Acral lamellar ichthyosis with amino acid substitution in the C‐terminus of keratin 2-Reference-Cited by-同舟云学术

Acral lamellar ichthyosis with amino acid substitution in the C‐terminus of keratin 2

Published:2022-11-17 Issue:4 Volume:37 Page:817-822
ISSN:0926-9959
Container-title:Journal of the European Academy of Dermatology and Venereology
language:en
Short-container-title:Acad Dermatol Venereol

Author:

Frommherz Leonie¹²^ORCID,Komlosi Katalin³^ORCID,Hewel Charlotte⁴,Kopp Julia³,Dewenter Malin⁴,Zimmer Andreas³^ORCID,Bartsch Oliver⁴,Linke Matthias⁴,Technau‐Hafsi Kristin¹,Gerber Susanne⁴⁵,Fischer Judith³,Has Cristina¹^ORCID

Affiliation:

1. Department of Dermatology, Medical Center, Faculty of Medicine University of Freiburg Freiburg Germany

2. Department of Dermatology and Allergy Ludwig‐Maximilians‐Universität München (LMU) Munich, University Hospital Munich Germany

3. Institute of Human Genetics, Medical Center, Faculty of Medicine University of Freiburg Freiburg Germany

4. Institute of Human Genetics University Medical Center of the Johannes Gutenberg University Mainz Mainz Germany

5. Computational Systems Genomics Group Johannes Gutenberg University Mainz Mainz Germany

Funder

European Academy of Dermatology and Venereology

Publisher

Wiley

Subject

Infectious Diseases,Dermatology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/jdv.18719

Reference14 articles.

1. Revised nomenclature and classification of inherited ichthyoses: Results of the First Ichthyosis Consensus Conference in Sorèze 2009

2. Bathing‐suit ichthyosis. A peculiar phenotype of lamellar ichthyosis in south African blacks;Jacyk WK;Eur J Dermatol,2005

3. Acral lamellar Ichthyosis - expanding the phenotype of temperature-sensitive keratinization disorders

4. Bathing suit ichthyosis is caused by transglutaminase-1 deficiency: evidence for a temperature-sensitive phenotype

5. Sixteen novel mutations in PNPLA1 in patients with autosomal recessive congenital ichthyosis reveal the importance of an extended patatin domain in PNPLA1 that is essential for proper human skin barrier function