|1.||Epidermolytic Hyperkeratosis (Bullous Congenital Ichthyosiform Erythroderma)
|2.||Muscular Dystrophies (Muscular Dystrophy)
|4.||Wounds and Injuries (Trauma)
|1.||Wiche, Gerhard: 15 articles (12/2015 - 01/2002)|
|2.||Lane, E Birgitte: 9 articles (01/2012 - 01/2002)|
|3.||Jonkman, Marcel F: 7 articles (06/2015 - 04/2002)|
|4.||Shimizu, Hiroshi: 7 articles (09/2013 - 06/2002)|
|5.||Bauer, Johann W: 7 articles (04/2013 - 03/2008)|
|6.||Hashimoto, Takashi: 7 articles (02/2013 - 02/2005)|
|7.||Bruckner-Tuderman, Leena: 7 articles (06/2010 - 01/2002)|
|8.||Lane, E B: 7 articles (01/2007 - 02/2000)|
|9.||Magin, Thomas M: 6 articles (10/2015 - 01/2007)|
|10.||Natsuga, Ken: 6 articles (03/2015 - 03/2010)|
|1.||trimethyloxamine (trimethylamine N-oxide)IBA
05/01/2010 - "Epidermolysis bullosa simplex due to KRT5 mutations: mutation-related differences in cellular fragility and the protective effects of trimethylamine N-oxide in cultured primary keratinocytes."
03/01/2009 - "Characterization of immortalized human epidermolysis bullosa simplex (KRT5) cell lines: trimethylamine N-oxide protects the keratin cytoskeleton against disruptive stress condition."
|2.||Cyproheptadine (Periactin)FDA Link
07/01/2002 - "This study presents new data, examines clinical, histological, ultrastructural, and molecular aspects of MECD, and compares the features seen in this condition with those observed in other well studied keratin diseases such as epidermolysis bullosa simplex. "
06/01/1999 - "Epidermolysis bullosa simplex (EBS) is caused by defective assembly of keratin intermediate filaments in basal keratinocytes and recent studies indicated causal mutations in the keratin KRT5 and KRT14 genes. "
01/01/1996 - "Epidermolysis bullosa simplex (EBS) is caused by an aberration of the keratin intermediate filaments and recent studies indicated causal mutations in the keratin K14 and K5 genes. "
01/01/1994 - "Ultrastructural and immunohistochemical studies of clinically intact skin obtained from three severe neonatal cases of epidermolysis bullosa herpetiformis (Dowling-Meara type) demonstrated disorders in the assembly of keratin intermediate filaments and desmosomes of the keratinocytes. "
10/01/2015 - "Distinct Impact of Two Keratin Mutations Causing Epidermolysis Bullosa Simplex on Keratinocyte Adhesion and Stiffness."
|5.||Keratin-5 (Keratin 5)IBA
07/01/2007 - "A novel autosomal partially dominant mutation designated G476D in the keratin 5 gene causing epidermolysis bullosa simplex Weber-Cockayne type: a family study with a genetic twist."
05/01/2015 - "Epidermolysis bullosa simplex (EBS) is caused by keratin 5 and 14 mutations. "
01/01/2014 - "Epidermolysis bullosa simplex: greater penetrance due to a keratin 5 gene variant."
09/04/2013 - "A novel keratin 5 mutation in an African family with epidermolysis bullosa simplex indicates the importance of the amino acid located at the boundary site between the H1 and coil 1A domains."
04/01/2013 - "Expression of a mutated allele, non-reduced by aging, in a Japanese family with localized epidermolysis bullosa simplex due to a novel mutation, p.Arg169Gly, of keratin 5 gene."
12/15/2015 - "We further demonstrate that keratinocytes have abnormal nuclear morphologies in the epidermis of plectin-deficient, epidermolysis bullosa simplex patients. "
06/01/2015 - "Mutation in exon 1a of PLEC, leading to disruption of plectin isoform 1a, causes autosomal-recessive skin-only epidermolysis bullosa simplex."
03/01/2015 - "Plectin deficiency causes autosomal recessive epidermolysis bullosa simplex (EBS) with involvement of the skin and other organs, such as muscle and gastrointestinal tract, depending on the expression pattern of the defective protein. "
01/01/2014 - "Plectin mutations underlie epidermolysis bullosa simplex in 8% of patients."
03/01/2010 - "Plectin expression patterns determine two distinct subtypes of epidermolysis bullosa simplex."
|7.||Proteins (Proteins, Gene)IBA
11/01/2014 - "Genetic alterations of these proteins cause epidermolysis bullosa simplex (EBS) characterized by disturbed cytoarchitecture and cell fragility. "
11/01/1998 - "The present study investigated the expression patterns of keratins and CCE precursor proteins in 15 patients with epidermolysis bullosa simplex (EBS), which is caused by mutations in the genes that encode for the basal keratins, keratins 5 and 14. "
01/01/2012 - "Epidermolysis bullosa simplex (EBS) is an inherited skin-blistering disease that is caused by dominant mutations in the genes for keratin K5 or K14 proteins. "
03/01/2010 - "One such disease is epidermolysis bullosa simplex (EBS), caused by mutations in the structural proteins (keratins K5 or K14) of the proliferative compartment of the epidermis (basal keratinocyte layer), leading to cell fragility and blistering. "
11/01/1998 - "Abnormalities of basal cell keratin in epidermolysis bullosa simplex do not affect the expression patterns of suprabasal keratins and cornified cell envelope proteins."
04/01/2003 - "In this study, we report two novel frameshift mutations that are predicted to alter the tail of keratin 1 or keratin 5, leading to an atypical form of epidermolytic hyperkeratosis and a mild form of epidermolysis bullosa simplex, respectively. "
04/01/2003 - "Epidermolytic hyperkeratosis and epidermolysis bullosa simplex caused by frameshift mutations altering the v2 tail domains of keratin 1 and keratin 5."
01/01/2006 - "Instead, they have been associated with several distinct clinical phenotypes, such as epidermolysis bullosa simplex with mottled pigmentation (mutation P25L in the V1 domain of keratin 5), epidermolysis bullosa simplex with migratory circinate erythema (frameshift mutation c1649delG in the V2 domain of keratin 5), striate palmoplantar keratoderma (PPK), and ichthyosis hystrix Curth-Macklin (different frameshift mutations in the V2 domain of keratin 1 (K1)). "
|9.||Pancreatic Elastase (Elastase)IBA
|10.||Carrier Proteins (Binding Protein)IBA
04/06/1998 - "Recent studies with patients suffering from epidermolysis bullosa simplex associated with muscular dystrophy and the targeted gene disruption in mice suggested that plectin, a versatile cytoskeletal linker and intermediate filament-binding protein, may play an essential role in hemidesmosome integrity and stabilization. "