Ouabagenin is a naturally occurring LXR ligand without causing hepatic steatosis as a side effect.

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Ouabagenin is a naturally occurring LXR ligand without causing hepatic steatosis as a side effect.

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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年學術文章

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2018年學術文章

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2018年學術文章

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Ouabagenin is a naturally occu ...... ic steatosis as a side effect.

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Ouabagenin is a naturally occu ...... ic steatosis as a side effect.

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Item

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Ouabagenin is a naturally occu ...... ic steatosis as a side effect.

@en

Ouabagenin is a naturally occu ...... ic steatosis as a side effect.

@nl

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Ouabagenin is a naturally occu ...... ic steatosis as a side effect.

@en

Ouabagenin is a naturally occu ...... ic steatosis as a side effect.

@nl

P1476

Ouabagenin is a naturally occu ...... ic steatosis as a side effect.

@en

P2093

Kohji Fukunaga

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

Maiko Okada

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

Norifumi Shioda

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

Satoru Tamura

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

Shigeaki Kato

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P2860

Role of LXRs in control of lipogenesis

Activation of the nuclear receptor LXR by oxysterols defines a new hormone response pathway

Identification of liver X receptor-retinoid X receptor as an activator of the sterol regulatory element-binding protein 1c gene promoter

Structural requirements of ligands for the oxysterol liver X receptors LXRalpha and LXRbeta

Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRalpha and LXRbeta

Hepatic cholesterol metabolism and resistance to dietary cholesterol in LXRbeta-deficient mice

Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPARgamma

Blood pressure and amiloride-sensitive sodium channels in vascular and renal cells

Oxysterols and EBI2 promote osteoclast precursor migration to bone surfaces and regulate bone mass homeostasis

The three-dimensional structure of the liver X receptor beta reveals a flexible ligand-binding pocket that can accommodate fundamentally different ligands

P2888

s41598-018-20663-z

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scholarly article

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10.1038/S41598-018-20663-Z

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P407

English

P433

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P478

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

P50

Kumiko Ui-Tei

Minoru Ueda

Yasuharu Shinoda

P577

2018-02-02T00:00:00Z

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P6179

1100699249

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29396543

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P932

5797171

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