ACS Publications. Most Trusted. Most Cited. Most Read
My Activity

Oligosaccharide Binding Characteristics of the Molecular Chaperones Calnexin and Calreticulin

View Author Information
Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2S2, Canada, and Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9041
Cite this: Biochemistry 1998, 37, 10, 3480–3490
Publication Date (Web):February 18, 1998
Copyright © 1998 American Chemical Society

    Article Views





    Other access options


    Calnexin and calreticulin are homologous molecular chaperones of the endoplasmic reticulum. Their binding to newly synthesized glycoproteins is mediated, at least in part, by a lectin site that recognizes the early N-linked oligosaccharide processing intermediate, Glc1Man9GlcNAc2. We compared the oligosaccharide binding specificities of calnexin and calreticulin in an effort to determine the basis for reported differences in their association with various glycoproteins. Using mono-, di-, and oligosaccharides to inhibit the binding of Glc1Man9GlcNAc2 to calreticulin and to a truncated, soluble form of calnexin, we show that the entire Glcα1−3Manα1−2Manα1−2Man structure, extending from the α1−3 branch point of the oligosaccharide core, is recognized by both proteins. Furthermore, analysis of the binding of monoglucosylated oligosaccharides containing progressively fewer mannose residues suggests that for both proteins the α1−6 mannose branch point of the oligosaccharide core is also essential for recognition. Consistent with their essentially identical substrate specificities, calnexin and calreticulin exhibited the same relative affinities when competing for binding to the Glc1Man9GlcNAc2 oligosaccharide. Thus, differential glycoprotein binding cannot be attributed to differences in the lectin specificities or binding affinities of calnexin and calreticulin. We also examined the effects of ATP, calcium, and disulfide reduction on the lectin properties of calnexin and calreticulin. Whereas oligosaccharide binding was only slightly enhanced for both proteins in the presence of high concentrations of a number of adenosine nucleotides, removal of bound calcium abrogated oligosaccharide binding, an effect that was largely reversible upon readdition of calcium. Disulfide reduction had no effect on oligosaccharide binding by calnexin, but binding by calreticulin was inhibited by 70%. Finally, deletion mutagenesis of calnexin and calreticulin identified a central proline-rich region characterized by two tandem repeat motifs as a segment capable of binding oligosaccharide. This segment bears no sequence homology to the carbohydrate recognition domains of other lectins.

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.


    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

     This work was supported by grants from the National Cancer Institute of Canada with funds from the Canadian Cancer society (to D.B.W.), from the Medical Research Council of Canada (to M.M.), and from the NIH (Grant GM38545) and the Welch Foundation (Grant I-1168) (to M.A.L.). A.V. is the recipient of a Steve Fonyo Studentship from the National Cancer Institute of Canada. M.M. is a Medical Research Council of Canada Scientist and Senior Scholar of the Alberta Heritage Foundation for Medical Research.

     University of Toronto.


     University of Alberta.

     University of Texas Southwestern Medical Center.


     To whom correspondence should be addressed:  Department of Biochemistry, Medical Sciences Building, University of Toronto, Toronto, Ontario M5S 1A8, Canada. Tel (416) 978-2546; Fax (416) 978-8548; e-mail [email protected].

    Cited By

    This article is cited by 204 publications.

    1. Tyler J. Bechtel, Chun Li, Eleni A. Kisty, Aaron J. Maurais, Eranthie Weerapana. Profiling Cysteine Reactivity and Oxidation in the Endoplasmic Reticulum. ACS Chemical Biology 2020, 15 (2) , 543-553.
    2. Vignesh Kotian, Deepaneeta Sarmah, Harpreet Kaur, Radhika Kesharwani, Geetesh Verma, Leela Mounica, Pabbala Veeresh, Kiran Kalia, Anupom Borah, Xin Wang, Kunjan R. Dave, Dileep R. Yavagal, Pallab Bhattacharya. Evolving Evidence of Calreticulin as a Pharmacological Target in Neurological Disorders. ACS Chemical Neuroscience 2019, 10 (6) , 2629-2646.
    3. Justin T. Marinko, Hui Huang, Wesley D. Penn, John A. Capra, Jonathan P. Schlebach, Charles R. Sanders. Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis. Chemical Reviews 2019, 119 (9) , 5537-5606.
    4. Ianina L. Conte,, Natasha Keith,, Clara Gutiérrez-González,, Armando J. Parodi, and, Julio J. Caramelo. The Interplay between Calcium and the in Vitro Lectin and Chaperone Activities of Calreticulin. Biochemistry 2007, 46 (15) , 4671-4680.
    5. Achim Brockmeier and, David B. Williams. Potent Lectin-Independent Chaperone Function of Calnexin under Conditions Prevalent within the Lumen of the Endoplasmic Reticulum. Biochemistry 2006, 45 (42) , 12906-12916.
    6. Jürgen Roth. Protein N-Glycosylation along the Secretory Pathway:  Relationship to Organelle Topography and Function, Protein Quality Control, and Cell Interactions. Chemical Reviews 2002, 102 (2) , 285-304.
    7. Norica Branza-Nichita,, Andrei J. Petrescu,, Gabriela Negroiu,, Raymond A. Dwek, and, Stefana M. Petrescu. N-Glycosylation Processing and Glycoprotein Folding−Lessons from the Tyrosinase-Related Proteins. Chemical Reviews 2000, 100 (12) , 4697-4712.
    8. Stacey M. Arnold,, Liselotte I. Fessler,, John H. Fessler, and, Randal J. Kaufman. Two Homologues Encoding Human UDP-Glucose:Glycoprotein Glucosyltransferase Differ in mRNA Expression and Enzymatic Activity. Biochemistry 2000, 39 (9) , 2149-2163.
    9. David Eisner, Erwin Neher, Holger Taschenberger, Godfrey Smith. Physiology of intracellular calcium buffering. Physiological Reviews 2023, 103 (4) , 2767-2845.
    10. Savita Bansal, Meenakshi Vachher, Archana Burman. Calreticulin: a quintessential multifaceted protein with therapeutic potential. Journal of Proteins and Proteomics 2023, 14 (3) , 187-200.
    11. Valentina Wong-Benito, Jill de Rijke, Brian Dixon. Antigen presentation in vertebrates: Structural and functional aspects. Developmental & Comparative Immunology 2023, 144 , 104702.
    12. Diego Esperante, Ana Flisser, Fela Mendlovic. The many faces of parasite calreticulin. Frontiers in Immunology 2023, 14
    13. Ashalatha Sreshty Mamidi, Avadhesha Surolia, . Mixed mechanism of conformational selection and induced fit as a molecular recognition process in the calreticulin family of proteins. PLOS Computational Biology 2022, 18 (12) , e1010661.
    14. Xiaojing Liang, Jiansheng Xie, Hao Liu, Rongjie Zhao, Wei Zhang, Haidong Wang, Hongming Pan, Yubin Zhou, Weidong Han. STIM1 Deficiency In Intestinal Epithelium Attenuates Colonic Inflammation and Tumorigenesis by Reducing ER Stress of Goblet Cells. Cellular and Molecular Gastroenterology and Hepatology 2022, 14 (1) , 193-217.
    15. F. Tudor Ilca, Louise H. Boyle. The glycosylation status of MHC class I molecules impacts their interactions with TAPBPR. Molecular Immunology 2021, 139 , 168-176.
    16. Hannah T. Perkins, Viki Allan. Intertwined and Finely Balanced: Endoplasmic Reticulum Morphology, Dynamics, Function, and Diseases. Cells 2021, 10 (9) , 2341.
    17. Ana P. Kutschat, Steven A. Johnsen, Feda H. Hamdan. Store-Operated Calcium Entry: Shaping the Transcriptional and Epigenetic Landscape in Pancreatic Cancer. Cells 2021, 10 (5) , 966.
    18. Cansu Doğan, Sabine Hänniger, David G. Heckel, Cathy Coutu, Dwayne D. Hegedus, Linda Crubaugh, Russell L. Groves, Şerife Bayram, Umut Toprak. Two calcium‐binding chaperones from the fat body of the Colorado potato beetle, Leptinotarsa decemlineata (Coleoptera: Chrysomelidae) involved in diapause. Archives of Insect Biochemistry and Physiology 2021, 106 (1)
    19. Benjamin M. Adams, Nathan P. Canniff, Kevin P. Guay, Daniel N. Hebert. The Role of Endoplasmic Reticulum Chaperones in Protein Folding and Quality Control. 2021, 27-50.
    20. Tadashi Suzuki, Haruhiko Fujihira. Folding and Quality Control of Glycoproteins. 2021, 1-28.
    21. Xiaoxue Yin, Hairong Wu, Liangliang Mu, Kailiang Han, Heyi Xu, Jichang Jian, Anli Wang, Jianmin Ye. Identification and characterization of calreticulin (CRT) from Nile tilapia (Oreochromis niloticus) in response to bacterial infection. Aquaculture 2020, 529 , 735706.
    22. Ning Jiang, Yanfeng Xiao, Yuesheng Liu, Weihua Liu, Shanxi Liu. Blood coagulation factor VIII D1241E polymorphism leads to a weak malectin interaction and reduction of factor VIII posttranslational modification and secretion. Experimental Cell Research 2020, 397 (1) , 112334.
    23. Xin-Yu Guo, Yi-Shi Liu, Xiao-Dong Gao, Taroh Kinoshita, Morihisa Fujita. Calnexin mediates the maturation of GPI-anchors through ER retention. Journal of Biological Chemistry 2020, 295 (48) , 16393-16410.
    24. Guennadi Kozlov, Kalle Gehring. Calnexin cycle – structural features of the ER chaperone system. The FEBS Journal 2020, 287 (20) , 4322-4340.
    25. Simon Trowitzsch, Robert Tampé. Multifunctional Chaperone and Quality Control Complexes in Adaptive Immunity. Annual Review of Biophysics 2020, 49 (1) , 135-161.
    26. Arum Han, Chen Li, Tara Zahed, Michael Wong, Ian Smith, Karl Hoedel, Douglas Green, Alexander D. Boiko, . Calreticulin is a Critical Cell Survival Factor in Malignant Neoplasms. PLOS Biology 2019, 17 (9) , e3000402.
    27. Yixin Ding, Jinlei Tang, Xun You, Xiongfeng Zhang, Guangliang Wang, Congying Yao, Mibin Lin, Xuerui Wang, Dai Cheng. Study on the mechanism underlying Al-induced hepatotoxicity based on the identification of the Al-binding proteins in liver. Metallomics 2019, 11 (8) , 1353-1362.
    28. Benjamin M. Adams, Michela E. Oster, Daniel N. Hebert. Protein Quality Control in the Endoplasmic Reticulum. The Protein Journal 2019, 38 (3) , 317-329.
    29. Mingye Feng, Kristopher D. Marjon, Fangfang Zhu, Rachel Weissman-Tsukamoto, Aaron Levett, Katie Sullivan, Kevin S. Kao, Maxim Markovic, Paul A. Bump, Hannah M. Jackson, Timothy S. Choi, Jing Chen, Allison M. Banuelos, Jie Liu, Phung Gip, Lei Cheng, Denong Wang, Irving L. Weissman. Programmed cell removal by calreticulin in tissue homeostasis and cancer. Nature Communications 2018, 9 (1)
    30. Yueh-Chien Lin, Chien-Chin Chen, Wei-Min Chen, Kuan-Ying Lu, Tang-Long Shen, Yeong-Chin Jou, Cheng-Huang Shen, Norihiko Ohbayashi, Yasunori Kanaho, Yuan-Li Huang, Hsinyu Lee. LPA1/3 signaling mediates tumor lymphangiogenesis through promoting CRT expression in prostate cancer. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 2018, 1863 (10) , 1305-1315.
    31. Simon Trowitzsch, Robert Tampé. ABC Transporters in Dynamic Macromolecular Assemblies. Journal of Molecular Biology 2018, 430 (22) , 4481-4495.
    32. Pucharee Songprakhon, Thawornchai Limjindaporn, Guey Chuen Perng, Chunya Puttikhunt, Thanawat Thaingtamtanha, Thanyaporn Dechtawewat, Sawanan Saitornuang, Chairat Uthaipibull, Sissades Thongsima, Pa-thai Yenchitsomanus, Prida Malasit, Sansanee Noisakran. Human glucose-regulated protein 78 modulates intracellular production and secretion of nonstructural protein 1 of dengue virus. Journal of General Virology 2018, 99 (10) , 1391-1406.
    33. Dajun Zhao, Pan Feng, Yang Sun, Zhigang Qin, Zhengbin Zhang, Yanzhen Tan, Erhe Gao, Wayne Bond Lau, Xinliang Ma, Jian Yang, Shiqiang Yu, Xuezeng Xu, Dinghua Yi, Wei Yi. Cardiac-derived CTRP9 protects against myocardial ischemia/reperfusion injury via calreticulin-dependent inhibition of apoptosis. Cell Death & Disease 2018, 9 (7)
    34. Richard Strasser. Protein Quality Control in the Endoplasmic Reticulum of Plants. Annual Review of Plant Biology 2018, 69 (1) , 147-172.
    35. Anna Rita Migliaccio, Vladimir N. Uversky. Dissecting physical structure of calreticulin, an intrinsically disordered Ca 2+ -buffering chaperone from endoplasmic reticulum. Journal of Biomolecular Structure and Dynamics 2018, 36 (6) , 1617-1636.
    36. Rama Bansil, Bradley S. Turner. The biology of mucus: Composition, synthesis and organization. Advanced Drug Delivery Reviews 2018, 124 , 3-15.
    37. Jürgen Roth, Christian Zuber. Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9. Histochemistry and Cell Biology 2017, 147 (2) , 269-284.
    38. Maryam Sarwat, Narendra Tuteja. Role of Plant Calreticulins in Calcium Signaling. 2017, 135-150.
    39. Lothar Jennes, Alfredo Ulloa-Aguirre, Jo Ann Janovick, P. Michael Conn. The Gonadotropin-Releasing Hormone and Its Receptor. 2017, 363-378.
    40. Irene De Almeida, Nidia M.M. Oliveira, Rebecca A. Randall, Caroline S. Hill, John M. McCoy, Claudio D. Stern. Calreticulin is a secreted BMP antagonist, expressed in Hensen's node during neural induction. Developmental Biology 2017, 421 (2) , 161-170.
    41. Guanghua Wang, Zengjie Jiang, Min Zhang, Ning Yang, Dongfa Zhu. Identification of a new calreticulin homolog from Yesso scallop ( Patinopecten yessoensis ) and its role in innate immunity. Fish & Shellfish Immunology 2016, 58 , 108-115.
    42. Lydia Lamriben, Jill B. Graham, Benjamin M. Adams, Daniel N. Hebert. N ‐Glycan‐based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle. Traffic 2016, 17 (4) , 308-326.
    43. Bruno Di Jeso, Peter Arvan. Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology. Endocrine Reviews 2016, 37 (1) , 2-36.
    44. Lili Wen, Fan Han, Yuxiu Shi. Changes in the Glucocorticoid Receptor and Ca2+/Calreticulin-Dependent Signalling Pathway in the Medial Prefrontal Cortex of Rats with Post-traumatic Stress Disorder. Journal of Molecular Neuroscience 2015, 56 (1) , 24-34.
    45. Abla Tannous, Giorgia Brambilla Pisoni, Daniel N. Hebert, Maurizio Molinari. N-linked sugar-regulated protein folding and quality control in the ER. Seminars in Cell & Developmental Biology 2015, 41 , 79-89.
    46. Yi-Chien Lu, Wen-Chin Weng, Hsinyu Lee. Functional Roles of Calreticulin in Cancer Biology. BioMed Research International 2015, 2015 , 1-9.
    47. Michisato Okudera, Takahiro Gojoubori, Ichiro Tsujino, Masatake Asano. Effect of ionomycin on interaction of calnexin with vesicular stomatitis virus glycoprotein is cell type-specific. Journal of Oral Science 2015, 57 (4) , 305-312.
    48. Hsing-Hui Li, Zi-Yu Huang, Shih-Png Ye, Chi-Yu Lu, Pai-Chiao Cheng, Shu-Hwa Chen, Chii-Shiarng Chen, . Membrane Labeling of Coral Gastrodermal Cells by Biotinylation: The Proteomic Identification of Surface Proteins Involving Cnidaria-Dinoflagellate Endosymbiosis. PLoS ONE 2014, 9 (1) , e85119.
    49. Shaista P. Nisar, Marie Lordkipanidzé, Matthew L. Jones, Ban B. Dawood, Sherina Murden, Margaret R. Cunningham, Andrew D. Mumford, Jonathan T. Wilde, Steve P. Watson, Stuart J. Mundell, Gillian C. Lowe, . A novel thromboxane A2 receptor N42S variant results in reduced surface expression and platelet dysfunction. Thrombosis and Haemostasis 2014, 112 (05) , 923-932.
    50. Tengteng Zhang, Yun Xia, Lijuan Zhang, Wanrong Bao, Chao Hong, Xiao-Ming Gao. CD1dhiCD5+ B cells differentiate into antibody-secreting cells under the stimulation with calreticulin fragment. Protein & Cell 2013, 4 (11) , 872-881.
    51. Tali Gidalevitz, Fred Stevens, Yair Argon. Orchestration of secretory protein folding by ER chaperones. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2013, 1833 (11) , 2410-2424.
    52. Chao Hong, Tengteng Zhang, Xiao-Ming Gao. Recombinant murine calreticulin fragment 39-272 expands CD1dhiCD5+ IL-10-secreting B cells that modulate experimental autoimmune encephalomyelitis in C57BL/6 mice. Molecular Immunology 2013, 55 (3-4) , 237-246.
    53. Joo Hee Lee, Eun Jeong Kwon, Do Han Kim. Calumenin has a role in the alleviation of ER stress in neonatal rat cardiomyocytes. Biochemical and Biophysical Research Communications 2013, 439 (3) , 327-332.
    54. Xuemei Liu, Na Xu, Shicui Zhang. Calreticulin is a microbial-binding molecule with phagocytosis-enhancing capacity. Fish & Shellfish Immunology 2013, 35 (3) , 776-784.
    55. Shang-Hui Huang, Li-Xiang Zhao, Chao Hong, Cui-Cui Duo, Bing-Nan Guo, Li-Juan Zhang, Zheng Gong, Si-Dong Xiong, Fang-Yuan Gong, Xiao-Ming Gao, . Self-Oligomerization Is Essential for Enhanced Immunological Activities of Soluble Recombinant Calreticulin. PLoS ONE 2013, 8 (6) , e64951.
    56. Wei-Fan Chiang, Tzer-Zen Hwang, Tzyh-Chyuan Hour, Lee-Hsin Wang, Chien-Chih Chiu, Hau-Ren Chen, Yu-Jen Wu, Chih-Chun Wang, Ling-Feng Wang, Chen-Yu Chien, Jen-Hao Chen, Chao-Tien Hsu, Jeff Yi-Fu Chen. Calreticulin, an endoplasmic reticulum-resident protein, is highly expressed and essential for cell proliferation and migration in oral squamous cell carcinoma. Oral Oncology 2013, 49 (6) , 534-541.
    57. Wei-Ji Li, Kai Long, Hong-Liang Dong, Xiao-Ming Gao. Adjuvanticity of a Recombinant Calreticulin Fragment in Assisting Anti-β-Glucan IgG Responses in T Cell-Deficient Mice. Clinical and Vaccine Immunology 2013, 20 (4) , 582-589.
    58. Xiang Qiu, Chao Hong, Zhaoyan Zhong, Yue Li, Tengteng Zhang, Wanrong Bao, Sidong Xiong, Xiao‐Ming Gao. Modulation of cellular immunity by antibodies against calreticulin. European Journal of Immunology 2012, 42 (9) , 2419-2430.
    59. G. S. Gupta. Lectins in Quality Control: Calnexin and Calreticulin. 2012, 29-56.
    60. Tim Vervliet, Santeri Kiviluoto, Geert Bultynck. ER Stress and UPR Through Dysregulated ER Ca2+ Homeostasis and Signaling. 2012, 107-142.
    61. Deborah L. Segaloff. Regulatory Processes Governing the Cell Surface Expression of LH and FSH Receptors. 2012, 113-129.
    62. C. Z. F. Costa, S. E. A. da Rosa, M. M. de Camargo. The Unfolded Protein Response: How Protein Folding Became a Restrictive Aspect for Innate Immunity and B Lymphocytes 1. Scandinavian Journal of Immunology 2011, 73 (5) , 436-448.
    63. Lori A Rutkevich, David B Williams. Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum. Current Opinion in Cell Biology 2011, 23 (2) , 157-166.
    64. Guennadi Kozlov, Cosmin L. Pocanschi, Angelika Rosenauer, Sara Bastos-Aristizabal, Alexei Gorelik, David B. Williams, Kalle Gehring. Structural Basis of Carbohydrate Recognition by Calreticulin. Journal of Biological Chemistry 2010, 285 (49) , 38612-38620.
    65. Chao Hong, Xiang Qiu, Yue Li, Qianrong Huang, Zhaoyan Zhong, Yan Zhang, Xiangyuan Liu, Lin Sun, Ping Lv, Xiao-Ming Gao. Functional Analysis of Recombinant Calreticulin Fragment 39–272: Implications for Immunobiological Activities of Calreticulin in Health and Disease. The Journal of Immunology 2010, 185 (8) , 4561-4569.
    66. Sian T. Patterson, Reinhart A.F. Reithmeier. Cell Surface Rescue of Kidney Anion Exchanger 1 Mutants by Disruption of Chaperone Interactions. Journal of Biological Chemistry 2010, 285 (43) , 33423-33434.
    67. Daniel C. Chapman, David B. Williams. ER quality control in the biogenesis of MHC class I molecules. Seminars in Cell & Developmental Biology 2010, 21 (5) , 512-519.
    68. Bradley R. Pearse, Daniel N. Hebert. Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2010, 1803 (6) , 684-693.
    69. Changzhen Liu, Hongmei Fu, Barry Flutter, Simon J. Powis, Bin Gao. Suppression of MHC class I surface expression by calreticulin's P-domain in a calreticulin deficient cell line. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2010, 1803 (5) , 544-552.
    70. Ana María Villamil Giraldo, Máximo Lopez Medus, Mariano Gonzalez Lebrero, Rodrigo S. Pagano, Carlos A. Labriola, Lucas Landolfo, José M. Delfino, Armando J. Parodi, Julio J. Caramelo. The Structure of Calreticulin C-terminal Domain Is Modulated by Physiological Variations of Calcium Concentration. Journal of Biological Chemistry 2010, 285 (7) , 4544-4553.
    71. Christopher Howe, Malgorzata Garstka, Mohammed Al-Balushi, Esther Ghanem, Antony N Antoniou, Susanne Fritzsche, Gytis Jankevicius, Nasia Kontouli, Clemens Schneeweiss, Anthony Williams, Tim Elliott, Sebastian Springer. Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules. The EMBO Journal 2009, 28 (23) , 3730-3744.
    72. Julie G. Donaldson, David B. Williams. Intracellular Assembly and Trafficking of MHC Class I Molecules. Traffic 2009, 10 (12) , 1745-1752.
    73. Richard C. Austin. The Unfolded Protein Response in Health and Disease. Antioxidants & Redox Signaling 2009, 11 (9) , 2279-2287.
    74. Mahesh Alur, Minh M. Nguyen, Scott E. Eggener, Feng Jiang, Soheil S. Dadras, Jeffrey Stern, Simon Kimm, Kim Roehl, James Kozlowski, Michael Pins, Marek Michalak, Rajiv Dhir, Zhou Wang. Suppressive Roles of Calreticulin in Prostate Cancer Growth and Metastasis. The American Journal of Pathology 2009, 175 (2) , 882-890.
    75. Daming Chen, Young Bong Choi, Gordon Sandford, John Nicholas. Determinants of Secretion and Intracellular Localization of Human Herpesvirus 8 Interleukin-6. Journal of Virology 2009, 83 (13) , 6874-6882.
    76. Sian T. Patterson, Jing Li, Jeong-Ah Kang, Amittha Wickrema, David B. Williams, Reinhart A.F. Reithmeier. Loss of Specific Chaperones Involved in Membrane Glycoprotein Biosynthesis during the Maturation of Human Erythroid Progenitor Cells. Journal of Biological Chemistry 2009, 284 (21) , 14547-14557.
    77. Marek Michalak, Jody Groenendyk, Eva Szabo, Leslie I. Gold, Michal Opas. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochemical Journal 2009, 417 (3) , 651-666.
    78. L. Jennes, A. Ulloa-Aguirre, J.A. Janovick, V.V. Adjan, P.M. Conn. The Gonadotropin-Releasing Hormone and Its Receptor. 2009, 1645-1669.
    79. Katrine Nørgaard Toft, Nanna Larsen, Flemming Steen Jørgensen, Peter Højrup, Gunnar Houen, Bente Vestergaard. Small angle X-ray scattering study of calreticulin reveals conformational plasticity. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2008, 1784 (9) , 1265-1270.
    80. Cornelius F.H. Mueller, Kerstin Wassmann, Anja Berger, Stefan Holz, Sven Wassmann, Georg Nickenig. Differential phosphorylation of calreticulin affects AT1 receptor mRNA stability in VSMC. Biochemical and Biophysical Research Communications 2008, 370 (4) , 669-674.
    81. A. Higashino, S. Yonezawa, T. Kageyama. Establishment of an ELISA system for the determination of Japanese monkey calreticulin and its application to plasma samples in macaques. Journal of Medical Primatology 2008, 37 (2) , 93-100.
    82. Julio J. Caramelo, Armando J. Parodi. How sugars convey information on protein conformation in the endoplasmic reticulum. Seminars in Cell & Developmental Biology 2007, 18 (6) , 732-742.
    83. Atsushi Tatami, Yung-Son Hon, Ichiro Matsuo, Maki Takatani, Hiroyuki Koshino, Yukishige Ito. Analyses of carbohydrate binding property of lectin-chaperone calreticulin. Biochemical and Biophysical Research Communications 2007, 364 (2) , 332-337.
    84. Song Ling, Xiujun Pi, Joseph Holoshitz. The Rheumatoid Arthritis Shared Epitope Triggers Innate Immune Signaling via Cell Surface Calreticulin. The Journal of Immunology 2007, 179 (9) , 6359-6367.
    85. Daisuke Yamaguchi, Norihito Kawasaki, Ichiro Matsuo, Kiichiro Totani, Hideto Tozawa, Naoki Matsumoto, Yukishige Ito, Kazuo Yamamoto. VIPL has sugar-binding activity specific for high-mannose-type N-glycans, and glucosylation of the α1,2 mannotriosyl branch blocks its binding. Glycobiology 2007, 17 (10) , 1061-1069.
    86. P. Michael Conn, Alfredo Ulloa-Aguirre, Joel Ito, Jo Ann Janovick. G Protein-Coupled Receptor Trafficking in Health and Disease: Lessons Learned to Prepare for Therapeutic Mutant Rescue in Vivo. Pharmacological Reviews 2007, 59 (3) , 225-250.
    87. Chhanda Biswas, Olga Ostrovsky, Catherine A. Makarewich, Sherry Wanderling, Tali Gidalevitz, Yair Argon. The peptide-binding activity of GRP94 is regulated by calcium. Biochemical Journal 2007, 405 (2) , 233-241.
    88. James N. Arnold, Mark R. Wormald, Robert B. Sim, Pauline M. Rudd, Raymond A. Dwek. The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins. Annual Review of Immunology 2007, 25 (1) , 21-50.
    89. T. Suzuki, K. Tanabe, Y. Funakoshi. Folding and Quality Control of Glycoproteins. 2007, 129-149.
    90. Bradley R. Pearse, Daniel N. Hebert. Calnexin, Calreticulin, and Their Associated Oxidoreductase ERp57. 2007, 275-305.
    91. Taisuke WATANABE, Ichiro MATSUO, Jun-ichi MARUYAMA, Katsuhiko KITAMOTO, Yukishige ITO. Identification and Characterization of an Intracellular Lectin, Calnexin, from Aspergillus oryzae Using N-Glycan-Conjugated Beads. Bioscience, Biotechnology, and Biochemistry 2007, 71 (11) , 2688-2696.
    92. Tadashi Satoh, Ken Sato, Akira Kanoh, Katsuko Yamashita, Yusuke Yamada, Noriyuki Igarashi, Ryuichi Kato, Akihiko Nakano, Soichi Wakatsuki. Structures of the Carbohydrate Recognition Domain of Ca2+-independent Cargo Receptors Emp46p and Emp47p. Journal of Biological Chemistry 2006, 281 (15) , 10410-10419.
    93. Kanta Yanagida, Shunji Natsuka, Sumihiro Hase. Structural diversity of cytosolic free oligosaccharides in the human hepatoma cell line, HepG2. Glycobiology 2006, 16 (4) , 294-304.
    94. David B. Williams. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. Journal of Cell Science 2006, 119 (4) , 615-623.
    95. Staffan Persson, Jeff Harper. The ER and Cell Calcium. 2006, 251-278.
    96. M. A. Blanco-Gelaz, B. Suárez-Alvarez, Segundo González, A. López-Vázquez, J. Martínez-Borra, Carlos López-Larrea. The amino acid at position 97 is involved in folding and surface expression of HLA-B27. International Immunology 2006, 18 (1) , 211-220.
    97. Yukiko Kamiya, Yoshiki Yamaguchi, Noriko Takahashi, Yoichiro Arata, Ken-ichi Kasai, Yoshito Ihara, Ichiro Matsuo, Yukishige Ito, Kazuo Yamamoto, Koichi Kato. Sugar-binding Properties of VIP36, an Intracellular Animal Lectin Operating as a Cargo Receptor. Journal of Biological Chemistry 2005, 280 (44) , 37178-37182.
    98. Tae Won Goo, Soojung Park, Byung Rae Jin, Eun Young Yun, Iksoo Kim, Si-kab Nho, Seok-Woo Kang, O-Yu Kwon. Endoplasmic Reticulum Stress Response of Bombyx Mori Calreticulin. Molecular Biology Reports 2005, 32 (3) , 133-139.
    99. Vilasack Thammavongsa, Laura Mancino, Malini Raghavan. Polypeptide Substrate Recognition by Calnexin Requires Specific Conformations of the Calnexin Protein. Journal of Biological Chemistry 2005, 280 (39) , 33497-33505.
    100. Michel Pieren, Carmela Galli, Angela Denzel, Maurizio Molinari. The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins. Journal of Biological Chemistry 2005, 280 (31) , 28265-28271.
    Load more citations

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Your Mendeley pairing has expired. Please reconnect