Johan C Sunryd
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    Explore the profile of Johan C Sunryd including associated specialties, affiliations and a list of published articles.
          
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              Articles
              5
            
            
              Citations
              173
            
            
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  Recent Articles
          1.
        
    
    Graham J, Sunryd J, Mathavan K, Weir E, Larsen I, Halim A, et al.
  
  
    Mol Biol Cell
    . 2019 Dec;
          31(3):167-183.
    
    PMID: 31851597
  
  
          Protein glycosylation plays essential roles in protein structure, stability, and activity such as cell adhesion. The cadherin superfamily of adhesion molecules carry O-linked mannose glycans at conserved sites and it...
      
2.
        
    
    Sunryd J, Cheon B, Graham J, Giorda K, Fissore R, Hebert D
  
  
    J Biol Chem
    . 2014 Apr;
          289(23):16085-99.
    
    PMID: 24764305
  
  
          The endoplasmic reticulum (ER) is organized in part by adapter proteins that nucleate the formation of large protein complexes. Tetratricopeptide repeats (TPR) are well studied protein structural motifs that support...
      
3.
        
    
    Tamura T, Sunryd J, Hebert D
  
  
    Mol Membr Biol
    . 2010 Jun;
          27(8):412-27.
    
    PMID: 20553226
  
  
          The endoplasmic reticulum (ER) is a highly organized and specialized organelle optimized for the production of proteins. It is comprised of a highly interconnected network of tubules that contain a...
      
4.
        
    
    Pearse B, Tamura T, Sunryd J, Grabowski G, Kaufman R, Hebert D
  
  
    J Cell Biol
    . 2010 May;
          189(5):829-41.
    
    PMID: 20498017
  
  
          An endoplasmic reticulum (ER) quality control system assists in efficient folding and disposal of misfolded proteins. N-linked glycans are critical in these events because their composition dictates interactions with molecular...
      
5.
        
    
    Cormier J, Tamura T, Sunryd J, Hebert D
  
  
    Mol Cell
    . 2009 Jun;
          34(5):627-33.
    
    PMID: 19524542
  
  
          Terminally misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently cleared by the ER-associated degradation (ERAD) pathway. The degradation of ERAD substrates involves mannose trimming...