The degradation of intracrystalline mollusc shell proteins: A proteomics study of Spondylus gaederopus

2021 ◽  
Vol 1869 (12) ◽  
pp. 140718
Author(s):  
Jorune Sakalauskaite ◽  
Meaghan Mackie ◽  
Alberto J. Taurozzi ◽  
Matthew J. Collins ◽  
Frédéric Marin ◽  
...  
2011 ◽  
Vol 72 (5-6) ◽  
pp. 531-546 ◽  
Author(s):  
Benjamin Marie ◽  
Nathalie Le Roy ◽  
Isabelle Zanella-Cléon ◽  
Michel Becchi ◽  
Frédéric Marin

Nature ◽  
1996 ◽  
Vol 381 (6577) ◽  
pp. 56-58 ◽  
Author(s):  
A. M. Belcher ◽  
X. H. Wu ◽  
R. J. Christensen ◽  
P. K. Hansma ◽  
G. D. Stucky ◽  
...  

Author(s):  
Z. Hong Zhou ◽  
Jing He ◽  
Joanita Jakana ◽  
J. D. Tatman ◽  
Frazer J. Rixon ◽  
...  

Herpes simplex virus-1 (HSV-1) is a ubiquitous virus which is implicated in diseases ranging from self-curing cold sores to life-threatening infections. The 2500 Å diameter herpes virion is composed of a glycoprotein spike containing, lipid envelope, enclosing a protein layer (the tegument) in which is embedded the capsid (which contains the dsDNA genome). The B-, and A- and C-capsids, representing different morphogenetic stages in HSV-1 infected cells, are composed of 7, and 5 structural proteins respectively. The three capsid types are organized in similar T=16 icosahedral shells with 12 pentons, 150 hexons, and 320 connecting triplexes. Our previous 3D structure study at 26 Å revealed domain features of all these structural components and suggested probable locations for the outer shell proteins, VP5, VP26, VP19c and VP23. VP5 makes up most of both pentons and hexons. VP26 appeared to bind to the VP5 subunit in hexon but not to that in penton.


2015 ◽  
Vol 122 (03) ◽  
Author(s):  
B Engelmann ◽  
J Bischof ◽  
AL Dirk ◽  
N Friedrich ◽  
E Hammer ◽  
...  

Oceanologia ◽  
2020 ◽  
Author(s):  
Konstantinos Tsolakos ◽  
George Katselis ◽  
John A. Theodorou
Keyword(s):  

ACS Omega ◽  
2021 ◽  
Author(s):  
Liu-Lin Xiong ◽  
Lu-Lu Xue ◽  
Yan-Jun Chen ◽  
Ruo-Lan Du ◽  
Qian Wang ◽  
...  

2017 ◽  
Vol 16 (9) ◽  
pp. 3470-3475 ◽  
Author(s):  
Ming-Zhi Zhu ◽  
Na Li ◽  
Yi-Tong Wang ◽  
Ning Liu ◽  
Ming-Quan Guo ◽  
...  

1994 ◽  
Vol 41 (3) ◽  
pp. 289-297 ◽  
Author(s):  
June E. Mirecki ◽  
Barry B. Miller

AbstractAmino acid epimeric (aIle/Ile) values from terrestrial molluscs are used to define and correlate three aminozones in loess sequences exposed across the central Mississippi Valley, in Arkansas and Tennessee. Three superposed aminozones are defined at Wittsburg quarry, Arkansas, primarily using aIle/Ile values from total hydrolysates of the gastropod genus Hendersonia: Peoria Loess (aIle/Ile = 0.07 ± 0.01), Roxana Silt (0.14 ± 0.02), and a third loess (0.28 ± 0.06). Loess units at Wittsburg quarry can be correlated on lithologic characteristics eastward across the Mississippi Valley to the Old River section, near Memphis, Tennessee; however, only one loess unit is fossil-bearing (Peoria Loess, aIle/Ile = 0.05) at that section. Radiocarbon analyses of charcoal from the upper Roxana Silt (ca. 26,000 to 29,000 yr old) and mollusc shell carbonate from the basal Roxana Silt (ca. 39,000 yr old) are used to calibrate amino acid epimeric data for the central Mississippi Valley. These data, applied to the apparent parabolic kinetic model of R. M. Mitterer and N. Kriausakul (1989, Quaternary Science Reviews 8, 353-357), suggest an Illinoian (>120,000 yr) age for the third loess in the central Mississippi Valley that is correlative with part of the Loveland Loess in Illinois and Iowa.


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