(Q33987871)

English

A single amino acid of human immunodeficiency virus type 2 capsid protein affects conformation of two external loops and viral sensitivity to TRIM5α.

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

A single amino acid of human immunodeficiency virus type 2 capsid protein affects conformation of two external loops and viral sensitivity to TRIM5α. (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

author name string

Tadashi Miyamoto

1

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Masaru Yokoyama

2

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Ken Kono

3

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Tatsuo Shioda

4

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Hironori Sato

5

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Emi E Nakayama

6

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Europe PubMed Central

PubMed publication ID

30 July 2017

language of work or name

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publication date

28 July 2011

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

6

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

7

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

e22779

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

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Creative Commons Attribution 4.0 International

28 July 2011

1 reference

April 2022 Public Data File from Crossref

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Multiple sites in the N-terminal half of simian immunodeficiency virus capsid protein contribute to evasion from rhesus monkey TRIM5α-mediated restriction

1 reference

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Contribution of RING domain to retrovirus restriction by TRIM5alpha depends on combination of host and virus

1 reference

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Active site remodeling switches HIV specificity of antiretroviral TRIMCyp

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Proteasomal degradation of TRIM5alpha during retrovirus restriction

1 reference

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1 reference

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Proteasome inhibitors uncouple rhesus TRIM5alpha restriction of HIV-1 reverse transcription and infection

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Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor

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Fitness cost of escape mutations in p24 Gag in association with control of human immunodeficiency virus type 1

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Differential restriction of human immunodeficiency virus type 2 and simian immunodeficiency virus SIVmac by TRIM5alpha alleles

1 reference

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5 July 2018

Human tripartite motif 5alpha domains responsible for retrovirus restriction activity and specificity

1 reference

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A specific region of 37 amino acid residues in the SPRY (B30.2) domain of African green monkey TRIM5alpha determines species-specific restriction of simian immunodeficiency virus SIVmac infection

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TRIM5alpha selectively binds a restriction-sensitive retroviral capsid

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Species-specific variation in the B30.2(SPRY) domain of TRIM5alpha determines the potency of human immunodeficiency virus restriction

1 reference

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Positive selection of primate TRIM5alpha identifies a critical species-specific retroviral restriction domain

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5 July 2018

A single amino acid change in the SPRY domain of human Trim5alpha leads to HIV-1 restriction

1 reference

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Retrovirus resistance factors Ref1 and Lv1 are species-specific variants of TRIM5alpha

1 reference

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The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys

1 reference

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Protein structure prediction and structural genomics

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Impact of a single amino acid in the variable region 2 of the Old World monkey TRIM5alpha SPRY (B30.2) domain on anti-human immunodeficiency virus type 2 activity.

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Identifiers

10.1371/JOURNAL.PONE.0022779

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

2011PLoSO...622779M

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

ResearchGate publication ID

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