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4.
J Eur Acad Dermatol Venereol ; 33(4): 786-792, 2019 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-30468535

RESUMO

BACKGROUND: Onychomycosis (OM) and traumatic onychodystrophy (OD) are common causes of toenail changes. A clinical diagnosis is often impossible without mycology. Dermoscopy is helpful in this setting but yet underexplored. Prospective comparative studies between OM and OD onychoscopic findings have not been previously performed. OBJECTIVES: We sought to determine distinguishing dermoscopic presentations of OM and traumatic OD. METHODS: We performed a prospective, observational study including patients presenting with ≥1 toenail onychodystrophy. All underwent onychoscopy, clinical and mycological examination. Based on these results, patients received a final diagnosis of OM or OD. Dermoscopic presentations of OM and OD patients were classified in patterns and compared. RESULTS: In all, 110 cases of OM and 82 of traumatic OD were compared. Statistical analyses revealed that the distal pulverized and the irregular spiked macular dermoscopic patterns were predictors of an OM diagnosis. The regular macular, the non-classifiable, the total and partial homogeneous background dermoscopic patterns correlated with traumatic OD diagnosis. CONCLUSIONS: We demonstrated that OM and traumatic OD have distinctive onychoscopic presentations. Dermoscopy may be an important ancillary tool to guide their differential.


Assuntos
Dermoscopia , Unhas Malformadas/diagnóstico por imagem , Onicomicose/diagnóstico por imagem , Ferimentos e Lesões/complicações , Adulto , Idoso , Diagnóstico Diferencial , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Unhas Malformadas/etiologia , Estudos Prospectivos , Dedos do Pé
9.
Nature ; 406(6793): 315-8, 2000 Jul 20.
Artigo em Inglês | MEDLINE | ID: mdl-10917534

RESUMO

Group II introns are self-splicing RNAs that are commonly found in the genes of plants, fungi, yeast and bacteria. Little is known about the tertiary structure of group II introns, which are among the largest natural ribozymes. The most conserved region of the intron is domain 5 (D5), which, together with domain 1 (D1), is required for all reactions catalysed by the intron. Despite the importance of D5, its spatial relationship and tertiary contacts to other active-site constituents have remained obscure. Furthermore, D5 has never been placed directly at a site of catalysis by the intron. Here we show that a set of tertiary interactions (lambda-lambda') links catalytically essential regions of D5 and D1, creating the framework for an active-site and anchoring it at the 5' splice site. Highly conserved elements similar to components of the lambda-lambda' interaction are found in the eukaryotic spliceosome.


Assuntos
Íntrons/fisiologia , RNA Catalítico/fisiologia , Pareamento de Bases , Domínio Catalítico , Sequência Conservada , Íntrons/genética , Mutação , Conformação de Ácido Nucleico , Plasmídeos , RNA Catalítico/genética
10.
Protein Sci ; 8(7): 1475-83, 1999 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-10422836

RESUMO

Production of folded and biologically active protein from Escherichia coli derived inclusion bodies can only be accomplished if a scheme exists for in vitro naturation. Motivated by the need for a rapid and statistically meaningful method of determining and evaluating protein folding conditions, we have designed a new fractional factorial protein folding screen. The screen includes 12 factors shown by previous experiments to enhance protein folding and it incorporates the 12 factors into 16 different folding conditions. By examining a 1/256th fraction of the full factorial, multiple folding conditions were determined for the ligand binding domains from glutamate and kainate receptors, and for lysozyme and carbonic anhydrase B. The impact of each factor on the formation of biologically active material was estimated by calculating factor main effects. Factors and corresponding levels such as pH (8.5) and L-arginine (0.5 M) consistently had a positive effect on protein folding, whereas detergent (0.3 mM lauryl maltoside) and nonpolar additive (0.4 M sucrose) were detrimental to the folding of these four proteins. One of the 16 conditions yielded the most folded material for three out of the four proteins. Our results suggest that this protein folding screen will be generally useful in determining whether other proteins will fold in vitro and, if so, what factors are important. Furthermore, fractional factorial folding screens are well suited to the evaluation of previously untested factors on protein folding.


Assuntos
Anidrases Carbônicas/metabolismo , Muramidase/metabolismo , Ligação Proteica , Receptores de Glutamato/metabolismo , Receptores de Ácido Caínico/metabolismo , Sequência de Aminoácidos , Sequência de Bases , Primers do DNA , Ligantes
11.
J Infect Dis ; 178(1): 164-71, 1998 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-9652436

RESUMO

Consecutive single-patient methicillin-resistant Staphylococcus aureus (MRSA) isolates (270) from 12 hospitals (8217 beds) in metropolitan New York City were collected during May 1996. In 11 of 12 hospitals, MRSA was most frequent in the general medical services. DNA typing ("fingerprinting") revealed that mecA:Tn554:PFGE (pulsed-field gel electrophoresis) type I:A:A accounted for 113 (42%) of 270 isolates, was detected in all hospitals, and was the predominant clone in 9. Thirteen of 15 I:E:F isolates were from 1 hospital, and the remaining 2 were from another hospital of the same health system. Type V:NH:E was isolated from 22 (79%) of the 28 patients with AIDS, including 8 of 9 patients from an additional hospital. Subtype V:NH:E2 was recovered from 11 patients, 9 of whom had AIDS, including all 5 AIDS patients from one floor of a nursing home affiliated with a third hospital. By using both mecA:Tn554 probes and PFGE, MRSA clusters and outbreaks may be detected and provide a rationale for appropriate infection control intervention.


Assuntos
Resistência a Meticilina/genética , Infecções Estafilocócicas/microbiologia , Staphylococcus aureus/efeitos dos fármacos , Staphylococcus aureus/genética , Adolescente , Adulto , Idoso , Idoso de 80 Anos ou mais , Técnicas de Tipagem Bacteriana , Criança , Pré-Escolar , DNA Bacteriano , Feminino , Hospitais Comunitários , Hospitais Universitários , Hospitais de Veteranos , Humanos , Lactente , Masculino , Pessoa de Meia-Idade , Epidemiologia Molecular , Cidade de Nova Iorque/epidemiologia , Infecções Estafilocócicas/epidemiologia , Staphylococcus aureus/classificação , Staphylococcus aureus/isolamento & purificação , Estados Unidos/epidemiologia
12.
J Clin Microbiol ; 34(9): 2121-4, 1996 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-8862569

RESUMO

Fifty-five methicillin-resistant Staphylococcus aureus (MRSA) isolates collected at New York Hospital Medical Center of Queens in 1989 were analyzed by molecular fingerprinting techniques. Close to 70% of these isolates (38 of 55) shared a common pulsed-field gel electrophoretic pattern, carried the same mecA gene polymorph type II, were free of the transposon Tn554, and would not react with a mecI-specific gene probe. An additional five isolates shared all properties of the major MRSA clone except that they carried mecA gene polymorph type III. All these isolates had an extremely heterogeneous methicillin resistance phenotype that belonged to population analysis profile class 1 or 2. The rest of the 12 MRSA isolates showed a variety of chromosomal pulsed-field gel electrophoretic patterns that carried different mecA polymorphs and that also gave positive reactions with DNA probes for Tn554 and for the mecI gene. The molecular features of the majority MRSA clone suggest that it is an archaic MRSA isolate similar in features to early MRSA isolates recovered in the 1960s.


Assuntos
DNA Bacteriano/análise , Resistência a Meticilina/genética , Staphylococcus aureus/isolamento & purificação , Impressões Digitais de DNA , Hospitais Urbanos , New York , Staphylococcus aureus/genética , Staphylococcus aureus/metabolismo
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