A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease

Jacques U. Baenziger

doi:10.1016/S0092-8674(03)00354-4

A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease

Jacques U. Baenziger

Department of Biochemistry & Molecular Biophysics

Research output: Contribution to journal › Review article › peer-review

17 Scopus citations

Abstract

The posttranslational conversion of cysteine to Cα-formylglycine in the catalytic site of mammalian sulfatases is deficient in the rare but devastating disorder multiple sulfatase deficiency (MSD). Two papers in this issue of Cell (Dierks et al., 2003; Cosma et al., 2003) report the cloning of a gene responsible for this activity.

Original language	English
Pages (from-to)	421-422
Number of pages	2
Journal	Cell
Volume	113
Issue number	4
DOIs	https://doi.org/10.1016/S0092-8674(03)00354-4
State	Published - May 16 2003

Access to Document

10.1016/S0092-8674(03)00354-4

Cite this

@article{4ee2d6b4f10a48eea8d8561f903060fb,

title = "A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease",

abstract = "The posttranslational conversion of cysteine to Cα-formylglycine in the catalytic site of mammalian sulfatases is deficient in the rare but devastating disorder multiple sulfatase deficiency (MSD). Two papers in this issue of Cell (Dierks et al., 2003; Cosma et al., 2003) report the cloning of a gene responsible for this activity.",

author = "Baenziger, {Jacques U.}",

year = "2003",

month = may,

day = "16",

doi = "10.1016/S0092-8674(03)00354-4",

language = "English",

volume = "113",

pages = "421--422",

journal = "Cell",

issn = "0092-8674",

number = "4",

}

TY - JOUR

T1 - A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease

AU - Baenziger, Jacques U.

PY - 2003/5/16

Y1 - 2003/5/16

N2 - The posttranslational conversion of cysteine to Cα-formylglycine in the catalytic site of mammalian sulfatases is deficient in the rare but devastating disorder multiple sulfatase deficiency (MSD). Two papers in this issue of Cell (Dierks et al., 2003; Cosma et al., 2003) report the cloning of a gene responsible for this activity.

AB - The posttranslational conversion of cysteine to Cα-formylglycine in the catalytic site of mammalian sulfatases is deficient in the rare but devastating disorder multiple sulfatase deficiency (MSD). Two papers in this issue of Cell (Dierks et al., 2003; Cosma et al., 2003) report the cloning of a gene responsible for this activity.

UR - http://www.scopus.com/inward/record.url?scp=0037726623&partnerID=8YFLogxK

U2 - 10.1016/S0092-8674(03)00354-4

DO - 10.1016/S0092-8674(03)00354-4

M3 - Review article

C2 - 12757700

AN - SCOPUS:0037726623

VL - 113

SP - 421

EP - 422

JO - Cell

JF - Cell

SN - 0092-8674

IS - 4

ER -

A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease

Abstract

Access to Document

Other files and links

Fingerprint

Cite this