Sialic acid catabolism by N-acetylneuraminate pyruvate lyase is essential for muscle function (Q61456223)

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15 April 2020

title

Sialic acid catabolism by N-acetylneuraminate pyruvate lyase is essential for muscle function (English)

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Bojana Rakic

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Suzan El-Rass

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Colin J. Ross

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Nurulamin Abu Bakar

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Britt Drogemoller

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Wyeth Wasserman

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Hilary Vallance

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Ron A. Wevers

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Alexey V Pshezhetsky

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author name string

Xiao-Yan Wen

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Koroboshka Brand-Arzamendi

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Anke Willems

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Karin Huijben

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Afitz Da Silva

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Xuefang Pan

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Robin Ng

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Katheryn Selby

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Anju Mary Philip

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Junghwa Yun

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X Cynthia Ye

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Anna M Lehman

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Fokje Zijlstra

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Jacqueline Moreland

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Monique van Scherpenzeel

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Farhad Karbassi

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Martin Hoskings

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Udo Engelke

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Arjan de Brouwer

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Clara Dm van Karnebeek

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Dirk J Lefeber

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language of work or name

English

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publication date

20 December 2018

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volume

3

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issue

24

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describes a project that uses

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ImageJ

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11 June 2022

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inferred from PubMed Central ID database lookup

cites work

Purification and Characterization ofN-Acetylneuraminate Lyase fromClostridium perfringens

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Pioneer neurons in the mouse trigeminal sensory system

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The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli

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Prenatal diagnosis of Sanfilippo disease type C using a simple fluorometric enzyme assay.

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Expression cloning of the Golgi CMP-sialic acid transporter

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A helix propensity scale based on experimental studies of peptides and proteins

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The terminal enzymes of sialic acid metabolism: acylneuraminate pyruvate-lyases

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Mutations in TMEM76* cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome)

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Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm

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Sialidases in vertebrates: a family of enzymes tailored for several cell functions

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CTCF promotes muscle differentiation by modulating the activity of myogenic regulatory factors

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10.1172/JCI.INSIGHT.122373

Identifiers

DOI

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