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1.
J Empir Res Hum Res Ethics ; 15(4): 279-291, 2020 10.
Article in English | MEDLINE | ID: mdl-32233729

ABSTRACT

Tribal Institutional Review Boards (TIRBs) in the United States assert their rights within sovereign nations by developing ethical research processes that align with tribal values to protect indigenous knowledge systems and their community from cultural appropriation, exploitation, misuse, and harm. We reviewed six TIRB applications and processes to gain a better understanding about their requirements and research ethics. We located 48 activated and deactivated TIRBs in a database, mapped them in relation to tribal reservation lands, and then conducted in-depth content analysis. Our analysis demonstrates the importance of building relationships, becoming fully acquainted with the TIRB's operating environment before seeking research approval, and issues related to tribal data management practices.


Subject(s)
Ethics Committees, Research , Indians, North American , Ethics, Research , Humans , United States
2.
Congenit Heart Dis ; 8(1): E13-6, 2013.
Article in English | MEDLINE | ID: mdl-21824332

ABSTRACT

We present a case of a premature female infant, with a delayed diagnosis of hemitruncus, who underwent primary repair at 105 days of life. There have been few published reports of premature infants with hemitruncus, and none to our knowledge who underwent repair that was significantly delayed.


Subject(s)
Aorta/abnormalities , Cardiac Surgical Procedures/methods , Infant, Extremely Low Birth Weight , Infant, Premature, Diseases/surgery , Pulmonary Artery/abnormalities , Aorta/diagnostic imaging , Ductus Arteriosus, Patent/surgery , Female , Humans , Infant, Newborn , Infant, Premature , Pulmonary Artery/diagnostic imaging , Pulmonary Artery/surgery , Time Factors , Ultrasonography , Vascular Surgical Procedures
3.
Langenbecks Arch Surg ; 396(7): 1047-53, 2011 Oct.
Article in English | MEDLINE | ID: mdl-21826521

ABSTRACT

BACKGROUND: The decision to optimize the processes in the operating tract was based on two factors: competition among clinics and a desire to optimize the use of available resources. The aim of the project was to improve operating room (OR) capacity utilization by reduction of change and throughput time per patient. SETTING: The study was conducted at Centre Hospitalier Emil Mayrisch Clinic for specialized care (n = 618 beds) Luxembourg (South). METHOD: A prospective analysis was performed before and after the implementation of optimized processes. Value stream analysis and design (value stream mapping, VSM) were used as tools. VSM depicts patient throughput and the corresponding information flows. Furthermore it is used to identify process waste (e.g. time, human resources, materials, etc.). For this purpose, change times per patient (extubation of patient 1 until intubation of patient 2) and throughput times (inward transfer until outward transfer) were measured. VSM, change and throughput times for 48 patient flows (VSM A(1), actual state = initial situation) served as the starting point. Interdisciplinary development of an optimized VSM (VSM-O) was evaluated. Prospective analysis of 42 patients (VSM-A(2)) without and 75 patients (VSM-O) with an optimized process in place were conducted. RESULTS: The prospective analysis resulted in a mean change time of (mean ± SEM) VSM-A(2) 1,507 ± 100 s versus VSM-O 933 ± 66 s (p < 0.001). The mean throughput time VSM-A(2) (mean ± SEM) was 151 min (±8) versus VSM-O 120 min (±10) (p < 0.05). This corresponds to a 23% decrease in waiting time per patient in total. CONCLUSION: Efficient OR capacity utilization and the optimized use of human resources allowed an additional 1820 interventions to be carried out per year without any increase in human resources. In addition, perioperative patient monitoring was increased up to 100%.


Subject(s)
Operating Rooms/statistics & numerical data , Surgical Procedures, Operative/statistics & numerical data , Time Management , Workload , Female , Health Care Surveys , Humans , Luxembourg , Male , Organizational Innovation , Patient Care , Prospective Studies , Surgical Procedures, Operative/methods , Total Quality Management , Waiting Lists
4.
Biol Chem ; 389(2): 127-34, 2008 Feb.
Article in English | MEDLINE | ID: mdl-18163882

ABSTRACT

Abstract Bacterial thiM riboswitches contain aptamer domains that bind the metabolite thiamine pyrophosphate (TPP). Binding of TPP to the aptamer domain induces structural rearrangements that are relayed to the expression domain, thereby interfering with gene expression. Here, we report identification of three putative thiM riboswitches from different bacteria and analysis of their secondary structures. Chemical probing revealed that the riboswitches share similar secondary structures in their aptamer domains that can communicate with the highly variant expression domains in a mechanism likely involving sequestration of the Shine-Dalgarno sequence. Remarkably, the aptamer domain of the thiM gene of Desulfovibrio vulgaris binds TPP with similar affinity and selectivity as that of Escherichia coli, although nucleotides previously shown to form direct contacts to the metabolite are mutated. We also designed small RNA hairpins for each riboswitch that bind the RNA only in the absence of the metabolite. Our study shows that aptamer domains in riboswitches with high similarity in their secondary structures can communicate with a broad variety of non-related expression domains by similar mechanisms.


Subject(s)
Aptamers, Peptide , Gram-Negative Bacteria/chemistry , Phosphotransferases (Alcohol Group Acceptor)/chemistry , Phosphotransferases (Alcohol Group Acceptor)/physiology , Protein Interaction Domains and Motifs , Desulfovibrio vulgaris , Pectobacterium carotovorum , Phosphotransferases (Alcohol Group Acceptor)/metabolism , Protein Structure, Secondary , Protein Structure, Tertiary , Rhodobacter sphaeroides , Thiamine Pyrophosphate/metabolism
6.
Nucleic Acids Res ; 35(11): 3713-22, 2007.
Article in English | MEDLINE | ID: mdl-17517779

ABSTRACT

The thiM riboswitch contains an aptamer domain that adaptively binds the coenzyme thiamine pyrophosphate (TPP). The binding of TPP to the aptamer domain induces structural rearrangements that are relayed to a second domain, the so-called expression domain, thereby interfering with gene expression. The recently solved crystal structures of the aptamer domains of the thiM riboswitches in complex with TPP revealed how TPP stabilizes secondary and tertiary structures in the RNA ligand complex. To understand the global modes of reorganization between the two domains upon metabolite binding the structure of the entire riboswitch in presence and absence of TPP needs to be determined. Here we report the secondary structure of the entire thiM riboswitch from Escherichia coli in its TPP-free form and its transition into the TPP-bound variant, thereby depicting domains of the riboswitch that serve as communication links between the aptamer and the expression domain. Furthermore, structural probing provides an explanation for the lack of genetic control exerted by a riboswitch variant with mutations in the expression domain that still binds TPP.


Subject(s)
Escherichia coli/genetics , RNA, Bacterial/chemistry , Regulatory Sequences, Ribonucleic Acid , Untranslated Regions/chemistry , Base Sequence , Molecular Sequence Data , Mutation , Nucleic Acid Conformation , RNA, Bacterial/metabolism , Thiamine Pyrophosphate/metabolism , Untranslated Regions/metabolism
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