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Pesquisa : D05.750.078.593.450.300.100 [Categoria DeCS]
Referências encontradas : 287 [refinar]
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[PMID]:28526297
[Au] Autor:Badowski C; Sim AYL; Verma C; Szeverényi I; Natesavelalar C; Terron-Kwiatkowski A; Harper J; O'Toole EA; Lane EB
[Ad] Endereço:Institute of Medical Biology (A*STAR) & Skin Research Institute of Singapore, Immunos, Singapore.
[Ti] Título:Modeling the Structure of Keratin 1 and 10 Terminal Domains and their Misassembly in Keratoderma.
[So] Source:J Invest Dermatol;137(9):1914-1923, 2017 Sep.
[Is] ISSN:1523-1747
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The terminal domains of suprabasal keratins of the skin epithelium are very resistant to evidence-based structural analysis because of their inherent flexibility and lack of predictable structure. We present a model for the structure and interactions of the head and tail domains of epidermal keratins 1 and 10, based on all-atom 3D simulations of keratin primary amino acid sequences, and tyrosine phosphorylation predictions, extracted from published databases. We observed that keratin 1 and 10 end domains are likely to form a tetrameric terminal domain complex incorporating a reversibly extendable region potentially acting as a molecular spring. This structure is formed by intermolecular stacking of aromatic residues, which would spatially constrain the keratin 1/keratin 10 end domains to allow filament compaction and bundling, whilst also retaining extensibility to ensure flexibility of the keratin filament network in the differentiating epidermis. The tetrameric terminal domain complex model may also help to elucidate the effects of mutations in the end domains of suprabasal keratins and so contribute to understanding of the mechanisms leading to keratinopathies such as striate palmoplantar keratoderma, as reported in this study.
[Mh] Termos MeSH primário: Imagem Tridimensional
Queratina-10/genética
Queratina-1/genética
Ceratodermia Palmar e Plantar/genética
[Mh] Termos MeSH secundário: Células Cultivadas
DNA/análise
Células Epiteliais/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Ceratodermia Palmar e Plantar/patologia
Mutação
Fenótipo
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Keratin-1); 147785-83-9 (Keratin-10); 9007-49-2 (DNA)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170521
[St] Status:MEDLINE


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[PMID]:28482041
[Au] Autor:Trivedi S; Uhlemann AC; Herman-Bausier P; Sullivan SB; Sowash MG; Flores EY; Khan SD; Dufrêne YF; Lowy FD
[Ad] Endereço:1Division of Infectious Diseases.
[Ti] Título:The Surface Protein SdrF Mediates Staphylococcus epidermidis Adherence to Keratin.
[So] Source:J Infect Dis;215(12):1846-1854, 2017 Jun 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Background: Staphylococcus epidermidis, a major component of skin flora, is an opportunist, often causing prosthetic device infections. A family of structurally related proteins mediates staphylococcal attachment to host tissues, contributing to the success of S. epidermidis as a pathogen. We examined the ability of the surface protein SdrF to adhere to keratin, a major molecule expressed on the skin surface. Methods: A heterologous Lactococcus lactis expression system was used to express SdrF and its ligand-binding domains. Adherence to keratin types 1 and 10, human foreskin keratinocytes, and nasal epithelial cells was examined. Results: SdrF bound human keratins 1 and 10 and adhered to keratinocytes and epithelial cells. Binding involved both the A and B domains. Anti-SdrF antibodies reduced adherence of S. epidermidis to keratin and keratinocytes. RNA interference reduced keratin synthesis in keratinocytes and, as a result, SdrF adherence. Direct force measurements using atomic force microscopy showed that SdrF mediates bacterial adhesion to keratin 10 through strong and weak bonds involving the A and B regions; strong adhesion was primarily mediated by the A region. Conclusions: These studies demonstrate that SdrF mediates adherence to human keratin and suggest that SdrF may facilitate S. epidermidis colonization of the skin.
[Mh] Termos MeSH primário: Aderência Bacteriana
Proteínas de Bactérias/metabolismo
Queratina-10/metabolismo
Queratina-1/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
Infecções Estafilocócicas/metabolismo
Staphylococcus epidermidis/fisiologia
[Mh] Termos MeSH secundário: Células Epiteliais/citologia
Seres Humanos
Queratinócitos/microbiologia
Lactococcus lactis
Proteínas de Membrana/metabolismo
Microscopia de Força Atômica
Nariz/citologia
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Keratin-1); 0 (Membrane Proteins); 0 (Membrane Transport Proteins); 147785-83-9 (Keratin-10)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jix213


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[PMID]:27722766
[Au] Autor:Severino-Freire M; Jonca N; Pichery M; Tournier E; Chassaing N; Mazereeuw-Hautier J
[Ad] Endereço:Department of Dermatology, Toulouse University Hospital, Toulouse, 24 chemin de Pouvourville TSA 30030, FR-31059 Toulouse cedex 9, France. maella.severino@hotmail.fr.
[Ti] Título:Extensive Post-zygotic Mosaicism of KRT1 or KRT10 Mutation Mimicking Classical Epider-molytic Ichthyosis.
[So] Source:Acta Derm Venereol;97(3):387-388, 2017 03 10.
[Is] ISSN:1651-2057
[Cp] País de publicação:Sweden
[La] Idioma:eng
[Mh] Termos MeSH primário: Hiperceratose Epidermolítica/genética
Queratina-10/genética
Queratina-1/genética
Mosaicismo
Mutação
[Mh] Termos MeSH secundário: Adolescente
Adulto
Análise Mutacional de DNA
Diagnóstico Diferencial
Feminino
Predisposição Genética para Doença
Seres Humanos
Hiperceratose Epidermolítica/diagnóstico
Masculino
Fenótipo
Valor Preditivo dos Testes
Pele/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KRT1 protein, human); 0 (KRT10 protein, human); 0 (Keratin-1); 147785-83-9 (Keratin-10)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161011
[St] Status:MEDLINE
[do] DOI:10.2340/00015555-2542


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[PMID]:27595935
[Au] Autor:Bunick CG; Milstone LM
[Ad] Endereço:Department of Dermatology, Yale University, New Haven, Connecticut, USA. Electronic address: christopher.bunick@yale.edu.
[Ti] Título:The X-Ray Crystal Structure of the Keratin 1-Keratin 10 Helix 2B Heterodimer Reveals Molecular Surface Properties and Biochemical Insights into Human Skin Disease.
[So] Source:J Invest Dermatol;137(1):142-150, 2017 Jan.
[Is] ISSN:1523-1747
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Keratins 1 (K1) and 10 (K10) are the primary keratins expressed in differentiated epidermis. Mutations in K1/K10 are associated with human skin diseases. We determined the crystal structure of the complex between the distal (2B) helices of K1 and K10 to better understand how human keratin structure correlates with function. The 3.3 Å resolution structure confirms many features inferred by previous biochemical analyses, but adds unexpected insights. It demonstrates a parallel, coiled-coil heterodimer with a predominantly hydrophobic intermolecular interface; this heterodimer formed a higher order complex with a second K1-K10-2B heterodimer via a Cys401 disulfide link, although the bond angle is unanticipated. The molecular surface analysis of K1-K10-2B identified several pockets, one adjacent to the disulfide linkage and conserved in K5-K14. The solvent accessible surface area of the K1-K10 structure is 20-25% hydrophobic. The 2B region contains mixed acidic and basic patches proximally (N-terminal), whereas it is largely acidic distally (C-terminal). Mapping of conserved and nonconserved residues between K1-K10 and K5-K14 onto the structure demonstrated the majority of unique residues align along the outer helical ridge. Finally, the structure permitted a fresh analysis of the deleterious effects caused by K1/K10 missense mutations found in patients with phenotypic skin disease.
[Mh] Termos MeSH primário: Queratina-10/genética
Queratina-1/genética
Estrutura Molecular
Dermatopatias/genética
[Mh] Termos MeSH secundário: Células Cultivadas
Epiderme/citologia
Epiderme/metabolismo
Seres Humanos
Queratina-1/química
Queratina-10/química
Mutação de Sentido Incorreto
Sensibilidade e Especificidade
Dermatopatias/patologia
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Keratin-1); 147785-83-9 (Keratin-10)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160907
[St] Status:MEDLINE


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[PMID]:27291450
[Au] Autor:Saito R; Boyce A; Hsu CK; Rashidghamat E; Hide M; Wedgeworth EK; Flohr C; Mellerio JE; McGrath JA
[Ad] Endereço:St John's Institute of Dermatology, King's College London, Guy's Hospital, London, U.K.
[Ti] Título:Predictive phenotyping of inherited ichthyosis by next-generation DNA sequencing.
[So] Source:Br J Dermatol;176(1):249-251, 2017 Jan.
[Is] ISSN:1365-2133
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Ictiose Lamelar/genética
[Mh] Termos MeSH secundário: Seres Humanos
Lactente
Queratina-10/genética
Masculino
Mutação/genética
Fenótipo
Sítios de Splice de RNA/genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:CASE REPORTS; LETTER
[Nm] Nome de substância:
0 (KRT10 protein, human); 0 (RNA Splice Sites); 147785-83-9 (Keratin-10)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160614
[St] Status:MEDLINE
[do] DOI:10.1111/bjd.14807


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[PMID]:27225831
[Au] Autor:Kono M; Fukai K; Omura R; Sugawara K; Tsuruta D; Sugiura K; Akiyama M
[Ad] Endereço:Department of Dermatology, Nagoya University Graduate School of Medicine, Nagoya, Japan.
[Ti] Título:A case of epidermolytic ichthyosis showing a very mild phenotype due to a novel tail extension mutation in KRT10.
[So] Source:J Eur Acad Dermatol Venereol;31(2):e68-e69, 2017 Feb.
[Is] ISSN:1468-3083
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Hiperceratose Epidermolítica/fisiopatologia
Queratina-10/genética
Mutação
[Mh] Termos MeSH secundário: Criança
Feminino
Seres Humanos
Hiperceratose Epidermolítica/genética
[Pt] Tipo de publicação:CASE REPORTS; LETTER
[Nm] Nome de substância:
0 (KRT10 protein, human); 147785-83-9 (Keratin-10)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160527
[St] Status:MEDLINE
[do] DOI:10.1111/jdv.13729


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[PMID]:27846299
[Au] Autor:Okano J; Kojima H; Katagi M; Nakagawa T; Nakae Y; Terashima T; Kurakane T; Kubota M; Maegawa H; Udagawa J
[Ad] Endereço:Department of Anatomy and Cell Biology, Shiga University of Medical Science, Shiga, Japan.
[Ti] Título:Hyperglycemia Induces Skin Barrier Dysfunctions with Impairment of Epidermal Integrity in Non-Wounded Skin of Type 1 Diabetic Mice.
[So] Source:PLoS One;11(11):e0166215, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diabetes causes skin complications, including xerosis and foot ulcers. Ulcers complicated by infections exacerbate skin conditions, and in severe cases, limb/toe amputations are required to prevent the development of sepsis. Here, we hypothesize that hyperglycemia induces skin barrier dysfunction with alterations of epidermal integrity. The effects of hyperglycemia on the epidermis were examined in streptozotocin-induced diabetic mice with/without insulin therapy. The results showed that dye leakages were prominent, and transepidermal water loss after tape stripping was exacerbated in diabetic mice. These data indicate that hyperglycemia impaired skin barrier functions. Additionally, the distribution of the protein associated with the tight junction structure, tight junction protein-1 (ZO-1), was characterized by diffuse and significantly wider expression in the diabetic mice compared to that in the control mice. In turn, epidermal cell number was significantly reduced and basal cells were irregularly aligned with ultrastructural alterations in diabetic mice. In contrast, the number of corneocytes, namely, denucleated and terminally differentiated keratinocytes significantly increased, while their sensitivity to mechanical stress was enhanced in the diabetic mice. We found that cell proliferation was significantly decreased, while apoptotic cells were comparable in the skin of diabetic mice, compared to those in the control mice. In the epidermis, Keratin 5 and keratin 14 expressions were reduced, while keratin 10 and loricrin were ectopically induced in diabetic mice. These data suggest that hyperglycemia altered keratinocyte proliferation/differentiation. Finally, these phenotypes observed in diabetic mice were mitigated by insulin treatment. Reduction in basal cell number and perturbation of the proliferation/differentiation process could be the underlying mechanisms for impaired skin barrier functions in diabetic mice.
[Mh] Termos MeSH primário: Proliferação Celular/genética
Diabetes Mellitus Tipo 1/metabolismo
Hiperglicemia/metabolismo
Pele/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/genética
Diferenciação Celular/efeitos dos fármacos
Diferenciação Celular/genética
Proliferação Celular/efeitos dos fármacos
Diabetes Mellitus Tipo 1/patologia
Epiderme/metabolismo
Epiderme/patologia
Epiderme/ultraestrutura
Regulação da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Hiperglicemia/patologia
Insulina/administração & dosagem
Insulina/metabolismo
Queratina-10/biossíntese
Queratina-10/genética
Queratina-14/biossíntese
Queratina-14/genética
Queratina-5/biossíntese
Queratina-5/genética
Queratinócitos/metabolismo
Queratinócitos/patologia
Queratinócitos/ultraestrutura
Proteínas de Membrana/biossíntese
Camundongos
Camundongos Endogâmicos NOD/metabolismo
Pele/patologia
Pele/ultraestrutura
Proteína da Zônula de Oclusão-1/biossíntese
Proteína da Zônula de Oclusão-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insulin); 0 (Keratin-14); 0 (Keratin-5); 0 (Krt1-14 protein, mouse); 0 (Membrane Proteins); 0 (Tjp1 protein, mouse); 0 (Zonula Occludens-1 Protein); 0 (loricrin); 147785-83-9 (Keratin-10)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161116
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0166215


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[PMID]:27664712
[Au] Autor:Lim YH; Choate KA
[Ad] Endereço:Department of Dermatology, Yale University School of Medicine, New Haven, Connecticut, USA; Department of Pathology, Yale University School of Medicine, New Haven, Connecticut, USA; Department of Genetics, Yale University School of Medicine, New Haven, Connecticut, USA.
[Ti] Título:Expanding the Mutation Spectrum of Ichthyosis with Confetti.
[So] Source:J Invest Dermatol;136(10):1941-1943, 2016 Oct.
[Is] ISSN:1523-1747
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ichthyosis with confetti is a rare, autosomal dominant disorder caused by frameshift mutations in KRT10 or KRT1 and characterized by the development of white, genetically revertant macules in red, diseased skin. All cases result from mutations affecting the tail domains of keratin-10 or keratin-1, and Suzuki et al. expand the mutation spectrum for ichthyosis with confetti caused by mutations in KRT1, showing that a polyarginine frameshift in the keratin-1 tail can also cause this disorder.
[Mh] Termos MeSH primário: Ictiose/genética
Queratina-10/genética
[Mh] Termos MeSH secundário: Seres Humanos
Ictiose Lamelar
Queratina-1/genética
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Keratin-1); 147785-83-9 (Keratin-10)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160925
[St] Status:MEDLINE


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[PMID]:27584795
[Au] Autor:Zhang J; An X; Han Y; Ma R; Yang K; Zhang L; Chi J; Li W; Llobet-Navas D; Xu Y; Jiang Y
[Ad] Endereço:Key Laboratory, Department of Otolaryngology-Head and Neck Surgery, Affiliated Hospital of Qingdao University, Qingdao, Shandong 266003, China.
[Ti] Título:Overexpression of JARID1B promotes differentiation via SHIP1/AKT signaling in human hypopharyngeal squamous cell carcinoma.
[So] Source:Cell Death Dis;7(9):e2358, 2016 Sep 01.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Histone H3 (H3K4) demethylase JARID1B is aberrantly upregulated in many types of tumor and has been proposed to function as oncogene. Here we show that JARID1B is elevated in moderate and high-differentiated human hypopharyngeal squamous cell carcinoma (HPSCC) compared with low-differentiated HPSCC. Overexpression of JARID1B in FaDu cells increased epithelial differentiation marker K10 expression and inhibited cell proliferation. JARID1B and K10 mRNA expression is high correlated in HPSCC patients. Mechanistically, we found JARID1B directly bound to PI3K/AKT signaling inhibitor SHIP1 gene promoter and decreased SHIP1 gene expression. Activation of downstream AKT resulted in increased ß-catenin signaling, by which promoted target genes Fra-1 and Jun, together with other AP-1 transcription factors, leading to K10 expression. Forced expression of SHIP1 rescued JARID1B-induced phenotypes on FaDu cell differentiation and proliferation. Taken together, our findings provide first evidence that elevated expression of JARID1B has a critical role in promoting HPSCC differentiation and inhibiting proliferation, suggesting JARID1B may function as a tumor suppressor in squamous cell cancers and implying a novel important therapeutic strategy of HPSCC.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/metabolismo
Carcinoma de Células Escamosas/patologia
Diferenciação Celular
Neoplasias Hipofaríngeas/metabolismo
Neoplasias Hipofaríngeas/patologia
Histona Desmetilases com o Domínio Jumonji/metabolismo
Proteínas Nucleares/metabolismo
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Repressoras/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Carcinoma de Células Escamosas/genética
Diferenciação Celular/genética
Linhagem Celular Tumoral
Regulação para Baixo/genética
Ativação Enzimática
Regulação Neoplásica da Expressão Gênica
Técnicas de Silenciamento de Genes
Seres Humanos
Neoplasias Hipofaríngeas/genética
Queratina-10/genética
Queratina-10/metabolismo
Fenótipo
Transcrição Genética
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Repressor Proteins); 0 (beta Catenin); 147785-83-9 (Keratin-10); EC 1.14.11.- (Jumonji Domain-Containing Histone Demethylases); EC 1.14.11.- (KDM5B protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.1.3.86 (INPP5D protein, human); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160902
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2016.262


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[PMID]:27418529
[Au] Autor:Rice RH; Durbin-Johnson BP; Ishitsuka Y; Salemi M; Phinney BS; Rocke DM; Roop DR
[Ti] Título:Proteomic Analysis of Loricrin Knockout Mouse Epidermis.
[So] Source:J Proteome Res;15(8):2560-6, 2016 Aug 05.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The crosslinked envelope of the mammalian epidermal corneocyte serves as a scaffold for assembly of the lipid barrier of the epidermis. Thus, deficient envelope crosslinking by keratinocyte transglutaminase (TGM1) is a major cause of the human autosomal recessive congenital ichthyoses characterized by barrier defects. Expectations that loss of some envelope protein components would also confer an ichthyosis phenotype have been difficult to demonstrate. To help rationalize this observation, the protein profile of epidermis from loricrin knockout mice has been compared to that of wild type. Despite the mild phenotype of the knockout, some 40 proteins were incorporated into envelope material to significantly different extents compared to those of wild type. Nearly half were also incorporated to similarly altered extents into the disulfide bonded keratin network of the corneocyte. The results suggest that loss of loricrin alters their incorporation into envelopes as a consequence of protein-protein interactions during cell maturation. Mass spectrometric protein profiling revealed that keratin 1, keratin 10, and loricrin are prominent envelope components and that dozens of other proteins are also components. This finding helps rationalize the potential formation of functional envelopes, despite loss of a single component, due to the availability of many alternative transglutaminase substrates.
[Mh] Termos MeSH primário: Epiderme/química
Proteínas de Membrana/genética
Proteínas/análise
Proteômica/métodos
[Mh] Termos MeSH secundário: Animais
Ictiose
Queratina-1
Queratina-10
Camundongos
Camundongos Knockout
Domínios e Motivos de Interação entre Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Keratin-1); 0 (Krt1-10 protein, mouse); 0 (Membrane Proteins); 0 (Proteins); 0 (loricrin); 147785-83-9 (Keratin-10)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160716
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.6b00108



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