Proteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV-1 and HIV-2 (Q24643016)

8

object named as

H G Krausslich

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author name string

U Schubert

1

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D E Ott

2

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E N Chertova

3

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R Welker

4

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U Tessmer

5

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M F Princiotta

6

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J R Bennink

7

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J W Yewdell

Proceedings of the National Academy of Sciences of the United States of America

9

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language of work or name

English

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publication date

21 November 2000

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published in

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volume

97

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issue

24

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page(s)

13057-62

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cites work

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Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus

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CD4 Glycoprotein Degradation Induced by Human Immunodeficiency Virus Type 1 Vpu Protein Requires the Function of Proteasomes and the Ubiquitin-Conjugating Pathway

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7 January 2021

inferred from DOI database lookup

A novel gene of HIV-1, vpu, and its 16-kilodalton product

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Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines

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PubMed

https://pubmed.ncbi.nlm.nih.gov/11087859

12 December 2020

inferred from PubMed ID database lookup

Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/11087859

12 December 2020

inferred from PubMed ID database lookup

Rapid Deubiquitination of Nucleosomal Histones in Human Tumor Cells Caused by Proteasome Inhibitors and Stress Response Inducers: Effects on Replication, Transcription, Translation, and the Cellular Stress Response

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PubMed

https://pubmed.ncbi.nlm.nih.gov/11087859

12 December 2020

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Identifiers

DOI

10.1073/PNAS.97.24.13057

1 reference

ADS bibcode

2000PNAS...9713057S

0 references

1 reference

1 reference

PubMed publication ID

11087859

1 reference