Growth differentiation factor 15 in patients with congenital dyserythropoietic anaemia (CDA) type II (Q83811886)

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28 January 2020

title

Growth differentiation factor 15 in patients with congenital dyserythropoietic anaemia (CDA) type II (English)

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28 January 2020

1

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Martina U Muckenthaler

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object named as

Martina U Muckenthaler

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28 January 2020

author name string

Dorine W Swinkels

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28 January 2020

Sandro Altamura

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28 January 2020

Klaus Schwarz

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28 January 2020

Coby M Laarakkers

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28 January 2020

Hans-Juergen Gross

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28 January 2020

Markus Wiesneth

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Hermann Heimpel

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publication date

8 April 2011

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Journal of Molecular Medicine

28 January 2020

published in

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volume

89

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28 January 2020

page(s)

811-816

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28 January 2020

issue

8

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https://scigraph.springernature.com/pub.10.1007/s00109-011-0751-5

28 January 2020

exact match

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cites work

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Congenital dyserythropoietic anemia type II: epidemiology, clinical appearance, and prognosis based on long-term observation

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Hepcidin is decreased in TFR2 hemochromatosis

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Congenital dyserythropoietic anemia type II: molecular basis and clinical aspects

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Soluble transferrin receptor-1 levels in mice do not affect iron absorption

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Elevated growth differentiation factor 15 expression in patients with congenital dyserythropoietic anemia type I.

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Regulation of iron metabolism through GDF15 and hepcidin in pyruvate kinase deficiency

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Regulation of growth differentiation factor 15 expression by intracellular iron.

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Congenital dyserythropoietic anemia type I is caused by mutations in codanin-1

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Regulation of hepcidin: insights from biochemical analyses on human serum samples

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High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin

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12 December 2020

Mutations affecting the secretory COPII coat component SEC23B cause congenital dyserythropoietic anemia type II.

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12 December 2020

Congenital dyserythropoietic anemia type I (CDA I): molecular genetics, clinical appearance, and prognosis based on long-term observation.

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12 December 2020

Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization

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