Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag. (Q39685850)

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scientific article published on November 2002

Language	Label	Description	Also known as
English	Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag.	scientific article published on November 2002

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag. (English)

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Lawrence Kleiman

5

object named as

Lawrence Kleiman

0 references

6

object named as

Mark A Wainberg

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

author name string

Chen Liang

1

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Jing Hu

2

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Rodney S Russell

3

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Ariel Roldan

4

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

language of work or name

0 references

publication date

1 November 2002

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Europe PubMed Central

PMC publication ID

14 September 2017

number of pages

9

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based on heuristic

inferred from page(s)

Journal of Virology

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Europe PubMed Central

PMC publication ID

14 September 2017

76

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

22

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

11729-11737

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

Viral late domains

1 reference

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14 September 2017

Identification of a minimal HIV-1 gag domain sufficient for self-association

1 reference

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HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress

1 reference

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Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding

1 reference

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Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells

1 reference

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Hydrophobic amino acids in the human immunodeficiency virus type 1 p2 and nucleocapsid proteins can contribute to the rescue of deleted viral RNA packaging signals.

1 reference

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Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)

1 reference

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Mapping and characterization of the N-terminal I domain of human immunodeficiency virus type 1 Pr55(Gag).

1 reference

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Kinetic analysis of human immunodeficiency virus type 1 assembly reveals the presence of sequential intermediates

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Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain

1 reference

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Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA.

1 reference

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Roles of matrix, p2, and N-terminal myristoylation in human immunodeficiency virus type 1 Gag assembly

1 reference

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Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein

1 reference

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Formation of virus assembly intermediate complexes in the cytoplasm by wild-type and assembly-defective mutant human immunodeficiency virus type 1 and their association with membranes.

1 reference

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Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution

1 reference

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In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain.

1 reference

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Virus maturation by budding

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The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly.

1 reference

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Detection of a trimeric human immunodeficiency virus type 1 Gag intermediate is dependent on sequences in the matrix protein, p17.

1 reference

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Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites.

1 reference

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A putative alpha-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly

1 reference

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14 September 2017

Analysis of the assembly function of the human immunodeficiency virus type 1 gag protein nucleocapsid domain.

1 reference

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In Vitro Assembly Properties of Purified Bacterially Expressed Capsid Proteins of Human Immunodeficiency Virus

1 reference

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Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein

1 reference

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Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation

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A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system

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Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid

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Crystal structure of dimeric HIV-1 capsid protein

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Prediction of protein secondary structure at better than 70% accuracy

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Phenotypic characterization of insertion mutants of the human immunodeficiency virus type 1 Gag precursor expressed in recombinant baculovirus-infected cells

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Identification of human immunodeficiency virus type 1 Gag protein domains essential to membrane binding and particle assembly

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Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids

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Recent advances and remaining problems in HIV assembly.

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Identifiers

10.1128/JVI.76.22.11729-11737.2002

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 September 2017

ResearchGate publication ID

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