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1.
Zentralbl Chir ; 142(1): 39-45, 2017 Feb.
Artigo em Alemão | MEDLINE | ID: mdl-25393734

RESUMO

Background: History taking and systematic clinical examination are central techniques of physicians. Medicine in general and surgery in particular frequently require immediate decisions and start of therapies. So far, a standardised surgical system for history taking and clinical examination in teaching has been lacking at our faculty. A consensus of all medical faculties on a standardised system could be a tool to improve the medical teaching and education at our teaching institutions. Methods: The established Anglo-Saxonian system of history taking and clinical examination was adapted to our own clinical needs. Thereafter, this system was sent out to all chairmen of general and visceral surgery departments in German University Hospitals asking for evaluation and improvements. We adapted the system according to the chairmen's comments and suggestions. Since winter semester 2011 this system has been integrated into the clinical course of history taking and examination. It is compulsory for all 5th semester students (first clinical year/graduate course) at the Universitätsmedizin Greifswald. In addition, a video was produced demonstrating all major techniques of clinical examination. This video is available for all students on a password blocked site of the World Wide Web. Results: Altogether, 89 % of all contacted chairmen returned their comments and suggestions for improvements. After implementation of the new system, positive evaluations of students increased significantly from 63.5 to 77.0 % in general and abdominal surgery (p < 0.0001) and from 76.4 to 83.5 % in vascular and thoracic surgery (p < 0.0001). Conclusions: The presented system is a standardised tool of history taking and clinical examination applicable for students as well as qualified surgeons in daily routine work. It has been approved by the majority of the departments of surgery of all German university hospitals. Furthermore, it can be applied by other medical specialties, in particular, internal medicine. Furthermore, the standardisation of history taking and clinical examination can contribute to improve patients' safety as well as medical documentation. Also, the standardisation will be a sound basis for expert medical opinions in legal actions. Finally, it has improved the value of medical education at our medical faculty and could form the basis for the development of national medical standards.


Assuntos
Educação Médica/normas , Cirurgia Geral/educação , Anamnese/normas , Exame Físico/normas , Universidades , Atitude do Pessoal de Saúde , Currículo/normas , Alemanha , Hospitais Universitários/normas , Humanos , Melhoria de Qualidade/normas
2.
Nucleic Acids Res ; 29(22): 4707-15, 2001 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-11713321

RESUMO

Kinetoplastid protozoa regulate their gene expression primarily through control of mRNA degradation and translation. We describe here the degradation of three reporter mRNAs in Trypanosoma brucei. One mRNA had the 3'-untranslated region (3'-UTR) from the developmentally regulated EP1 mRNA, which is abundant in the procyclic (tsetse fly) form of the parasite but is almost undetectable in the bloodstream form. This untranslated region includes a 26 nt U-rich sequence that causes extreme RNA instability in the bloodstream form. The two other RNAs, which are not developmentally regulated, had either the actin 3'-UTR, or a version of the EP1 sequence lacking the 26 nt bloodstream-form instability element. All RNAs had poly(A) tails approximately 200 nt long, in both bloodstream and procyclic forms. Degradation of the two constitutively expressed mRNAs involved deadenylation and degradation by both 5'-->3' and 3'-->5' exonucleases. In contrast, in bloodstream forms, the 3'-end of the RNA bearing the bloodstream-form instability element disappeared very rapidly after transcription inhibition and partially deadenylated intermediates were not seen. The instability element may cause extremely rapid deadenylation, or it may be targeted by an endonuclease.


Assuntos
Regiões 3' não Traduzidas/metabolismo , Glicoproteínas de Membrana/genética , Proteínas de Protozoários , RNA Mensageiro/metabolismo , Trypanosoma brucei brucei/genética , Regiões 3' não Traduzidas/genética , Animais , Cloranfenicol O-Acetiltransferase/genética , RNA Polimerases Dirigidas por DNA/metabolismo , Plasmídeos/genética , Poli A/genética , Poli A/metabolismo , RNA Mensageiro/genética , RNA de Protozoário/genética , RNA de Protozoário/metabolismo , Proteínas Recombinantes de Fusão/genética , Transcrição Gênica , Trypanosoma brucei brucei/metabolismo , Proteínas Virais
3.
J Biol Chem ; 272(4): 2230-5, 1997 Jan 24.
Artigo em Inglês | MEDLINE | ID: mdl-8999928

RESUMO

The homo-oligomeric Hip protein cooperates with the 70-kDa heat shock cognate Hsc70 in the folding of newly synthesized polypeptide chains and in the conformational regulation of signaling molecules known to interact with Hsc70 and Hsp90. In order to further assess the role of Hip during protein biogenesis, a structure-function analysis of the Hip protein was initiated. By employing the yeast two-hybrid system, the Hsc70-binding site of Hip was mapped to a domain comprising multiple tetratricopeptide repeats and flanking charged alpha-helices. Affinity chromatography confirmed direct interaction of isolated Hip fragments and protein fusions bearing this region with the ATPase domain of Hsc70 in an ATP- and salt-dependent manner. Contact of Hip with the ATPase domain appears to be mediated primarily by the positively charged alpha-helix following the tetratricopeptide repeats. Furthermore, a domain required for homo-oligomerization was identified at the extreme amino terminus of Hip.


Assuntos
Proteínas de Fase Aguda/química , Antígenos de Neoplasias , Biomarcadores Tumorais , Lectinas Tipo C , Lectinas/química , Adenosina Trifosfatases/metabolismo , Sequência de Aminoácidos , Animais , Sítios de Ligação , Proteínas de Transporte/química , Proteínas de Transporte/metabolismo , Cromatografia em Gel , Sequência Consenso , Proteínas de Choque Térmico HSC70 , Proteínas de Choque Térmico HSP70/metabolismo , Proteínas de Choque Térmico HSP90/química , Proteínas de Choque Térmico HSP90/metabolismo , Dados de Sequência Molecular , Proteínas Associadas a Pancreatite , Conformação Proteica , Estrutura Secundária de Proteína , Ratos , Relação Estrutura-Atividade
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