Polylysine binding to unphosphorylated smooth muscle myosin enhances formation and stabilizes myosin filaments in vitro.

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Polylysine binding to unphosphorylated smooth muscle myosin enhances formation and stabilizes myosin filaments in vitro.

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2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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Polylysine binding to unphosph ...... zes myosin filaments in vitro.

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Polylysine binding to unphosph ...... zes myosin filaments in vitro.

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Polylysine binding to unphosph ...... zes myosin filaments in vitro.

@en

Polylysine binding to unphosph ...... zes myosin filaments in vitro.

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Polylysine binding to unphosph ...... zes myosin filaments in vitro.

@en

Polylysine binding to unphosph ...... zes myosin filaments in vitro.

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P1476

Polylysine binding to unphosph ...... zes myosin filaments in vitro.

@en

P2093

Ferguson DG

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Paul RJ

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Szymanski PT

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P2860

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The binding of calmodulin to myelin basic protein and histone H2B.

A simple method of preparing actin-free myosin from smooth muscle.

Intranuclear injection of anti-actin antibodies into Xenopus oocytes blocks chromosome condensation.

The interaction of calmodulin and polylysine as studied by 1H NMR spectroscopy and sedimentation equilibrium centrifugation.

Effect of caldesmon on the assembly of smooth muscle myosin.

Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes

P304

337-346

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scholarly article

P356

10.1046/J.1365-201X.2002.00950.X

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P433

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P478

174

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P577

2002-04-01T00:00:00Z

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P698

11942921

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