(Q47917290)

English

The phage lambda terminase enzyme: 1. Reconstitution of the holoenzyme from the individual subunits enhances the thermal stability of the small subunit

scientific article published in July 1998

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scholarly article

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

The phage lambda terminase enzyme: 1. Reconstitution of the holoenzyme from the individual subunits enhances the thermal stability of the small subunit (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

Carlos Enrique Catalano

4

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

author name string

Meyer JD

1

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

Hanagan A

2

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

Manning MC

3

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

publication date

1 July 1998

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

International Journal of Biological Macromolecules

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

23

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

1

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

27-36

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

Bacteriophage lambda DNA maturation and packaging

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Virus DNA packaging: the strategy used by phage lambda

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Bacteriophage lambda DNA: the beginning of the end

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Mechanism of cos DNA cleavage by bacteriophage lambda terminase: multiple roles of ATP

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Kinetic characterization of the ATPase activity of the DNA packaging enzyme from bacteriophage lambda

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The control of lambda DNA terminase synthesis

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The overproduction of DNA terminase of coliphage lambda

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Overproduction of Escherichia coli integration host factor, a protein with nonidentical subunits

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Cosmid DNA packaging in vivo

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Kinetic analysis of the endonuclease activity of phage lambda terminase: assembly of a catalytically competent nicking complex is rate-limiting.

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Measuring and increasing protein stability

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Calculation of protein extinction coefficients from amino acid sequence data

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Stability of proteins: small globular proteins

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Protein folding

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Kinetic and thermodynamic thermal stabilities of ribonuclease A and ribonuclease B.

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Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride.

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Molten Globules

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A native tertiary interaction stabilizes the A state of cytochrome c

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The molten globule state of alpha-lactalbumin.

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The phage lambda terminase enzyme: 2. Refolding of the gpNu1 subunit from the detergent-denatured and guanidinium hydrochloride-denatured state yields different oligomerization states and altered protein stabilities

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Assembly of a nucleoprotein complex required for DNA packaging by bacteriophage lambda.

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Interference with phage lambda development by the small subunit of the phage 21 terminase, gp1

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Coexpression of nuclear receptor partners increases their solubility and biological activities.

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Identifiers

10.1016/S0141-8130(98)00009-9

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/9644594

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