Structure-activity relationships of retinoids as inhibitors of calmodulin-dependent human erythrocyte Ca(2+)-ATPase activity and calmodulin binding to membranes.

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Vitamin neurotoxicity Stereochemical requirements for the modulation by retinoic acid of thyroid hormone activation of Ca(2+)-ATPase and binding at the human erythrocyte membrane

P2860

Q28186901-0B47133E-F51B-457D-B0C8-EB874AAD507F Q42797669-68F99E6A-105C-4A4D-928B-36D4F55D493D

P2860

Structure-activity relationships of retinoids as inhibitors of calmodulin-dependent human erythrocyte Ca(2+)-ATPase activity and calmodulin binding to membranes.

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http://www.wikidata.org/entity/Q42862138

description

1991 nî lūn-bûn

@nan

1991年の論文

@ja

1991年論文

@yue

1991年論文

@zh-hant

1991年論文

@zh-hk

1991年論文

@zh-mo

1991年論文

@zh-tw

1991年论文

@wuu

1991年论文

@zh

1991年论文

@zh-cn

name

Structure-activity relationshi ...... dependent human erythrocyte Ca

@nl

Structure-activity relationshi ...... lmodulin binding to membranes.

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type

Item

label

Structure-activity relationshi ...... dependent human erythrocyte Ca

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Structure-activity relationshi ...... lmodulin binding to membranes.

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prefLabel

Structure-activity relationshi ...... dependent human erythrocyte Ca

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Structure-activity relationshi ...... lmodulin binding to membranes.

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P1476

Structure-activity relationshi ...... lmodulin binding to membranes.

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P2093

Blas SD

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Davis FB

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Davis PJ

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Smith TJ

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P2860

Protein measurement with the Folin phenol reagent

An improved assay for nanomole amounts of inorganic phosphate

Retinoic acid inhibits calmodulin binding to human erythrocyte membranes and reduces membrane Ca2(+)-adenosine triphosphatase activity.

Role of calmodulin in thyroid hormone stimulation in vitro of human erythrocyte Ca2+-ATPase activity

Interaction of drugs with calmodulin. Biochemical, pharmacological and clinical implications.

Selective inhibitors of Ca2+-binding modulator of phosphodiesterase produce vascular relaxation and inhibit actin-myosin interaction.

A fluorescent calmodulin that reports the binding of hydrophobic inhibitory ligands.

Action of long-chain fatty acids in vitro on Ca2+-stimulatable, Mg2+-dependent ATPase activity in human red cell membranes.

Comparative effects of calmodulin inhibitors on calmodulin's hydrophobic sites and on the activation of cyclic nucleotide phosphodiesterase by calmodulin.

Retinoic acid is a modulator of thyroid hormone activation of Ca2+-ATPase in the human erythrocyte membrane.

P304

603-606

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scholarly article

P356

10.1042/BJ2770603

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P407

English

P478

277 ( Pt 3)

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P577

1991-08-01T00:00:00Z

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P5875

21325332

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P698

1831350

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P932

1151283

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Structure-activity relationships of retinoids as inhibitors of calmodulin-dependent human erythrocyte Ca(2+)-ATPase activity and calmodulin binding to membranes.

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P2860

P2860

Structure-activity relationships of retinoids as inhibitors of calmodulin-dependent human erythrocyte Ca(2+)-ATPase activity and calmodulin binding to membranes.

description

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P5875

P698

P932