scholarly journals Species-Specific Functional Regions of the Green Alga Gamete Fusion Protein HAP2 Revealed by Structural Studies

2018 ◽  
Author(s):  
Eduard Baquero-Salazar ◽  
Juliette Fedry ◽  
Pierre Legrand ◽  
Thomas Krey ◽  
Felix Rey
Keyword(s):  
Fusion Protein ◽  
Green Alga ◽  
Structural Studies ◽  
Gamete Fusion ◽  
Functional Regions ◽  
Species Specific

scholarly journals Species-Specific Functional Regions of the Green Alga Gamete Fusion Protein HAP2 Revealed by Structural Studies

Structure ◽  
2019 ◽  
Vol 27 (1) ◽  
pp. 113-124.e4 ◽  
Author(s):  
Eduard Baquero ◽  
Juliette Fedry ◽  
Pierre Legrand ◽  
Thomas Krey ◽  
Felix A. Rey
Keyword(s):  
Fusion Protein ◽  
Green Alga ◽  
Structural Studies ◽  
Gamete Fusion ◽  
Functional Regions ◽  
Species Specific

scholarly journals Functional analysis and purification of a Pen-2 fusion protein for γ-secretase structural studies

2014 ◽  
Vol 131 (1) ◽  
pp. 94-100
Author(s):  
Oliver Holmes ◽  
Swetha Paturi ◽  
Michael S. Wolfe ◽  
Dennis J. Selkoe
Keyword(s):  
Functional Analysis ◽  
Fusion Protein ◽  
Structural Studies

Structural studies of a glucan isolated from blue-green alga Spirulina platensis

1989 ◽  
Vol 31 (2) ◽  
pp. 85-91 ◽  
Author(s):  
K.Madhavi Sekharam ◽  
L.V. Venkataraman ◽  
P.V. Salimath
Keyword(s):  
Green Alga ◽  
Spirulina Platensis ◽  
Structural Studies ◽  
Blue Green Alga

scholarly journals Progress of sperm IZUMO1 relocation during spontaneous acrosome reaction

Reproduction ◽  
2014 ◽  
Vol 147 (2) ◽  
pp. 231-240 ◽  
Author(s):  
Natasa Sebkova ◽  
Lukas Ded ◽  
Katerina Vesela ◽  
Katerina Dvorakova-Hortova
Keyword(s):  
Fusion Protein ◽  
Acrosome Reaction ◽  
Mating Behaviour ◽  
Calcium Ionophore ◽  
Cumulus Cells ◽  
Sperm Head ◽  
High Rate ◽  
Field Mice ◽  
Species Specific

It has been recently shown in mice that sperm undergo acrosome reaction (AR) by passing through cumulus cells; furthermore, the acrosome-reacted sperm can bind to zona pellucida and consequently fertilise the egg. During AR, the relocation of the primary fusion protein IZUMO1 into the equatorial segment is crucial for sperm–egg fusion. There is a high rate of spontaneous AR in rodents, with up to 60% in promiscuous species. The aim of this study was to clarify whether the IZUMO1 relocation in sperm after spontaneous and induced AR is the same, and whether there is a correlation between the speed of IZUMO1 relocation and species-specific mating behaviour in field mice. Immunofluorescent detection of IZUMO1 dynamics during the in vitro capacitation, spontaneous, calcium ionophore and progesterone-induced AR was monitored. Our results show that during spontaneous AR, there is a clear IZUMO1 relocation from the acrosomal cap to the equatorial segment, and further over the whole sperm head. In addition, there is positive tail tyrosine phosphorylation (TyrP) associated with hyperactive motility. Moreover, the beginning and the progress of IZUMO1 relocation and tail TyrP positively correlate with the level of promiscuity and the acrosome instability in promiscuous species. The findings that crucial molecular changes essential for sperm–egg fusion represented by dynamic movements of IZUMO1 also happen during spontaneous AR are vital for understanding fertilisation in mice.

scholarly journals Structural Studies of β-Carbonic Anhydrase from the Green Alga Coccomyxa: Inhibitor Complexes with Anions and Acetazolamide

PLoS ONE ◽  
2011 ◽  
Vol 6 (12) ◽  
pp. e28458 ◽  
Author(s):  
Shenghua Huang ◽  
Tobias Hainzl ◽  
Christin Grundström ◽  
Cecilia Forsman ◽  
Göran Samuelsson ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Green Alga ◽  
Structural Studies

scholarly journals Monoclonal antibodies specific for the C-terminus of the laminin B2 subunit. Evidence for glycosylation differences between murine and human laminin

1991 ◽  
Vol 277 (3) ◽  
pp. 593-596
Author(s):  
J C Brown ◽  
J H Spragg ◽  
P W Taylor
Keyword(s):  
Amino Acids ◽  
Monoclonal Antibodies ◽  
Fusion Protein ◽  
Adult Mouse ◽  
Yolk Sac ◽  
Specific Difference ◽  
C Terminus ◽  
Mouse Tissues ◽  
Species Specific ◽  
Beta Galactosidase

We have raised a panel of monoclonal antibodies against a beta-galactosidase fusion protein (XLB2.1) containing the C-terminal 153 amino acids of the murine laminin B2 subunit. Five of the nine antibodies characterized recognize human placental laminin as well as murine Engelbreth-Holm-Swarm (EHS)-tumour laminin. Only two of the antibodies recognize both rat parietal-yolk-sac laminin and murine EHS-tumour laminin. Two antibodies recognize an epitope on the human laminin B2 subunit which is masked by N-linked oligosaccharide in murine EHS-tumour laminin. These antibodies also fail to bind to laminin from adult-mouse tissues. These results demonstrate a species-specific difference in the glycosylation of the laminin B2 subunit.

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