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Determination of Death in Mountain Rescue: Recommendations of the International Commission for Mountain Emergency Medicine (ICAR MedCom).

https://arctichealth.org/en/permalink/ahliterature304405
Source
Wilderness Environ Med. 2020 Dec; 31(4):506-520
Publication Type
Journal Article
Review
Date
Dec-2020
Author
Corinna A Schön
Les Gordon
Natalie Hölzl
Mario Milani
Peter Paal
Ken Zafren
Author Affiliation
International Commission for Mountain Emergency Medicine (ICAR MedCom), Zürich, Switzerland; Institute of Forensic Medicine, University of Bern, Bern, Switzerland. Electronic address: corinna.schoen@irm.unibe.ch.
Source
Wilderness Environ Med. 2020 Dec; 31(4):506-520
Date
Dec-2020
Language
English
Publication Type
Journal Article
Review
Keywords
Cardiopulmonary Resuscitation - methods
Death
Humans
Mountaineering
Practice Guidelines as Topic
Rescue Work - standards
Abstract
Determination of death requires specific knowledge, training, and experience in most cases. It can be particularly difficult when external conditions, such as objective hazards in mountains, prevent close physical examination of an apparently lifeless person, or when examination cannot be accomplished by an authorized person. Guidelines exist, but proper use can be difficult. In addition to the absence of vital signs, definitive signs of death must be present. Recognition of definitive signs of death can be problematic due to the variability in time course and the possibility of mimics. Only clear criteria such as decapitation or detruncation should be used to determine death from a distance or by laypersons who are not medically trained. To present criteria that allow for accurate determination of death in mountain rescue situations, the International Commission for Mountain Emergency Medicine convened a panel of mountain rescue doctors and a forensic pathologist. These recommendations are based on a nonsystematic review of the literature including articles on determination of death and related topics.
PubMed ID
33077333 View in PubMed
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Nanobody interaction unveils structure, dynamics and proteotoxicity of the Finnish-type amyloidogenic gelsolin variant.

https://arctichealth.org/en/permalink/ahliterature297443
Source
Biochim Biophys Acta Mol Basis Dis. 2019 Mar 01; 1865(3):648-660
Publication Type
Journal Article
Date
Mar-01-2019
Author
Toni Giorgino
Davide Mattioni
Amal Hassan
Mario Milani
Eloise Mastrangelo
Alberto Barbiroli
Adriaan Verhelle
Jan Gettemans
Maria Monica Barzago
Luisa Diomede
Matteo de Rosa
Author Affiliation
Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Milano, Italy; Dipartimento di Bioscienze, Università degli Studi di Milano, Milano, Italy.
Source
Biochim Biophys Acta Mol Basis Dis. 2019 Mar 01; 1865(3):648-660
Date
Mar-01-2019
Language
English
Publication Type
Journal Article
Abstract
AGel amyloidosis, formerly known as familial amyloidosis of the Finnish-type, is caused by pathological aggregation of proteolytic fragments of plasma gelsolin. So far, four mutations in the gelsolin gene have been reported as responsible for the disease. Although D187N is the first identified variant and the best characterized, its structure has been hitherto elusive. Exploiting a recently-developed nanobody targeting gelsolin, we were able to stabilize the G2 domain of the D187N protein and obtained, for the first time, its high-resolution crystal structure. In the nanobody-stabilized conformation, the main effect of the D187N substitution is the impairment of the calcium binding capability, leading to a destabilization of the C-terminal tail of G2. However, molecular dynamics simulations show that in the absence of the nanobody, D187N-mutated G2 further misfolds, ultimately exposing its hydrophobic core and the furin cleavage site. The nanobody's protective effect is based on the enhancement of the thermodynamic stability of different G2 mutants (D187N, G167R and N184K). In particular, the nanobody reduces the flexibility of dynamic stretches, and most notably decreases the conformational entropy of the C-terminal tail, otherwise stabilized by the presence of the Ca2+ ion. A Caenorhabditis elegans-based assay was also applied to quantify the proteotoxic potential of the mutants and determine whether nanobody stabilization translates into a biologically relevant effect. Successful protection from G2 toxicity in vivo points to the use of C. elegans as a tool for investigating the mechanisms underlying AGel amyloidosis and rapidly screen new therapeutics.
PubMed ID
30625383 View in PubMed
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