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Alan S. Cohen

Statens Serum Institut

ORCID: 0009-0005-4099-9271

Publishes on Amyloidosis: Diagnosis, Treatment, Outcomes, Alzheimer's disease research and treatments, Parathyroid Disorders and Treatments. 362 papers and 33k citations.

362Publications
33kTotal Citations

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Top publicationsby citations

The 1982 revised criteria for the classification of systemic lupus erythematosus
Eng M. Tan, Alan S. Cohen, James F. Fries et al.|Arthritis & Rheumatism|1982
Cited by 14.6k

The 1971 preliminary criteria for the classification of systemic lupus erythematosus (SLE) were revised and updated to incorporate new immunologic knowledge and improve disease classification. The 1982 revised criteria include fluorescence antinuclear antibody and antibody to native DNA and Sm antigen. Some criteria involving the same organ systems were aggregated into single criteria. Raynaud's phenomenon and alopecia were not included in the 1982 revised criteria because of low sensitivity and specificity. The new criteria were 96% sensitive and 96% specific when tested with SLE and control patient data gathered from 18 participating clinics. When compared with the 1971 criteria, the 1982 revised criteria showed gains in sensitivity and specificity.

HIGH-RESOLUTION ELECTRON MICROSCOPIC ANALYSIS OF THE AMYLOID FIBRIL
Tsuranobu Shirahama, Alan S. Cohen|The Journal of Cell Biology|1967
Cited by 385Open Access

The ultrastructural organization of the fibrous component of amyloid has been analyzed by means of high resolution electron microscopy of negatively stained isolated amyloid fibrils and of positively stained amyloid fibrils in thin tissue sections. It was found that a number of subunits could be resolved according to their dimensions. The following structural organization is proposed. The amyloid fibril, the fibrous component of amyloid as seen in electron microscopy of thin tissue sections, consists of a number of filaments aggregated side-by-side. These amyloid filaments are approximately 75-80 A in diameter and consist of five (or less likely six) subunits (amyloid protofibrils) which are arranged parallel to each other, longitudinal or slightly oblique to the long axis of the filament. The filament has often seemed to disperse into several longitudinal rows. The amyloid protofibril is about 25-35 A wide and appears to consist of two or three subunit strands helically arranged with a 35-50-A repeat (or, less likely, is composed of globular subunits aggregated end-to-end). These amyloid subprotofibrillar strands measure approximately 10-15 A in diameter.