S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.

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S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.

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S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.

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S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.

@en

S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.

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S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.

@en

S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.

@nl

P1476

S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain

@en

P2093

Lee-Wei Yang

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

Md Imran Khan

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

Yu-Kai Su

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

P2860

S100A13. Biochemical characterization and subcellular localization in different cell lines

Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins

Ca2+ -dependent interaction of S100A1 with the sarcoplasmic reticulum Ca2+ -ATPase2a and phospholamban in the human heart

A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form

Structural insights into the oligomerization mode of the human receptor for advanced glycation end-products

S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains

Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E

Crystal structure of a T cell receptor Valpha11 (AV11S5) domain: new canonical forms for the first and second complementarity determining regions

The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process

The structure of S100A12 in a hexameric form and its proposed role in receptor signalling

P304

e0190545

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P31

scholarly article

P356

10.1371/JOURNAL.PONE.0190545

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

P407

English

P433

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

P478

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

P50

Jinhao Zou

Ruey-Hwang Chou

Chin Yu

P577

2018-02-14T00:00:00Z

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

P698

29444082

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P932

5812564

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