Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes (Q24535752)

peptidylprolyl isomerase A

1 reference

Protein phosphatase 3 catalytic subunit alpha

1 reference

cyclosporin A binding

1 reference

7

Hengming Ke

0 references

author name string

Qing Huai

1

0 references

Hwa-Young Kim

2

0 references

Yudong Liu

3

0 references

Yingdong Zhao

4

0 references

Angelo Mondragon

5

0 references

Jun O Liu

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

6

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language of work or name

English

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publication date

17 September 2002

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published in

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volume

99

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page(s)

12037-42

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issue

19

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cites work

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X-ray structure of a decameric cyclophilin-cyclosporin crystal complex

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The latch region of calcineurin B is involved in both immunosuppressant-immunophilin complex docking and phosphatase activation

21 January 2018

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Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activity

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Cyclosporine and its analogue SDZ IMM 125 mediate very similar effects on T-cell activation--a comparative analysis in vitro

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PubMed

https://pubmed.ncbi.nlm.nih.gov/12218175

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Immunosuppressive activity of [MeBm2t]1-, D-diaminobutyryl-8-, and D-diaminopropyl-8-cyclosporin analogues correlates with inhibition of calcineurin phosphatase activity

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12218175

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.192206699

1 reference

2294929

ADS bibcode

2002PNAS...9912037H

0 references

2294929

1 reference

1 reference

1 reference