Braakman Lab – Publications

*# equal contribution

Lars Ellgaard, Nicholas McCaul, Anna Chatsisvili, Ineke Braakman. Co- and Post-Translational Protein Folding in the ER. Traffic (2016) 17(6).
Pubmed | DOI | PDF

Jevtov I, Zacharogianni M, van Oorschot MM, van Zadelhoff G, Aguilera-Gomez A, Vuillez I, Braakman I, Hafen E, Stocker H, Rabouille C. TORC2 mediates the heat stress response in Drosophila by promoting the formation of stress granules. J Cell Sci 2015 128.
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Li, X., M.M. van Oers, J.M. Vlak, I. Braakman. Folding of influenza virus hemagglutinin in insect cells is fast and efficient. J. Biotech (2015) in press
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Mathys*, L., K.O. François*, M. Quandte, I. Braakman, J. Balzarini. Deletion of the Highly Conserved N-Glycan at Asn260 of HIV-1 gp120 Affects Folding and Lysosomal Degradation of gp120, and Results in Loss of Viral Infectivity. PLOS One (2014) 9(6): e10118.
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Koritzinsky, M., T. van den Beucken, F. Levitin, R. Rumantir, N.J. Harding, K.C. Chu, P.C. Boutros, I. Braakman, B.G. Wouters. Oxygen is required for post-translational disulfide bond formation in mammalian cells. J. Cell Biol. (2013) 203(4).
Comment: Short, B. A call for oxygen in the ER. J. Cell Biol. (2013) 203(4).
Comment: Baumann, K. Protein folding: A late need for oxygen. Nat Rev Mol Cell Biol (2014) 15(5).
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Hansen, R.E., M. Otsu, I. Braakman, J.R. Winther. Quantifying changes in the cellular thiol-disulfide status during differentiation of B cells into antibody-secreting plasma cells. Intl. J Cell Biol. (2013) Article ID 898563.
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Oka, O.B.V., M.A. Pringle, I.M. Schopp, I. Braakman, N.J. Bulleid. ERdj5 is the ER Reductase that Catalyses the Removal of Non-Native Disulfides and Correct Folding of the LDL-Receptor. Mol. Cell (2013) 50(6).
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Kleizen, B., I. Braakman. A sweet send-off. Science (2013) 340(6135)
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Braakman, I., D.N. Hebert. Protein folding in the endoplasmic reticulum. Cold Spring Harb Perspect Biol. (Endoplasmic Reticulum. Ed. S. Ferro-Novick, T. Rapoport, R. Schekman), (2013) May 1; 5(5).
Pubmed | DOI | PDF

Tabak , H.F., A. Van der Zand, I. Braakman. Peroxisome formation and maintenance are dependent on the endoplasmic reticulum. Annu. Rev. Biochem. (2013) 82.
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Benham, A.M., M. van Lith, R. Sitia, I. Braakman. Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum. Philos. Trans. R. Soc. Lond. B. Biol. Sci. (2013) 368 (1617).
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Van der Zand, A., J. Gent, I. Braakman*, H.F. Tabak*. Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes. Cell (2012) 149(2).
Comment: Schuldt, A. When two become one. Nat Rev Mol Cell Biol. (2012) 13(6): 337.
Comment: Goodman, C. Cell biology: Peroxisomes come together. Nature Chem. Biol. 8: 503.
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Peters, K.W., T. Okiyoneda, W.E. Balch, I. Braakman, J.L. Brodsky, W.B. Guggino, C.M. Penland, H.B. Pollard, E.J. Sorscher, W.R. Skach, P.J. Thomas, G.L. Lukacs, R.A. Frizzell. CFTR Folding Consortium: methods available for studies of CFTR folding and correction. Methods Mol Biol. (2011) 742.
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Braakman, I., N. Bulleid. Cellular Protein Folding and Modification in the Endoplasmic Reticulum. Annu. Rev. Biochem. (2011) 80.
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*Hoelen, H., *B. Kleizen, A. Schmidt, J. Richardson, P. Charitou, P.J. Thomas, I. Braakman. The primary folding defect and rescue of ∆F508 CFTR emerge during translation of the mutant domain. PLoS ONE (2010) 5(11).
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Van der Zand, A., I. Braakman*, H.F. Tabak*. Peroxisomal membrane proteins insert into the endoplasmic reticulum. Mol. Biol. Cell (2010) 21(12).
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Balch, W.E., I. Braakman, R. Frizzell, W. Guggino, G. Lukacs, C. Penland, W. Skach, E. Sorscher, P. Thomas, H. Pollard. The Folding Biology of Cystic Fibrosis: a Consortium-based Approach to Disease. In: Protein Misfolding Diseases: Current and Emerging Principles and Therapies. Ramirez-Alvarado, M., Kelly, J.W., Dobson, C.M. (Eds.). John Wiley & Sons, Inc., Wiley-Blackwell Division, Hoboken, NJ (2010) Chapter 20.
DOI | PDF

Pena*, F., A. Jansens*, G. van Zadelhoff, I. Braakman. Calcium as a crucial cofactor for low density lipoprotein receptor folding in the ER. J. Biol. Chem. (2010) 285.
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Christis, C., A. Fullaondo, D. Schildknegt, S. Mkrtchian, A.J.R. Heck., I. Braakman. Regulated increase in folding capacity prevents unfolded protein stress in the ER. J. Cell Sci. (2010) 123.
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Van Anken*, E., F. Pena*, N. Hafkemeijer, C. Christis, E.P. Romijn, U. Grauschopf, V.M.J. Oorschot, T. Pertel, S. Engels, A. Ora, V. Lăstun, R. Glockshuber, J. Klumperman, A.J.R. Heck, J. Luban, I. Braakman. Efficient IgM assembly and secretion require the plasma cell induced ER protein pERp1. Proc. Natl. Acad. Sci. (2009) 106(40).
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Braakman, I. Entering a new era with Ero. Nature Rev Mol. Cell Biol. (2009) 10(8).
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Bontjer, I., A. Land, D. Eggink, E. Verkade, K. Tuin, C. Baldwin, G. Pollakis, W.A. Paxton, I. Braakman, B. Berkhout, R.W. Sanders. Optimization of human immunodeficiency virus type 1 envelope glycoproteins with V1/V2 deleted, using virus evolution. J. Virol. (2009) 83(1).
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Sanders*, R.W., S.-T. Hsu*, E. van Anken*, I.M. Liscaljet, M. Dankers, I. Bontjer, A. Land, I. Braakman, A.M. Bonvin, B. Berkhout. Evolution rescues folding of HIV-1 Envelope glycoprotein gp120 lacking a conserved disulfide bond. Mol. Biol. Cell (2008) 19(11).
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Christis, C., N.H. Lubsen, I. Braakman. Protein folding includes oligomerization: examples from the ER and cytosol. FEBS J. (2008) 275(19): 4700-4727.
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Braakman, I., M. Otsu. Cargo load reduction. Science (2008) 321(5888).
DOI

Van Anken*, E., R.W. Sanders*, I.M. Liscaljet*, A. Land, I. Bontjer, S. Tillemans, A.A. Nabatov, W.A. Paxton, B. Berkhout, I. Braakman. Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein. Mol. Biol. Cell (2008) 19(10).
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Tabak, H.F., A. van der Zand, I. Braakman. Peroxisomes: minted by the ER. Curr. Opin. Cell Biol. (2008) 20(4).
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Sanders, R.W., E. Van Anken, A.A. Nabatov, I.M. Liscaljet, I. Bontjer, D. Eggink, M. Melchers, E. Busser, M.M. Dankers, F. Groot, I. Braakman, B. Berkhout, W.A. Paxton. The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion. Retrovirology (2008) 5(1).
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Tabak, H.F., D. Hoepfner, A. Van der Zand, H.J. Geuze, I. Braakman, M.A. Huynen. Formation of peroxisomes: present and past. Biochim. Biophys. Acta (2006) 1763.
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Piersma, D., E.M.J.J. Berns, M. Verhoef-Post, M.P. Look, J.G.M Klijn, A.G. Uitterlinden, I. Braakman, H.A.P. Pols, A.P.N. Themmen. A common polymorphism renders the Luteinizing Hormone receptor protein more active by improving signal peptide function and predicts adverse outcome in breast cancer patients. J. Clin. Endocrinol. Metab. (2006) 91.
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Van der Zand, A., I. Braakman, H.J. Geuze, H.F. Tabak. The return of the peroxisome. J. Cell Sci. (2006) 119.
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De Jonge, W., H.F. Tabak, I. Braakman. Chaperone proteins and peroxisomal protein import. Topics in Current Genetics (2006) 16.
PDF

Kleizen, B., T. van Vlijmen, H. de Jonge, I. Braakman. CFTR folds predominantly co-translational. Mol. Cell. (2005) 20.
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Van Anken, E., I. Braakman. Endoplasmic reticulum stress and the making of a professional secretory cell. Crit. Rev. Biochem. Mol. Biol. (2005) 40 (5).
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Van Anken, E., I. Braakman. Versatility of the endoplasmic reticulum protein folding factory. Crit. Rev. Biochem. Mol. Biol. (2005) 40 (4).
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Romijn*, E.P., C. Christis*, M. Wieffer, J.W. Gouw, A. Fullaondo, P. van der Sluijs, I. Braakman, A.J.R. Heck. Expression clustering reveals detailed coexpression patterns of functionally related proteins during B cell differentiation. A proteomic study using a combination of one-dimensional gel electrophoresis, LC-MS/MS and stable isotope labeling by amino acids in cell culture (SILAC). Mol. Cell. Proteomics (2005) 131(4).
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Hoepfner, D., D. Schildknegt, I. Braakman, P. Philippsen, Tabak H.F. Contribution of the endoplasmic reticulum to peroxisome formation. Cell (2005) 122 (1).
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Comment: Schekman, R. Peroxisomes: another branch of the secretory pathway? Cell (2005) 122.
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Comment: Kunau, W.H. Peroxisome biogenesis: end of the debate. Curr Biol. (2005) 15(18).
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Maggioni, M.C., I.M. Liscaljet, I. Braakman. A critical step in the folding of influenza virus HA, determined with a novel folding assay. Nat. Struct. Mol. Biol. (2005) 12.
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Liscaljet, I.M., B. Kleizen, I. Braakman. Studying protein folding in vivo. Handbook of protein folding. (2005) Part II, Volume 1, Chapter 3: 73-104 (Eds Buchner, J. & Kiefhaber, T.).
DOI

Maggioni, C., I. Braakman. Synthesis and quality control of viral membrane proteins. Curr Topics Microbiol. Immunol. (2005) 285.
Pubmed | DOI

Gent, J., I. Braakman. Low-density lipoprotein receptor structure and folding. Cell. Mol. Life Sci. (2004) 61.
Pubmed | DOI | PDF

Kleizen B., I. Braakman. Protein folding in the ER. Curr Opin Cell Biol. (2004) 16(4).
Pubmed | DOI | PDF

Sitia, R., I. Braakman. Quality control in the ER protein factory. Nature (2003) 426.
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Van Anken*, E., E.P. Romijn*, C. Maggioni*, A. Mezghrani, R. Sitia#, I. Braakman#, A.J. Heck#. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity (2003) 18(2).
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Jansens, A., I. Braakman. Pulse-chase labeling techniques for the analysis of protein maturation and degradation. Methods Mol. Biol. (2003) 232: 133-145. (In: Protein misfolding and disease. (eds. P. Bross, N. Gregersen; Humana Press, Inc., Totowa, NJ, USA, 2003): 133-145).
Pubmed | DOI

Tabak H.F., J.L. Murk, I. Braakman, H.J. Geuze. Peroxisomes start their life in the endoplasmic reticulum. Traffic (2003) 4(8).
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Land, A., D. Zonneveld, I. Braakman. Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage. FASEB J. (2003) 17(9).
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Van der Vlies, D., M. Makkinje, A. Jansens, I. Braakman, A.J. Verkleij, K.W. Wirtz, J.A. Post. Oxidation of ER resident proteins upon oxidative stress: effects of altering cellular redox/antioxidant status and implications for protein maturation. Antioxid. Redox Signal. (2003) 5(4).
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Jansens, A, E. van Duijn, I. Braakman. Coordinated nonvectorial folding in a newly synthesized multidomain protein. Science (2002) 298.
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News & views: Radford, S.E. Co-translocational misfolding in the ER of living cells. Nat Struct Biol. 2003 10(3).
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Tabak, H.F., I. Braakman. Bakkersgist: een model voor een neurologische ziekte? In: Gekkekoeienziekte. De BSE voorbij?, Chapter 4 (eds. R. Lieverse, J.J.E. van Everdingen; Uitgeverij Belvédère/Medidact, Overveen/Alphen aan den Rijn, 2001).
PDF

Braakman, I. A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination. EMBO Rep. (2001) 2.
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Land, A., I. Braakman. Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. Biochimie (2001) 83.
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Mezghrani, A., A. Fassio, A. Benham, T. Simmen, I. Braakman, R. Sitia. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. (2001) 20.
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Benham, A.M., I. Braakman. Glycoprotein folding in the endoplasmic reticulum. Crit. Rev. Biochem. Mol. Biol. (2000) 35.
Pubmed | DOI | PDF

Kleizen, B., I. Braakman, H.R. de Jonge. Regulated trafficking of the CFTR chloride channel. Eur. J. Cell Biol. (2000) 79.
Pubmed | DOI | PDF

Braakman, I., E. van Anken. Folding of viral envelope glycoproteins in the endoplasmic reticulum. Traffic (2000) 1.
Pubmed | DOI | PDF

Distel, B., I. Braakman, Y. Elgersma, H.F. Tabak. Transactions at the peroxisomal membrane. Subcell. Biochem. (2000) 34.
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Benham, A.M., A. Cabibbo, A. Fassio, N. Bulleid, R. Sitia, I. Braakman. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lα. EMBO J. (2000) 19.
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Ermonval, M., S. Duvet, D. Zonneveld, R. Cacan, G. Buttin, I. Braakman. Truncated N-glycans affect protein folding in the ER of CHO-derived mutant cell lines without preventing calnexin binding. Glycobiol. (2000) 10.
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Tabak, H.F., I. Braakman, B. Distel. Peroxisomes: simple in function but complex in maintenance. Trends Cell Biol. (1999) 9.
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Das, A.T., A. Land, I. Braakman, B. Klaver, B. Berkhout. HIV-1 evolves into a non-syncytium-inducing virus upon prolonged culture in vitro. Virol., (1999) 263.
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Tabak, H.F., I. Braakman. Bakkersgist: een model voor een neurologische ziekte? In: Vouwfouten. Prionziekten als model, Chapter 6 (eds. P. Borst, J.J.E. van Everdingen, W.A. van Gool; Uitgeverij Boom/Belvédère, Amsterdam/Overveen, 1998).
PDF

Hettema, E.H., C.C.M. Ruigrok, M. Groot Koerkamp, M. van den Berg, H.F. Tabak, B. Distel, I. Braakman. The cytosolic DnaJ-like protein Djp1p is involved specifically in peroxisomal protein import. J. Cell Biol., (1998) 142.
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Van Weering, D.H.J., T.C. Moen, I. Braakman, P.D.Baas, J.L. Bos. Expression of the receptor tyrosine kinase Ret on the plasma membrane is dependent on calcium. J. Biol. Chem. (1998) 273.
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Zhang, J.-X., I. Braakman, K.E.S. Matlack, A. Helenius. Quality control in the secretory pathway: the role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations. Mol. Biol. Cell (1997) 8.
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Braakman, I., D.N. Hebert. Disulfide (-SS-) bond formation overview. In: Curr Protoc Protein Sci, Chapter 14.1 (eds. J. Coligan, B. Dunn, H. Ploegh, D. Speicher, P. Wingfield; John Wiley and Sons, Inc, New York, 1996, 2001):.
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Chen, W., J. Helenius, I. Braakman, A. Helenius. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl. Acad. Sci. USA (1995) 92.
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Hammond, C., I. Braakman, A. Helenius. Role of N-linked oligosaccharides, glucose trimming and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA, (1994).
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Helenius, A., U. Tatu, T. Marquardt, I. Braakman. Protein folding in the endoplasmic reticulum. in: Cell Biology and Biotechnology. Novel Approaches to Increased Cellular Productivity (eds. Oka, M.S. and Rupp, R.G., Springer Verlag, New York, 1993).
DOI

Tatu, U., I. Braakman, A. Helenius. Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells. EMBO J. (1993) 12
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De Silva, A., I. Braakman, A. Helenius. Posttranslational folding of VSV G protein in the ER: involvement of noncovalent and covalent complexes. J. Cell Biol. (1993) 120.
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Helenius, A., I. Braakman, T. Marquardt, U. Tatu. Protein folding and assembly in the endoplasmic reticulum. Fresenius J. Anal. Chem. (1992) 343.
Pubmed

Helenius, A., T. Marquardt, I. Braakman. The endoplasmic reticulum as a protein folding compartment. Trends Cell Biol. (1992) 2.
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Braakman, I., J. Helenius, A. Helenius. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J. (1992) 11.
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Braakman, I., J. Helenius, A. Helenius. The role of ATP and disulfide bonds during protein folding in the endoplasmic reticulum. Nature (1992) 356.
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Braakman, I., H. Hoover-Litty, K.R. Wagner, A. Helenius. Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. (1991) 114.
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Braakman, I., J. Keij, M.J. Hardonk, D.K.F. Meijer, G.M.M. Groothuis. Separation of periportal and perivenous rat hepatocytes by fluorescence activated cell sorting: confirmation with colloidal gold as an exogenous marker. Hepatology (1991) 13.
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Thalhammer, T., A. Gessl, I. Braakman, J. Graf. Separation of hepatocytes of different acinar zones by flow cytometry after their selective staining with acridine orange. Cytometry (1989) 10.
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Braakman, I., T. Pijning, O. Verest, B. Weert, D.K.F. Meijer, G.M.M. Groothuis. A vesicular uptake system for the cation lucigenin in the rat hepatocyte. Mol. Pharmacol. (1989) 36.
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Braakman, I., O. Verest, T. Pijning, D.K.F. Meijer, G.M.M. Groothuis. Zonal distribution of the cation lucigenin in rat liver: influence of taurocholate. Mol. Pharmacol. (1989) 36.
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Braakman, I., G.M.M. Groothuis, D.K.F. Meijer. Zonal compartmentation of perfused rat liver: plasma reappearance of rhodamine B explained. J. Pharmacol. Exp. Ther. (1989) 249.
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Van der Sluijs, P., I. Braakman, D.K.F. Meijer, G.M.M. Groothuis. Heterogeneous acinar localization of the asialoglycoprotein internalization system in rat hepatocytes. Hepatology (1988) 8.
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Braakman, I., G.M.M. Groothuis, D.K.F. Meijer. Acinar redistribution and heterogeneity in transport of the organic cation rhodamine B. Hepatology (1987) 7.
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Reviews

Lars Ellgaard, Nicholas McCaul, Anna Chatsisvili, Ineke Braakman. Co- and Post-Translational Protein Folding in the ER. Traffic (2016) 17(6).
Pubmed | DOI | PDF

Braakman, I., D.N. Hebert. Protein folding in the endoplasmic reticulum. Cold Spring Harb Perspect Biol. (Endoplasmic Reticulum. Ed. S. Ferro-Novick, T. Rapoport, R. Schekman), (2013) May 1; 5(5): a013201.
Pubmed | DOI | PDF

Tabak , H.F., A. Van der Zand, I. Braakman. Peroxisome formation and maintenance are dependent on the endoplasmic reticulum. Annu. Rev. Biochem. (2013) 82.
Pubmed | DOI | PDF

Braakman, I., N. Bulleid. Cellular Protein Folding and Modification in the Endoplasmic Reticulum. Annu. Rev. Biochem. (2011) 80.
Pubmed | DOI | PDF

Balch, W.E., I. Braakman, R. Frizzell, W. Guggino, G. Lukacs, C. Penland, W. Skach, E. Sorscher, P. Thomas, H. Pollard. The Folding Biology of Cystic Fibrosis: a Consortium-based Approach to Disease. In: Protein Misfolding Diseases: Current and Emerging Principles and Therapies. Ramirez-Alvarado, M., Kelly, J.W., Dobson, C.M. (Eds.). John Wiley & Sons, Inc., Wiley-Blackwell Division, Hoboken, NJ (2010) Chapter 20.
DOI | PDF

Christis, C., N.H. Lubsen, I. Braakman. Protein folding includes oligomerization: examples from the ER and cytosol. FEBS J. (2008) 275(19).
Pubmed | DOI | PDF

Tabak, H.F., A. van der Zand, I. Braakman. Peroxisomes: minted by the ER. Curr. Opin. Cell Biol. (2008) 20(4).
Pubmed | DOI | PDF

Van der Zand, A., I. Braakman, H.J. Geuze, H.F. Tabak. The return of the peroxisome. J. Cell Sci. (2006) 119.
Pubmed | DOI | PDF

De Jonge, W., H.F. Tabak, I. Braakman. Chaperone proteins and peroxisomal protein import. Topics in Current Genetics (2006) 16.
PDF

Van Anken, E., I. Braakman. Endoplasmic reticulum stress and the making of a professional secretory cell. Crit. Rev. Biochem. Mol. Biol. (2005) 40 (5).
Pubmed | DOI | PDF

Van Anken, E., I. Braakman. Versatility of the endoplasmic reticulum protein folding factory. Crit. Rev. Biochem. Mol. Biol. (2005) 40 (4).
Pubmed | DOI | PDF

Maggioni, C., I. Braakman. Synthesis and quality control of viral membrane proteins. Curr Topics Microbiol. Immunol. (2005) 285.
Pubmed | DOI

Gent, J., I. Braakman. Low-density lipoprotein receptor structure and folding. Cell. Mol. Life Sci. (2004) 61.
Pubmed | DOI | PDF

Kleizen B., I. Braakman. Protein folding in the ER. Curr Opin Cell Biol. (2004) 16(4).
Pubmed | DOI | PDF

Sitia, R., I. Braakman. Quality control in the ER protein factory. Nature (2003) 426.
Pubmed | DOI

Tabak, H.F., I. Braakman. Bakkersgist: een model voor een neurologische ziekte? In: Gekkekoeienziekte. De BSE voorbij?, Chapter 4 (eds. R. Lieverse, J.J.E. van Everdingen; Uitgeverij Belvédère/Medidact, Overveen/Alphen aan den Rijn, 2001).
PDF

Land, A., I. Braakman. Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. Biochimie (2001) 83.
Pubmed | DOI | PDF

Benham, A.M., I. Braakman. Glycoprotein folding in the endoplasmic reticulum. Crit. Rev. Biochem. Mol. Biol. (2000) 35.
Pubmed | DOI | PDF

Kleizen, B., I. Braakman, H.R. de Jonge. Regulated trafficking of the CFTR chloride channel. Eur. J. Cell Biol. (2000) 79.
Pubmed | DOI | PDF

Braakman, I., E. van Anken. Folding of viral envelope glycoproteins in the endoplasmic reticulum. Traffic (2000) 1.
Pubmed | DOI | PDF

Distel, B., I. Braakman, Y. Elgersma, H.F. Tabak. Transactions at the peroxisomal membrane. Subcell. Biochem. (2000) 34.
Pubmed | DOI

Tabak, H.F., I. Braakman, B. Distel. Peroxisomes: simple in function but complex in maintenance. Trends Cell Biol. (1999) 9.
Pubmed | DOI | PDF

Tabak, H.F., I. Braakman. Bakkersgist: een model voor een neurologische ziekte? In: Vouwfouten. Prionziekten als model, Chapter 6 (eds. P. Borst, J.J.E. van Everdingen, W.A. van Gool; Uitgeverij Boom/Belvédère, Amsterdam/Overveen, 1998): 70-78.
PDF

Helenius, A., U. Tatu, T. Marquardt, I. Braakman. Protein folding in the endoplasmic reticulum. in: Cell Biology and Biotechnology. Novel Approaches to Increased Cellular Productivity (eds. Oka, M.S. and Rupp, R.G., Springer Verlag, New York, 1993): 125-136.
DOI

Helenius, A., I. Braakman, T. Marquardt, U. Tatu. Protein folding and assembly in the endoplasmic reticulum. Fresenius J. Anal. Chem. (1992) 343.
Pubmed

Helenius, A., T. Marquardt, I. Braakman. The endoplasmic reticulum as a protein folding compartment. Trends Cell Biol. (1992) 2.
Pubmed | DOI | PDF

 

Methods

Peters, K.W., T. Okiyoneda, W.E. Balch, I. Braakman, J.L. Brodsky, W.B. Guggino, C.M. Penland, H.B. Pollard, E.J. Sorscher, W.R. Skach, P.J. Thomas, G.L. Lukacs, R.A. Frizzell. CFTR Folding Consortium: methods available for studies of CFTR folding and correction. Methods Mol Biol. (2011) 742.
Pubmed | DOI | PDF

Liscaljet, I.M., B. Kleizen, I. Braakman. Studying protein folding in vivo. Handbook of protein folding. (2005) Part II, Volume 1, Chapter 3: 73-104 (Eds Buchner, J. & Kiefhaber, T.).
DOI

Jansens, A., I. Braakman. Pulse-chase labeling techniques for the analysis of protein maturation and degradation. Methods Mol. Biol. (2003) 232: 133-145. (In: Protein misfolding and disease. (eds. P. Bross, N. Gregersen; Humana Press, Inc., Totowa, NJ, USA, 2003): 133-145).
Pubmed | DOI

Braakman, I., D.N. Hebert. Disulfide (-SS-) bond formation overview. In: Curr Protoc Protein Sci, Chapter 14.1 (eds. J. Coligan, B. Dunn, H. Ploegh, D. Speicher, P. Wingfield; John Wiley and Sons, Inc, New York, 1996, 2001).
PDF

 

Perspectives/Comments

Kleizen, B., I. Braakman. A sweet send-off. Science (2013) 340(6135).
Pubmed | DOI | PDF

Braakman, I. Entering a new era with Ero. Nature Rev Mol. Cell Biol. (2009) 10(8).
Pubmed | DOI

Braakman, I., M. Otsu. Cargo load reduction. Science (2008) 321(5888).
DOI

Braakman, I. A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination. EMBO Rep. (2001) 2.
Pubmed | DOI | PDF

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