¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

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¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

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2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

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¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

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¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

@en

¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

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¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

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¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

@nl

P1476

¹H, ¹³C and ¹⁵N resonance assignments of Ca²⁺-bound human S100A15.

@en

P2093

Chin Yu

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

Ching-Chang Cho

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

Kuo-Wei Hung

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P2860

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

Intracellular and extracellular roles of S100 proteins

Novel S100A7 (psoriasin)/S100A15 (koebnerisin) subfamily: highly homologous but distinct in regulation and function

P2888

s12104-013-9476-4

P304

169-171

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P31

scholarly article

P356

10.1007/S12104-013-9476-4

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P433

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

P478

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

P577

2013-06-29T00:00:00Z

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P698

23813220

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