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7 November 2022

Molecular architecture of Escherichia coli F1 adenosinetriphosphatase

13

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10.1016/0022-2836(91)90923-T

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7 November 2022

Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex

14

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10.1016/0022-2836(91)90923-T

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7 November 2022

Structure and Function of the Genome of Coliphage T5. Transcription in vitro of the "Nicked" and "Nick-Free" T5+ DNA

16

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10.1016/0022-2836(91)90923-T

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7 November 2022

Interactions of Escherichia coli transcription termination factor rho with RNA. I. Binding stoichiometries and free energies.

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10.1016/0022-2836(91)90923-T

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7 November 2022

RNA sequence and secondary structure requirements for rho-dependent transcription termination

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10.1016/0022-2836(91)90923-T

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7 November 2022

Observations on the structure of the termination factor rho and its attachment to DNA

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10.1016/0022-2836(91)90923-T

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7 November 2022

Transcription termination and the regulation of gene expression

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10.1016/0022-2836(91)90923-T

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7 November 2022

Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA. II. Physical chemical studies.

27

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10.1016/0022-2836(91)90923-T

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7 November 2022

Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli

29

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10.1016/0022-2836(91)90923-T

https://api.crossref.org/works/10.1016/0022-2836(91)90923-T

7 November 2022

Tandem termination sites in the tryptophan operon of Escherichia coli

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10.1016/0022-2836(91)90923-T

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7 November 2022

Identifiers

10.1016/0022-2836(91)90923-T

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Europe PubMed Central

7 December 2017

1 reference

Europe PubMed Central

7 December 2017

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