(Q45722413)

15 December 2017

title

Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics (English)

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15 December 2017

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7

Wah Chiu

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15 December 2017

Matthew L Baker

1

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15 December 2017

Wen Jiang

2

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15 December 2017

Brian R Bowman

3

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15 December 2017

Z Hong Zhou

4

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15 December 2017

Florante A Quiocho

5

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15 December 2017

Frazer J Rixon

6

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15 December 2017

language of work or name

English

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publication date

1 August 2003

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Journal of Molecular Biology

15 December 2017

published in

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15 December 2017

volume

331

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15 December 2017

issue

2

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15 December 2017

page(s)

447-456

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

15 December 2017

cites work

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https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900696-X

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

7 January 2021

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The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid.

7 January 2021

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Seeing the herpesvirus capsid at 8.5 A

7 January 2021

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Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus

7 January 2021

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Bridging the information gap: computational tools for intermediate resolution structure interpretation

7 January 2021

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The PSIPRED protein structure prediction server

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900696-X

Seventy-five percent accuracy in protein secondary structure prediction

7 January 2021

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Exploiting the past and the future in protein secondary structure prediction

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900696-X

Structure of the herpesvirus major capsid protein

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900696-X

Diversity of functions of proteins with internal symmetry in spatial arrangement of secondary structural elements

7 January 2021

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Comparison of spatial arrangements of secondary structural elements in proteins.

7 January 2021

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Three-dimensional structure of annexins

7 January 2021

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7 January 2021

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https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900696-X

Handedness of the herpes simplex virus capsid and procapsid

7 January 2021

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The PROSITE database, its status in 1997.

7 January 2021

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

7 January 2021

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Enhanced genome annotation using structural profiles in the program 3D-PSSM

7 January 2021

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Second site mutations in the N-terminus of the major capsid protein (VP5) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1.

7 January 2021

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Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging

7 January 2021

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Structure of the herpes simplex virus capsid: peptide A862-H880 of the major capsid protein is displayed on the rim of the capsomer protrusions

7 January 2021

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Crystal structure of the annexin XII hexamer and implications for bilayer insertion

7 January 2021

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Finding and using local symmetry in identifying lower domain movements in hexon subunits of the herpes simplex virus type 1 B capsid

7 January 2021

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Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus.

7 January 2021

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Hexon-only binding of VP26 reflects differences between the hexon and penton conformations of VP5, the major capsid protein of herpes simplex virus

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900696-X

inferred from DOI database lookup

7 January 2021

based on heuristic

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

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900696-X

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0022-2836(03)00696-X

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15 December 2017

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