Discovery of Highly Selective Inhibitors of the Immunoproteasome Low Molecular Mass Polypeptide 2 (LMP2) Subunit.

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Immunoproteasome functions explained by divergence in cleavage specificity and regulation.Binding of the Microbial Cyclic Tetrapeptide Trapoxin A to the Class I Histone Deacetylase HDAC8.

P2860

Q46132051-F7DBFFEB-9F28-492A-B57D-C5A38BC1694B Q47897379-D73C9AA8-BF54-4B55-AD0C-80EFD23A30E6

P2860

Discovery of Highly Selective Inhibitors of the Immunoproteasome Low Molecular Mass Polypeptide 2 (LMP2) Subunit.

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http://www.wikidata.org/entity/Q36354644

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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name

Discovery of Highly Selective ...... Polypeptide 2 (LMP2) Subunit.

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Discovery of Highly Selective ...... Polypeptide 2 (LMP2) Subunit.

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Discovery of Highly Selective ...... Polypeptide 2 (LMP2) Subunit.

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Discovery of Highly Selective ...... Polypeptide 2 (LMP2) Subunit.

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Discovery of Highly Selective ...... Polypeptide 2 (LMP2) Subunit.

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Discovery of Highly Selective ...... Polypeptide 2 (LMP2) Subunit.

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P1476

Discovery of Highly Selective ...... Polypeptide 2 (LMP2) Subunit.

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P2093

Christopher Kirk

http://www.w3.org/2001/XMLSchema#string

David C Moebius

http://www.w3.org/2001/XMLSchema#string

Dustin McMinn

http://www.w3.org/2001/XMLSchema#string

Eric Lowe

http://www.w3.org/2001/XMLSchema#string

Erin K Bradley

http://www.w3.org/2001/XMLSchema#string

Henry W B Johnson

http://www.w3.org/2001/XMLSchema#string

Janet L Anderl

http://www.w3.org/2001/XMLSchema#string

Jeffrey Jones

http://www.w3.org/2001/XMLSchema#string

John Bui

http://www.w3.org/2001/XMLSchema#string

Lisa M Kelly

http://www.w3.org/2001/XMLSchema#string

P2860

Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S β5-subunit

Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity

Structure-based design of β1i or β5i specific inhibitors of human immunoproteasomes

Crystal structure of the human 20S proteasome in complex with carfilzomib

The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design

Unexpected role for the immunoproteasome subunit LMP2 in antiviral humoral and innate immune responses.

Interferon-gamma inducible exchanges of 20S proteasome active site subunits: why?

Design and synthesis of an orally bioavailable and selective peptide epoxyketone proteasome inhibitor (PR-047).

A selective inhibitor of the immunoproteasome subunit LMP2 induces apoptosis in PC-3 cells and suppresses tumour growth in nude mice.

Beneficial effect of novel proteasome inhibitors in murine lupus via dual inhibition of type I interferon and autoantibody-secreting cells.

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413-417

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scholarly article

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10.1021/ACSMEDCHEMLETT.6B00496

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28435528

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5392757

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Discovery of Highly Selective Inhibitors of the Immunoproteasome Low Molecular Mass Polypeptide 2 (LMP2) Subunit.

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P2860

P2860

Discovery of Highly Selective Inhibitors of the Immunoproteasome Low Molecular Mass Polypeptide 2 (LMP2) Subunit.

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