N-glycosylation Triggers a Dual Selection Pressure in Eukaryotic Secretory Proteins

[1]  B. Schulz,et al.  N-glycoprotein macroheterogeneity: biological implications and proteomic characterization , 2016, Glycoconjugate Journal.

[2]  Qinglian Liu,et al.  Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP. , 2015, Structure.

[3]  J. Caramelo,et al.  A sweet code for glycoprotein folding , 2015, FEBS letters.

[4]  G. Lederkremer,et al.  Glycan regulation of ER-associated degradation through compartmentalization. , 2015, Seminars in cell & developmental biology.

[5]  R. Gilmore,et al.  Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum. , 2015, Seminars in cell & developmental biology.

[6]  J. Kelly,et al.  The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis. , 2014, Nature chemical biology.

[7]  C. Sevier,et al.  Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress , 2014, eLife.

[8]  J. Brodsky,et al.  The BiP Molecular Chaperone Plays Multiple Roles during the Biogenesis of TorsinA, an AAA+ ATPase Associated with the Neurological Disease Early-onset Torsion Dystonia* , 2014, The Journal of Biological Chemistry.

[9]  Ryan K. Schott,et al.  Encoding Asymmetry of the N-Glycosylation Motif Facilitates Glycoprotein Evolution , 2014, PloS one.

[10]  T. Gidalevitz,et al.  Orchestration of secretory protein folding by ER chaperones. , 2013, Biochimica et biophysica acta.

[11]  D. Hebert,et al.  Protein folding in the endoplasmic reticulum. , 2013, Cold Spring Harbor perspectives in biology.

[12]  R. Gilmore,et al.  Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST , 2013, The Journal of cell biology.

[13]  D. Pincus,et al.  Endoplasmic reticulum stress sensing in the unfolded protein response. , 2013, Cold Spring Harbor perspectives in biology.

[14]  Roman Kityk,et al.  Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. , 2012, Molecular cell.

[15]  H. Freeze,et al.  A sensitive green fluorescent protein biomarker of N‐glycosylation site occupancy , 2012, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[16]  M. Molinari,et al.  Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis , 2012, Trends in Biochemical Sciences.

[17]  M. Taura,et al.  STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein. , 2012, Molecular cell.

[18]  Jianzhi Zhang,et al.  Genome-wide evolutionary conservation of N-glycosylation sites. , 2011, Molecular biology and evolution.

[19]  Markus Aebi,et al.  Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation , 2011, Journal of Inherited Metabolic Disease.

[20]  J. Weissman,et al.  J Domain Co-chaperone Specificity Defines the Role of BiP during Protein Translocation* , 2010, The Journal of Biological Chemistry.

[21]  Y. Levy,et al.  Folding of glycoproteins: toward understanding the biophysics of the glycosylation code. , 2009, Current opinion in structural biology.

[22]  Cameron V. Jennings,et al.  Suggestive Evidence for Darwinian Selection against Asparagine-Linked Glycans of Plasmodium falciparum and Toxoplasma gondii , 2009, Eukaryotic Cell.

[23]  Temple F. Smith,et al.  Darwinian selection for sites of Asn-linked glycosylation in phylogenetically disparate eukaryotes and viruses , 2009, Proceedings of the National Academy of Sciences.

[24]  R. Glockshuber,et al.  Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency , 2009, Proceedings of the National Academy of Sciences.

[25]  M. Aebi,et al.  Analysis of Glycosylation Site Occupancy Reveals a Role for Ost3p and Ost6p in Site-specific N-Glycosylation Efficiency*S , 2009, Molecular & Cellular Proteomics.

[26]  S. Brunak,et al.  Locating proteins in the cell using TargetP, SignalP and related tools , 2007, Nature Protocols.

[27]  D. Kelleher,et al.  An evolving view of the eukaryotic oligosaccharyltransferase. , 2006, Glycobiology.

[28]  Avadhesha Surolia,et al.  N-linked oligosaccharides as outfitters for glycoprotein folding, form and function. , 2006, Trends in biochemical sciences.

[29]  Guillaume Vogt,et al.  Gains of glycosylation comprise an unexpectedly large group of pathogenic mutations , 2005, Nature Genetics.

[30]  V. Herzog,et al.  Misfolded BiP is degraded by a proteasome-independent endoplasmic-reticulum-associated degradation pathway. , 2005, The Biochemical journal.

[31]  Conrad C. Huang,et al.  UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..

[32]  Raymond A Dwek,et al.  Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding. , 2003, Glycobiology.

[33]  Kenji Kohno,et al.  Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. , 2003, Molecular biology of the cell.

[34]  R Apweiler,et al.  On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. , 1999, Biochimica et biophysica acta.

[35]  B. Imperiali,et al.  Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. , 1999, Current opinion in chemical biology.

[36]  L. Kasturi,et al.  The amino acid following an asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency. , 1998, Biochemistry.

[37]  J. Winther,et al.  Competition between folding and glycosylation in the endoplasmic reticulum. , 1996, The EMBO journal.

[38]  L. Kasturi,et al.  The Amino Acid at the X Position of an Asn-X-Ser Sequon Is an Important Determinant of N-Linked Core-glycosylation Efficiency (*) , 1996, The Journal of Biological Chemistry.

[39]  R. Young,et al.  Epitope tagging of the human endoplasmic reticulum HSP70 protein, BiP, to facilitate analysis of BiP--substrate interactions. , 1995, Analytical biochemistry.

[40]  James R. Eshleman,et al.  The Hydroxy Amino Acid in an Asn-X-Ser/Thr Sequon Can Influence N-Linked Core Glycosylation Efficiency and the Level of Expression of a Cell Surface Glycoprotein (*) , 1995, The Journal of Biological Chemistry.

[41]  T. Blundell,et al.  Comparative protein modelling by satisfaction of spatial restraints. , 1993, Journal of molecular biology.

[42]  S. W. Lin,et al.  Characterization of genetic defects of hemophilia A in patients of Chinese origin. , 1993, Genomics.

[43]  T. Sugimura,et al.  A simple and rapid method for generating a deletion by PCR. , 1991, Nucleic acids research.

[44]  S. Ho,et al.  Site-directed mutagenesis by overlap extension using the polymerase chain reaction. , 1989, Gene.

[45]  D. Carrington,et al.  Polypeptide ligation occurs during post-translational modification of concanavalin A , 1985, Nature.

[46]  B. Schulz Beyond the Sequon: Sites of N-Glycosylation , 2012 .

[47]  B. Poorthuis,et al.  Identification of 31 novel mutations in the N‐acetylgalactosamine‐6‐sulfatase gene reveals excessive allelic heterogeneity among patients with Morquio A syndrome , 1997, Human mutation.