A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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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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A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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P1476

A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K.

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P2093

Haruo Homareda

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Makoto Ushimaru

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Masahiro Otsu

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Sachiko Yamamoto

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Sayaka Ito

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Taeho Jo

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Toshiyuki Fukutomi

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Yoshinobu Eishi

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Yukichi Hara

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P2860

Transport and pharmacological properties of nine different human Na, K-ATPase isozymes

Homology modeling of the cation binding sites of Na+K+-ATPase.

Crystal structure of the sodium-potassium pump at 2.4 A resolution

Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain

Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo

Importance of conserved Thr214 in domain A of the Na+,K+ -ATPase for stabilization of the phosphoryl transition state complex in E2P dephosphorylation

Na+, K+-ATPase isozyme diversity; comparative biochemistry and physiological implications of novel functional interactions.

A eukaryotic (insect) tricistronic mRNA encodes three proteins selected by context-dependent scanning.

The functional role of beta subunits in oligomeric P-type ATPases.

Isoform-specific interactions of Na,K-ATPase subunits are mediated via extracellular domains and carbohydrates

P2888

s10863-017-9729-5

P304

463-472

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P31

scholarly article

P356

10.1007/S10863-017-9729-5

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P433

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

P478

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P577

2017-10-19T00:00:00Z

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P698

29047027

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