2014
DOI: 10.3109/13506129.2014.964858
|View full text |Cite
|
Sign up to set email alerts
|

Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1

Citation Types

1
373
0
13

Year Published

2015
2015
2020
2020

Publication Types

Select...
8
2

Relationship

1
9

Authors

Journals

citations
Cited by 462 publications
(387 citation statements)
references
References 14 publications
1
373
0
13
Order By: Relevance
“…The designations ATTRwt and ATTRm amyloidosis may be used for WT and hereditary ATTR amyloidosis, respectively. This chemically based nomenclature has been adopted by the World Health Organization [9] and consistently recommended by the ISA Nomenclature Committee (reviewed in reference [10]). It is of utmost importance to use the chemically based nomenclature, e.g.…”
Section: Amyloidosis Nomenclaturementioning
confidence: 99%
“…The designations ATTRwt and ATTRm amyloidosis may be used for WT and hereditary ATTR amyloidosis, respectively. This chemically based nomenclature has been adopted by the World Health Organization [9] and consistently recommended by the ISA Nomenclature Committee (reviewed in reference [10]). It is of utmost importance to use the chemically based nomenclature, e.g.…”
Section: Amyloidosis Nomenclaturementioning
confidence: 99%
“…Amyloid deposits characteristically stain with Congo red and show anomalous color change (so-called applegreen birefringence) when examined under polarized light. Thirty-one precursor proteins of amyloid have been identified so far (1). Amyloidosis can be systemic or localized.…”
Section: Introductionmentioning
confidence: 99%
“…The dominant secondary structure is a cross-␤ structure stabilized by an ordered hydrogen bond network. Although they were found to be associated with Ͼ30 types of amyloidoses, including dialysis-related amyloidosis caused by ␤ 2 -microglobulin (␤2m) 4 (4), various proteins not associated with diseases have also been shown to form amyloid fibrils, indicating that amyloid fibrillation is a generic property of denatured proteins (1). Previous studies proposed that amyloid fibrils formed in the supersaturated solutions of precursor proteins through a nucleation and growth mechanism that was characterized by a lag phase or via seed-dependent growth without a lag phase (5-7).…”
mentioning
confidence: 99%