Arg452 substitution of the erythroid-specific 5-aminolaevulinate synthase, a hot spot mutation in X-linked sideroblastic anaemia, does not itself affect enzyme activity.
about
X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2).Clinical and genetic characteristics of congenital sideroblastic anemia: comparison with myelodysplastic syndrome with ring sideroblast (MDS-RS).Sideroblastic anemia: functional study of two novel missense mutations in ALAS2Detection and characterization of a thermophilic biotin biosynthetic enzyme, 7-keto-8-aminopelargonic acid synthase, from various thermophiles.
P2860
Arg452 substitution of the erythroid-specific 5-aminolaevulinate synthase, a hot spot mutation in X-linked sideroblastic anaemia, does not itself affect enzyme activity.
description
2006 nî lūn-bûn
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2006年の論文
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name
Arg452 substitution of the ery ...... itself affect enzyme activity.
@en
Arg452 substitution of the ery ...... itself affect enzyme activity.
@nl
type
label
Arg452 substitution of the ery ...... itself affect enzyme activity.
@en
Arg452 substitution of the ery ...... itself affect enzyme activity.
@nl
prefLabel
Arg452 substitution of the ery ...... itself affect enzyme activity.
@en
Arg452 substitution of the ery ...... itself affect enzyme activity.
@nl
P2093
P2860
P1476
Arg452 substitution of the ery ...... itself affect enzyme activity.
@en
P2093
Ben C J Hamel
Elisabeth I Minder
Hideo Harigae
Kazumichi Furuyama
Nicole Blijlevens
Shigeki Shibahara
Shigeru Sassa
Tadao Kuribara
Tom Heller
Toru Shimizu
P2860
P356
10.1111/J.1600-0609.2005.00541.X
P577
2006-01-01T00:00:00Z