2017
DOI: 10.1016/j.aaf.2017.03.005
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Hic74, a novel alanine and glycine rich matrix protein related to nacreous layer formation in the mollusc Hyriopsis cumingii

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Cited by 13 publications
(6 citation statements)
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“…This protein was also securely identified in all of the freshwater unionoid reference shells (coverage varying from 34% in M. margaritifera , supported by 67 peptides, to 50% in U. crassus, supported by 203 peptides). Hic74 is an acidic, Ala- and Gly-rich shell matrix protein (Liu et al, 2017a). Consisting of 19 poly-A blocks, GA repeats, short acidic motifs (that probably bind to the mineral) and a GS-rich domain at the C-terminus (which resembles that of lustrin-A), this silk fibroin-like protein is likely to play a structural role in nacre formation and in enhancing its mechanical properties (Liu et al, 2017a).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…This protein was also securely identified in all of the freshwater unionoid reference shells (coverage varying from 34% in M. margaritifera , supported by 67 peptides, to 50% in U. crassus, supported by 203 peptides). Hic74 is an acidic, Ala- and Gly-rich shell matrix protein (Liu et al, 2017a). Consisting of 19 poly-A blocks, GA repeats, short acidic motifs (that probably bind to the mineral) and a GS-rich domain at the C-terminus (which resembles that of lustrin-A), this silk fibroin-like protein is likely to play a structural role in nacre formation and in enhancing its mechanical properties (Liu et al, 2017a).…”
Section: Resultsmentioning
confidence: 99%
“…Hic74 (GenBank: ARG42316.1) is an acidic (IP 4.68), alanine and glycine rich matrix protein, supposedly involved in nacreous layer formation (Liu et al, 2017a). Its structure consists of poly-alanine blocks (at least 17) with short acidic motifs, a ‘GS loop’ type coil structure of lustrin A (Wustman et al, 2002) at the C-terminus, the C-terminal 30 residues of which consist of short acidic-basic motifs.…”
Section: ​1​ Archaeological Sites and Double-buttonsmentioning
confidence: 99%
“…Furthermore, we identified one marker peak (m/z 1570.8), that likely corresponds to a peptide shared by the two Unionida shells (freshwater bivalves) Unio pictorum (family Unionidae) and Pseudunio auricularius (family Margaritiferidae). We suggest that the peptide at m/ z 1570.8 (Table 2) belongs to protein Hic74 [64], which was found to be the dominant protein in unionoid shells [16]. The peak can be assigned to peptide sequence EAD(-18.01)DLALLSLLFGGR and it was previously identified by LC-MS/MS analyses.…”
Section: The Application Of "Palaeoshellomics": Shell Pmfsmentioning
confidence: 76%
“…Meanwhile, Webster et al (1999) reported that compounding animal and plant protein sources with additional amino acid profiles may enhance the possibility of nutrient inadequacy that could adversely affect fish growth. Fishmeal is successfully substituted with other vegetable protein sources in fish feeds, there is some concern that the current evaluations of essential amino acid requirements are unsatisfactory goal (Furuya et al, 2004), Some AAs may also turn into a limiting factor and thus need to be supplemented in feed for important species of fish (El-Sayed, 2014;Liu et al, 2017).…”
Section: Introductionmentioning
confidence: 99%