scholarly journals Egg Coat Proteins Activate Ca2+ Entry into Mouse Sperm via CATSPER Channels

2009 ◽  
Vol 96 (3) ◽  
pp. 183a-184a
Author(s):  
Jingsheng Xia ◽  
Dejian Ren
Keyword(s):  
Coat Proteins ◽  
Mouse Sperm ◽  
Egg Coat

scholarly journals Duplicate Abalone Egg Coat Proteins Bind Sperm Lysin Similarly, but Evolve Oppositely, Consistent with Molecular Mimicry at Fertilization

PLoS Genetics ◽  
2013 ◽  
Vol 9 (2) ◽  
pp. e1003287 ◽  
Author(s):  
Jan E. Aagaard ◽  
Stevan A. Springer ◽  
Scott D. Soelberg ◽  
Willie J. Swanson
Keyword(s):  
Molecular Mimicry ◽  
Coat Proteins ◽  
Egg Coat

Structure of clathrin cages and coats in ice

1986 ◽  
Vol 44 ◽  
pp. 94-97
Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse
Keyword(s):  
Electron Microscopy ◽  
Heavy Chain ◽  
Outer Part ◽  
Coated Vesicles ◽  
Eukaryotic Cells ◽  
Coat Proteins ◽  
Terminal Domain ◽  
Clathrin Heavy Chain ◽  
Membrane Components

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.

Regulation of lipid droplet coat proteins in adipocytes in relation to insulin resistance

2013 ◽  
Author(s):  
Maria M Malagon ◽  
Yoana Rabanal-Ruiz ◽  
Rocio Guzman-Ruiz ◽  
Alberto Diaz-Ruiz ◽  
Andres Travez ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Lipid Droplet ◽  
Coat Proteins

TRPM8 in mouse sperm detects temperature changes and may influence the acrosome reaction

2011 ◽  
Vol 226 (6) ◽  
pp. 1620-1631 ◽  
Author(s):  
Pablo Martínez-López ◽  
Claudia L. Treviño ◽  
José Luis de la Vega-Beltrán ◽  
Gerardo De Blas ◽  
Esteban Monroy ◽  
...  
Keyword(s):  
Acrosome Reaction ◽  
Temperature Changes ◽  
Mouse Sperm

scholarly journals Comparison of Monoclonal Gammopathies Linked to Poliovirus or Coxsackievirus vs. Other Infectious Pathogens

Cells ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 438
Author(s):  
Jean Harb ◽  
Nicolas Mennesson ◽  
Cassandra Lepetit ◽  
Maeva Fourny ◽  
Margaux Louvois ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
B Cell ◽  
Monoclonal Gammopathy ◽  
Coat Proteins ◽  
Chronic Stimulation ◽  
B Cell Epitopes ◽  
Monoclonal Immunoglobulins ◽  
Self Antigen ◽  
Coxsackievirus B1 ◽  
Undetermined Significance

Chronic stimulation by infectious pathogens or self-antigen glucosylsphingosine (GlcSph) can lead to monoclonal gammopathy of undetermined significance (MGUS) and multiple myeloma (MM). Novel assays such as the multiplex infectious antigen microarray (MIAA) and GlcSph assays, permit identification of targets for >60% purified monoclonal immunoglobulins (Igs). Searching for additional targets, we selected 28 purified monoclonal Igs whose antigen was not represented on the MIAA and GlcSph assays; their specificity of recognition was then analyzed using microarrays consisting of 3760 B-cell epitopes from 196 pathogens. The peptide sequences PALTAVETG and PALTAAETG of the VP1 coat proteins of human poliovirus 1/3 and coxsackievirus B1/B3, respectively, were specifically recognized by 6/28 monoclonal Igs. Re-analysis of patient cohorts showed that purified monoclonal Igs from 10/155 MGUS/SM (6.5%) and 3/147 MM (2.0%) bound to the PALTAVETG or PALTAAETG epitopes. Altogether, PALTAV/AETG-initiated MGUS are not rare and few seem to evolve toward myeloma.

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