Isozyme-specific comprehensive characterization of transglutaminase-crosslinked substrates in kidney fibrosis.

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Isozyme-specific comprehensive characterization of transglutaminase-crosslinked substrates in kidney fibrosis.

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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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Isozyme-specific comprehensive ...... substrates in kidney fibrosis.

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Isozyme-specific comprehensive ...... substrates in kidney fibrosis.

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Isozyme-specific comprehensive ...... substrates in kidney fibrosis.

@en

Isozyme-specific comprehensive ...... substrates in kidney fibrosis.

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Isozyme-specific comprehensive ...... substrates in kidney fibrosis.

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Isozyme-specific comprehensive ...... substrates in kidney fibrosis.

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P1476

Isozyme-specific comprehensive ...... substrates in kidney fibrosis.

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P2093

Hideki Tatsukawa

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Kiyotaka Hitomi

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Risa Otsu

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Ryosuke Wakita

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Yuji Tani

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P2860

Transglutaminase 2 has opposing roles in the regulation of cellular functions as well as cell growth and death

Transglutaminase 2: an enigmatic enzyme with diverse functions

Legumain/asparaginyl endopeptidase controls extracellular matrix remodeling through the degradation of fibronectin in mouse renal proximal tubular cells

Evidence that fibroblasts derive from epithelium during tissue fibrosis

Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: identification of peptide substrates for TGASE 2 and Factor XIIIA.

Identification of preferred substrate sequences for transglutaminase 1--development of a novel peptide that can efficiently detect cross-linking enzyme activity in the skin.

Transglutaminase regulation of cell function.

Molecular basis of renal fibrosis.

Phosphorylation of transglutaminase 2 (TG2) at serine-216 has a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of PTEN

Role of moesin in renal fibrosis.

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7306

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scholarly article

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10.1038/S41598-018-25674-4

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English

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P478

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2018-05-09T00:00:00Z

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29743665

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5943318

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