The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly (Q41633915)

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scientific article published on November 1996

Language	Label	Description	Also known as
English	The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly	scientific article published on November 1996

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scholarly article

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Europe PubMed Central

5 October 2017

The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly (English)

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Europe PubMed Central

5 October 2017

author name string

Trus BL

1

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Europe PubMed Central

5 October 2017

Booy FP

2

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Europe PubMed Central

5 October 2017

Newcomb WW

3

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Europe PubMed Central

5 October 2017

Brown JC

4

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Europe PubMed Central

5 October 2017

Homa FL

5

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Europe PubMed Central

5 October 2017

Thomsen DR

6

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Europe PubMed Central

5 October 2017

Steven AC

7

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Europe PubMed Central

5 October 2017

language of work or name

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publication date

1 November 1996

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Europe PubMed Central

5 October 2017

number of pages

16

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inferred from page(s)

Journal of Molecular Biology

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Europe PubMed Central

5 October 2017

263

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447-462

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Europe PubMed Central

5 October 2017

3

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Europe PubMed Central

5 October 2017

A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy

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The capsid of small papova viruses contains 72 pentameric capsomeres: direct evidence from cryo-electron-microscopy of simian virus 40.

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The transformation of τ-particles into T4 heads. I. Evidence for the conservative mode of this transformation

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DNA packaging in dsDNA bacteriophages

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Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus

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The effects of radiation damage on the structure of frozen hydrated HSV-1 capsids

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Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system

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Visualization of three-dimensional density maps reconstructed from cryoelectron micrographs of viral capsids

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Identification of structural proteins of channel catfish virus by mass spectrometry

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Identification of genes encoding two capsid proteins (VP24 and VP26) of herpes simplex virus type 1.

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Structural transitions during maturation of bacteriophage lambda capsids

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Cryo-electron microscopy of vitrified specimens

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The T=4 envelope of Sindbis virus is organized by interactions with a complementary T=3 capsid

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Form determination of the heads of bacteriophages

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X-ray diffraction study of tail-tubes from bacteriophage T2L

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Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes

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Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation

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Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a

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The product of the UL6 gene of herpes simplex virus type 1 is associated with virus capsids

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Biochemical studies of the maturation of herpesvirus nucleocapsid species

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Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus.

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Processing of the herpes simplex virus assembly protein ICP35 near its carboxy terminal end requires the product of the whole of the UL26 reading frame

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The herpes simplex virus gene UL26 proteinase in the presence of the UL26.5 gene product promotes the formation of scaffold-like structures

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The products of herpes simplex virus type 1 gene UL26 which are involved in DNA packaging are strongly associated with empty but not with full capsids

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The correlation averaging of a regularly arranged bacterial cell envelope protein

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Three-dimensional structure of the HSV1 nucleocapsid

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Characterization of intranuclear capsids made by ts morphogenic mutants of HSV-1.

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Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses

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Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins

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Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy

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Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids

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Mutations in herpes simplex virus type 1 genes encoding VP5 and VP23 abrogate capsid formation and cleavage of replicated DNA.

1 reference

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7 January 2021

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Identification and Characterization of a Herpes Simplex Virus Gene Product Required for Encapsidation of Virus DNA

1 reference

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Hexavalent capsomers of herpes simplex virus type 2: symmetry, shape, dimensions, and oligomeric status

1 reference

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based on heuristic

inferred from DOI database lookup

Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of VP26.

1 reference

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inferred from DOI database lookup

Herpesvirus proteinase: site-directed mutagenesis used to study maturational, release, and inactivation cleavage sites of precursor and to identify a possible catalytic site serine and histidine.

1 reference

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7 January 2021

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Identifiers

10.1016/S0022-2836(96)80018-0

1 reference

Europe PubMed Central

5 October 2017

1 reference

Europe PubMed Central

5 October 2017

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