Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment (Q23924139)

HELD

1 reference

25 September 2023

1 reference

19 July 2017

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1 reference

29 March 2020

10

A. A. Shvedova

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Valerian E. Kagan

12

V. E. Kagan

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Bengt Fadeel

11

B. Fadeel

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Yulia Y. Tyurina

1

Y. Y. Tyurina

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Hülya Bayır

7

H. Bayir

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author name string

L. V. Basova

2

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N. V. Konduru

3

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V. A. Tyurin

4

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A. I. Potapovich

5

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P. Cai

6

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D. Stoyanovsky

8

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B. R. Pitt

Journal of Biological Chemistry

9

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language of work or name

English

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publication date

16 March 2007

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published in

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volume

282

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issue

11

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page(s)

8498-8509

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performing organization

University of Pittsburgh

University of Pittsburgh at Pittsburgh

1 reference

NIOSHTIC-2

on focus list of Wikimedia project

2 February 2024

Wikimedia–NIOSH collaboration

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1 reference

25 September 2023

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Corpse clearance defines the meaning of cell death

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The role of regulated CFTR trafficking in epithelial secretion

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Programmed cell clearance

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Proteins involved in lipid translocation in eukaryotic cells.

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Identification and purification of aminophospholipid flippases

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Lipid antioxidant, etoposide, inhibits phosphatidylserine externalization and macrophage clearance of apoptotic cells by preventing phosphatidylserine oxidation

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Fas-triggered phosphatidylserine exposure is modulated by intracellular ATP.

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Phosphatidylserine exposure in Fas type I cells is mitochondria-dependent

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Thiol oxidation enforces phosphatidylserine externalization in apoptosis-sensitive and -resistant cells through a deltapsim/cytochrome C release-dependent mechanism

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Prolonged storage of red blood cells affects aminophospholipid translocase activity.

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Antigen recognition induces phosphatidylserine exposure on the cell surface of human CD8+ T cells

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S-nitrosylation regulates apoptosis.

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Nitric oxide production is regulated by fever-range thermal stimulation of murine macrophages.

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Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69.

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