The Human Factor: Algorithms, Dissenters, and Detention in Immigration Enforcement

2019 ◽  
Author(s):  
Robert Koulish ◽  
Ernesto F. Calvo
Keyword(s):  
Human Factor ◽  
Immigration Enforcement

The Human Factor: Algorithms, Dissenters, and Detention in Immigration Enforcement

2021 ◽  
Author(s):  
Robert Koulish ◽  
Ernesto Calvo
Keyword(s):  
Human Factor ◽  
Immigration Enforcement

An Application of the HFACS Method to Aviation Accidents in Africa

2016 ◽  
Vol 6 (1) ◽  
pp. 33-38 ◽  
Author(s):  
Isaac Munene
Keyword(s):  
Human Factors ◽  
Physical Environment ◽  
Human Factor ◽  
Flight Training ◽  
African Countries ◽  
Causal Factors ◽  
Aviation Accidents ◽  
Factors Analysis ◽  
Adverse Weather ◽  
Decision Errors

Abstract. The Human Factors Analysis and Classification System (HFACS) methodology was applied to accident reports from three African countries: Kenya, Nigeria, and South Africa. In all, 55 of 72 finalized reports for accidents occurring between 2000 and 2014 were analyzed. In most of the accidents, one or more human factors contributed to the accident. Skill-based errors (56.4%), the physical environment (36.4%), and violations (20%) were the most common causal factors in the accidents. Decision errors comprised 18.2%, while perceptual errors and crew resource management accounted for 10.9%. The results were consistent with previous industry observations: Over 70% of aviation accidents have human factor causes. Adverse weather was seen to be a common secondary casual factor. Changes in flight training and risk management methods may alleviate the high number of accidents in Africa.

Review of Flightdeck Performance: The Human Factor.

1991 ◽  
Vol 36 (8) ◽  
pp. 730-730
Author(s):  
No authorship indicated
Keyword(s):  
Human Factor

THE HUMAN FACTOR IN ARMY AVIATION.

1967 ◽  
Author(s):  
WALLACE W. PROPHET
Keyword(s):  
Human Factor

Using cognitive work analysis techniques to identify human factor hazards

2010 ◽  
Author(s):  
M. E. Hassall ◽  
P. M. Sanderson ◽  
I. T. Cameron
Keyword(s):  
Human Factor ◽  
Cognitive Work Analysis ◽  
Work Analysis ◽  
Analysis Techniques ◽  
Cognitive Work

The Human Factor in Safe Transportation, Another Mad Patent Bill, and more

1913 ◽  
Vol 108 (18) ◽  
pp. 392-393
Keyword(s):  
Human Factor

Considering the human factor

1987 ◽  
Vol 66 (1) ◽  
pp. 11
Keyword(s):  
Human Factor

Characterization of Monoclonal Anti-human Factor VII Antibody (B101/B1) that Recognized Three-dimensional Structures near Arg at Position 79 in the First EGF-like Domain

1998 ◽  
Vol 79 (01) ◽  
pp. 104-109 ◽  
Author(s):  
Osamu Takamiya
Keyword(s):  
Monoclonal Antibodies ◽  
Tissue Factor ◽  
Human Factor ◽  
Solid Phase ◽  
Three Dimensional ◽  
Coagulation Factors ◽  
Factor Vii ◽  
Dimensional Structure ◽  
Epidermal Growth

SummaryMurine monoclonal antibodies (designated hVII-B101/B1, hVIIDC2/D4 and hVII-DC6/3D8) directed against human factor VII (FVII) were prepared and characterized, with more extensive characterization of hVII-B101/B1 that did not bind reduced FVIIa. The immunoglobulin of the three monoclonal antibodies consisted of IgG1. These antibodies did not inhibit procoagulant activities of other vitamin K-dependent coagulation factors except FVII and did not cross-react with proteins in the immunoblotting test. hVII-DC2/D4 recognized the light chain after reduction of FVIIa with 2-mercaptoethanol, and hVIIDC6/3D8 the heavy chain. hVII-B101/B1 bound FVII without Ca2+, and possessed stronger affinity for FVII in the presence of Ca2+. The Kd for hVII-B101/B1 to FVII was 1.75 x 10–10 M in the presence of 5 mM CaCl2. The antibody inhibited the binding of FVII to tissue factor in the presence of Ca2+. hVII-B101/B1 also inhibited the activation of FX by the complex of FVIIa and tissue factor in the presence of Ca2+. Furthermore, immunoblotting revealed that hVII-B101/B1 reacted with non-reduced γ-carboxyglutaminic acid (Gla)-domainless-FVII and/or FVIIa. hVII-B101/B1 showed a similar pattern to that of non-reduced proteolytic fragments of FVII by trypsin with hVII-DC2/D4 on immunoblotting test. hVII-B101/B1 reacted differently with the FVII from the dysfunctional FVII variant, FVII Shinjo, which has a substitution of Gln for Arg at residue 79 in the first epidermal growth factor (1st EGF)-like domain (Takamiya O, et al. Haemosta 25, 89-97,1995) compared with normal FVII, when used as a solid phase-antibody for ELISA by the sandwich method. hVII-B101/B1 did not react with a series of short peptide sequences near position 79 in the first EGF-like domain on the solid-phase support for epitope scanning. These results suggested that the specific epitope of the antibody, hVII-B101/B1, was located in the three-dimensional structure near position 79 in the first EGF-like domain of human FVII.

Sign in / Sign up

Export Citation Format

Share Document