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Prof. dr. Ineke Braakman

Hoogleraar 
Bètawetenschappen
Scheikunde
Biomolecular Sciences
Cellular Protein Chemistry
Cellular Protein Chemistry

Prof. dr. Ineke Braakman

Hoogleraar
Cellular Protein Chemistry
Profiel Publicaties Onderzoek Onderwijs Nevenwerkzaamheden Contact
Profiel Publicaties Onderzoek Onderwijs Nevenwerkzaamheden Contact
Onderzoeksthema's

Publicaties

2023

Wetenschappelijke publicaties

Braakman, I., High, S., Kadler, K., Sitia, R., Tokatlidis, K., & Woodman, P. (2023). Neil J. Bulleid (1960-2023), a virtuoso of protein folding and redox biology. EMBO Journal, 42(17), 1-2. Article e115046. https://doi.org/10.15252/embj.2023115046
https://dspace.library.uu.nl/bitstream/handle/1874/435358/braakman-et-al-2023-neil-j-bulleid-_1960-2023_-a-virtuoso-of-protein-folding-and-redox-biology.pdf?sequence=1
Kleizen, B., de Mattos, E., Papaioannou, O., Monti, M., Tartaglia, G. G., van der Sluijs, P., & Braakman, I. (2023). Transmembrane Helices 7 and 8 Confer Aggregation Sensitivity to the Cystic Fibrosis Transmembrane Conductance Regulator. International Journal of Molecular Sciences, 24(21), Article 15741. https://doi.org/10.3390/ijms242115741
Im, J., Hillenaar, T., Yeoh, H. Y., Sahasrabudhe, P., Mijnders, M., van Willigen, M., Hagos, A., de Mattos, E., van der Sluijs, P., & Braakman, I. (2023). ABC-transporter CFTR folds with high fidelity through a modular, stepwise pathway. Cellular and Molecular Life Sciences, 80(1), 1-26. Article 33. https://doi.org/10.1007/s00018-022-04671-x
https://dspace.library.uu.nl/bitstream/handle/1874/434160/s00018-022-04671-x.pdf?sequence=1
Hwang, T.-C., Braakman, I., van der Sluijs, P., & Callebaut, I. (2023). Structure basis of CFTR folding, function and pharmacology. Journal of Cystic Fibrosis, 22(S1), S5-S11. https://doi.org/10.1016/j.jcf.2022.09.010

2022

Wetenschappelijke publicaties

McCaul, N., & Braakman, I. (2022). Hold the fold: how delayed folding aids protein secretion. EMBO Journal, 41(23), Article e112787. https://doi.org/10.15252/embj.2022112787
Hillenaar, T., Beekman, J., van der Sluijs, P., & Braakman, I. (2022). Redefining Hypo- and Hyper-Responding Phenotypes of CFTR Mutants for Understanding and Therapy. International Journal of Molecular Sciences, 23(23), Article 15170. https://doi.org/10.3390/ijms232315170

2021

Wetenschappelijke publicaties

McCaul, N., Quandte, M., Bontjer, I., van Zadelhoff, G., Land, A., Crooks, E. T., Binley, J. M., Sanders, R. W., & Braakman, I. (2021). Intramolecular quality control: HIV-1 envelope gp160 signal-peptide cleavage as a functional folding checkpoint. Cell Reports, 36(9), 1-21. Article 109646. https://doi.org/10.1016/j.celrep.2021.109646
Sabusap, C. M., Joshi, D., Simhaev, L., Oliver, K. E., Senderowitz, H., van Willigen, M., Braakman, I., Rab, A., Sorscher, E. J., & Hong, J. S. (2021). The CFTR P67L variant reveals a key role for N-terminal lasso helices in channel folding, maturation, and pharmacologic rescue. Journal of Biological Chemistry, 296, 1-16. Article 100598. https://doi.org/10.1016/j.jbc.2021.100598
Kleizen, B., van Willigen, M., Mijnders, M., Peters, F., Grudniewska, M., Hillenaar, T., Thomas, A., Kooijman, L., Peters, K. W., Frizzell, R., van der Sluijs, P., & Braakman, I. (2021). Co-Translational Folding of the First Transmembrane Domain of ABC-Transporter CFTR is Supported by Assembly with the First Cytosolic Domain. Journal of Molecular Biology, 433(13), 1-24. Article 166955. https://doi.org/10.1016/j.jmb.2021.166955
Haq, I. J., Althaus, M., Gardner, A. I., Yeoh, H. Y., Joshi, U., Saint-Criq, V., Verdon, B., Townshend, J., O'Brien, C., Ben-Hamida, M., Thomas, M., Bourke, S., van der Sluijs, P., Braakman, I., Ward, C., Gray, M. A., & Brodlie, M. (2021). Clinical and molecular characterization of the R751L-CFTR mutation. American Journal of Physiology - Lung Cellular and Molecular Physiology, 320(2), L288-L300. https://doi.org/10.1152/AJPLUNG.00137.2020

2020

Wetenschappelijke publicaties

Armengaud, J., Delaunay-Moisan, A., Thuret, J. Y., van Anken, E., Acosta-Alvear, D., Aragón, T., Arias, C., Blondel, M., Braakman, I., Collet, J. F., Courcol, R., Danchin, A., Deleuze, J. F., Lavigne, J. P., Lucas, S., Michiels, T., Moore, E. R. B., Nixon-Abell, J., Rossello-Mora, R., ... Vicenzi, E. (2020). The importance of naturally attenuated SARS-CoV-2in the fight against COVID-19. Environmental Microbiology, 22(6), 1997-2000. https://doi.org/10.1111/1462-2920.15039

2019

Wetenschappelijke publicaties

Oliver, K. E., Rauscher, R., Mijnders, M., Wang, W., Wolpert, M. J., Maya, J., Sabusap, C. M., Kesterson, R. A., Kirk, K. L., Rab, A., Braakman, I., Hong, J. S., Hartman, J. L., Ignatova, Z., & Sorscher, E. J. (2019). Slowing ribosome velocity restores folding and function of mutant CFTR. Journal of Clinical Investigation, 129(12), 5236-5253. https://doi.org/10.1172/JCI124282
https://dspace.library.uu.nl/bitstream/handle/1874/387704/124282.2_20191118212345_covered_253bed37ca4c1ab43d105aefdf7b5536.pdf?sequence=1
Van Willigen, M., Vonk, A. M., Yeoh, H. Y., Kruisselbrink, E., Kleizen, B., Van Der Ent, C. K., Egmond, M. R., De Jonge, H. R., Braakman, I., Beekman, J. M., & Van Der Sluijs, P. (2019). Folding-function relationship of the most common cystic fibrosis-causing CFTR conductance mutants. Life Science Alliance, 2(1), Article e201800172. https://doi.org/10.26508/lsa.201800172
Schildknegt, D., Lodder, N., Pandey, A., Egmond, M., Pena, F., Braakman, I., & van der Sluijs, P. (2019). Characterization of CNPY5 and its family members. Protein Science, 28(7), 1276-1289. https://doi.org/10.1002/pro.3635
McCaul, N., Yeoh, H. Y., van Zadelhoff, G., Lodder, N., Kleizen, B., & Braakman, I. (2019). Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase. Journal of Visualized Experiments, (144). https://doi.org/10.3791/58952

2018

Wetenschappelijke publicaties

Feige, M. J., Braakman, I., & Hendershot, L. M. (2018). CHAPTER 1.1. Disulfide Bonds in Protein Folding and Stability. In Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering (pp. 1-33). (Chemical Biology Series). Royal Society of Chemistry. https://doi.org/10.1039/9781788013253-00001
https://dspace.library.uu.nl/bitstream/handle/1874/372766/9781788013253_00001.pdf?sequence=1
Mall, M. A., Hwang, T.-C., & Braakman, I. (2018). Cystic fibrosis research topics featured at the 14th ECFS Basic Science Conference: Chairman's summary. Journal of Cystic Fibrosis, 17(2 Supplement), S1-S4. https://doi.org/10.1016/j.jcf.2017.11.008
https://dspace.library.uu.nl/bitstream/handle/1874/394457/Cystic.pdf?sequence=1

2017

Wetenschappelijke publicaties

Kirchner, S., Cai, Z., Rauscher, R., Kastelic, N., Anding, M., Czech, A., Kleizen, B., Ostedgaard, L. S., Braakman, I., Sheppard, D. N., & Ignatova, Z. (2017). Alteration of protein function by a silent polymorphism linked to tRNA abundance. PLoS Biology, 15(5). https://doi.org/10.1371/journal.pbio.2000779
Peters, F., Sahasrabudhe, P., Gross-Wilde, H., Kleizen, B., Conrath, K., & Braakman, I. (2017). Deciphering the mode of action of clinically relevant next generation c2 corrector compounds GLPG2737 and GLPG3221. Pediatric Pulmonology, 52, 230-231. https://doi.org/10.1002/ppul.23840
https://dspace.library.uu.nl/bitstream/handle/1874/361094/Pages_from_ppul23840.pdf?sequence=1
Snapp, E. L., McCaul, N., Quandte, M., Cabartova, Z., Bontjer, I., Källgren, C., Nilsson, I., Land, A., Von Heijne, G., Sanders, R. W., & Braakman, I. (2017). Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide. eLife, 6, Article 26067. https://doi.org/10.7554/eLife.26067
Braakman, I., Lamriben, L., van Zadelhoff, G., & Hebert, D. N. (2017). Analysis of Disulfide Bond Formation. Current Protocols in Protein Science, 90, 14.1.1-14.1.21. https://doi.org/10.1002/cpps.43
Mijnders, M., Kleizen, B., & Braakman, I. (2017). Correcting CFTR folding defects by small-molecule correctors to cure cystic fibrosis. Current Opinion in Pharmacology, 34, 83-90. https://doi.org/10.1016/j.coph.2017.09.014

Overige resultaten

Mijnders, M., Musch, S., Peters, F., Conrath, K., Braakman, I., & Kleizen, B. (2017). Mutations in the second cytoplasmic loop of CFTR suggest distinct mode of action between potentiators VX-770 and glpg1837. S224. https://doi.org/10.1002/ppul.23840

2016

Wetenschappelijke publicaties

Braakman, I., Kleizen, B., Mijnders, M., Van Willigen, M., Peters, F., Frizzell, R. A., & Peters, K. W. (2016). Corrector and potentiator action on CFTR domain assembly. Pediatric Pulmonology, 51, 142. https://doi.org/10.1002/ppul.23575
Peters, F., Mijnders, M., Andrews, M., Van Der Plas, S., Conrath, K., Braakman, I., & Kleizen, B. (2016). The novel potentiator GLPG1837 modulates CFTR through different mode of action than Ivacaftor (kalydeco). Pediatric Pulmonology, 51, 195. https://doi.org/10.1002/ppul.23576
McCaffrey, K., & Braakman, I. (2016). Protein quality control at the endoplasmic reticulum. Essays in Biochemistry, 60(2), 227-235. https://doi.org/10.1042/EBC20160003
Kakkar, V., Kuiper, E. F. E., Pandey, A., Braakman, I., & Kampinga, H. H. (2016). Versatile members of the DNAJ family show Hsp70 dependent anti-aggregation activity on RING1 mutant parkin C289G. Scientific Reports, 6, Article 34830. https://doi.org/10.1038/srep34830
Shen, S., Wang, M., Li, X., Li, S., van Oers, M. M., Vlak, J. M., Braakman, I., Hu, Z., Deng, F., & Wang, H. (2016). Mutational and functional analysis of N-linked glycosylation of envelope fusion protein F of Helicoverpa armigera nucleopolyhedrovirus. Journal of General Virology, 97(4), 988-99. https://doi.org/10.1099/jgv.0.000404
Ellgaard, L., McCaul, N., Chatsisvili, A., & Braakman, I. (2016). Co- and Post-Translational Protein Folding in the ER. Traffic, 17(6), 615-38. https://doi.org/10.1111/tra.12392

2015

Wetenschappelijke publicaties

Peters, F., Kleizen, B., Andrews, M., Van Der Plas, S., Tse, C., Conrath, K., & Braakman, I. (2015). Potentiators: How do they impact the fate of CFTR during biogenesis? Pediatric Pulmonology, 50, 210. https://doi.org/10.1002/ppul.23297
Knoblach, B., Rachubinski, R. A., Adeyo, O., Horn, P. J., Lee, S., Binns, D. D., Chandrahas, A., Chapman, K. D., Goodman, J. M., Agrawal, G., Subramani, S., Altmann, K. H., Frank, M., Neumann, D., Jakobs, S., Westermann, B., Arai, S., Noda, Y., Kainuma, S., ... Bretscher, A. (2015). Sharing the cell's bounty - organelle inheritance in yeast. In Journal of cell science (pp. 621-30). (Journal of cell science; Vol. 128). The Company of Biologists Ltd. https://doi.org/10.1242/jcs.151423
Li, X., van Oers, M. M., Vlak, J. M., & Braakman, I. (2015). Folding of influenza virus hemagglutinin in insect cells is fast and efficient. Journal of Biotechnology, 203, 77-83. https://doi.org/10.1016/j.jbiotec.2015.03.018
Jevtov, I., Zacharogianni, M., van Oorschot, M. M., van Zadelhoff, G., Aguilera-Gomez, A., Vuillez, I., Braakman, I., Hafen, E., Stocker, H., & Rabouille, C. (2015). TORC2 mediates the heat stress response in Drosophila by promoting the formation of stress granules. Journal of Cell Science, 128(14), 2497-2508. https://doi.org/10.1242/jcs.168724

2014

Wetenschappelijke publicaties

Mathys, L., François, K. O., Quandte, M., Braakman, I., & Balzarini, J. (2014). Erratum: 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 (e101181) DOI: 10.1371/journal.pone.0101181). PLoS One, 9(10). https://doi.org/10.1371/journal.pone.0110202
Mathys, L., François, K. O., Quandte, M., Braakman, I., & Balzarini, J. (2014). 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. In PLoS ONE (PLoS ONE; Vol. 9). Public Library of Science. https://doi.org/10.1371/journal.pone.0101181

2013

Wetenschappelijke publicaties

Koritzinsky, M., Levitin, F., Van Den Beucken, T., Rumantir, R. A., Harding, N. J., Chu, K. C., Boutros, P. C., Braakman, I., & Wouters, B. G. (2013). Two phases of disulfide bond formation have differing requirements for oxygen. Journal of Cell Biology, 203(4), 615-627. https://doi.org/10.1083/jcb.201307185
Oka, O. B. V., Pringle, M. A., Schopp, I. M., Braakman, I., & Bulleid, N. J. (2013). ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor. Molecular Cell, 50(6), 793-804. https://doi.org/10.1016/j.molcel.2013.05.014
Benham, A. M., Lith, M. V., Sitia, R., & Braakman, I. (2013). Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum. Philosophical transactions / Royal Society of London. Biological sciences, 368(1617), Article 20110403. https://doi.org/10.1098/rstb.2011.0403
Kleizen, B., & Braakman, I. (2013). A sweet send-off. Science, 340(6135), 930-931. https://doi.org/10.1126/science.1239294
Braakman, I., & Hebert, D. N. (2013). Protein folding in the endoplasmic reticulum. In T. R. R. Schekman S. Ferro-Novick (Ed.), The Endoplasmic Reticulum : a subject collection from Cold Spring Harbor perspectives in biology (Cold Spring Harbor Perspectives in Biology; No. 5). Cold Spring Harbor Laboratory.
Hansen, R. E., Otsu, M., Braakman, I., & Winther, J. R. (2013). Quantifying changes in the cellular thiol-disulfide status during differentiation of B cells into antibody-secreting plasma cells. International Journal of Cell Biology, 1-10. Article 898563. https://doi.org/10.1155/2013/898563
Tabak, H. F., Braakman, I., & van der Zand, A. (2013). Peroxisome Formation and Maintenance Are Dependent on the Endoplasmic Reticulum. Annual Review of Biochemistry, 82, 723-744. https://doi.org/10.1146/annurev-biochem-081111-125123

2012

Wetenschappelijke publicaties

Koritzinsky, M., Van Den Beucken, T., Chu, K., Boutros, P. C., Braakman, I., & Wouters, B. G. (2012). Hypoxia inhibits disulfide bond formation and protein folding in the endoplasmic reticulum. Radiotherapy and Oncology, 102, 185-186. https://doi.org/10.1016/S0167-8140(12)70311-0
van der Zand, A., Gent, J. C. M., Braakman, I., & Tabak, H. F. (2012). Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes. Cell, 149(2), 397-409. https://doi.org/10.1016/j.cell.2012.01.054

2011

Wetenschappelijke publicaties

Braakman, L. J., & Bulleid, N. J. (2011). Protein Folding and Modification in the Mammalian Endoplasmic Reticulum. Annual Review of Biochemistry, 80, 71-99. https://doi.org/10.1146/annurev-biochem-062209-093836
Peters, K. W., Okiyoneda, T., Balch, W. E., Braakman, L. J., Brodsky, J. L., Guggino, W. B., Penland, C. M., Pollard, H. B., Sorscher, E. J., Skach, W. R., Thomas, P. J., Lukacs, G. L., & Frizzell, R. A. (2011). CFTR Folding Consortium: methods available for studies of CFTR folding and correction. Methods in Molecular Biology, 742, 335-353.

2010

Wetenschappelijke publicaties

Pyle, L. C., Balch, W. E., Lukacs, G., Braakman, I., Guggino, W., Thomas, P. J., Penland, C., Pollard, H., Brodsky, J. L., Frizzell, R., Sorscher, E. J., & Skach, W. R. (2010). Developing a cellular roadmap for correctors of CFTR misfolding. Pediatric Pulmonology, 45, 222. https://doi.org/10.1002/(ISSN)1099-0496
Hoelen, H. M., Kleizen, B., Schmidt, A., Richardson, J., Charitou, P., Braakman, L. J., & Thomas, P. J. (2010). The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain. PLoS One, 5(11), 1-10. https://doi.org/10.1371/journal.pone.0015458
https://dspace.library.uu.nl/bitstream/handle/1874/196856/The-primary-folding-defect-and-rescue_2010_PLoS-ONE.pdf?sequence=1
Pena, F., Jansens, A., van Zadelhoff, G., & Braakman, L. J. (2010). Calcium as a crucial cofactor for low density lipoprotein receptor folding in the endoplasmic reticulum. Journal of Biological Chemistry, 285(12), 8656-8664. https://doi.org/10.1074/jbc.M110.105718
https://dspace.library.uu.nl/bitstream/handle/1874/200564/Calcium-as-a-crucial-cofactor-for-low-density_2010_Journal-of-Biological-Chemistry.pdf?sequence=1
van der Zand, A., Braakman, L. J., & Tabak, H. F. (2010). Peroxisomal membrane proteins insert into the endoplasmic reticulum. Molecular Biology of the Cell, 21(12), 2057-2065. https://doi.org/10.1091/mbc.E10-02-0082
https://dspace.library.uu.nl/bitstream/handle/1874/202445/Peroxisomal-membrane-proteins_2010_Molecular-Biology-of-the-Cell.pdf?sequence=1
Christis, C., Fullaondo, A., Schildknegt, D., Mkrtchian, S., Heck, A. J. R., & Braakman, L. J. (2010). Regulated increase in folding capacity prevents unfolded protein stress in the ER. Journal of Cell Science, 123(5), 787-794. https://doi.org/10.1242/jcs.041111
https://dspace.library.uu.nl/bitstream/handle/1874/200563/Regulated-increase-in-folding-capacity_2010_Journal-of-Cell-Science.pdf?sequence=1

2009

Wetenschappelijke publicaties

Bontjer, I., Land, A., Eggink, D., Verkade, E., Tuin, K., Baldwin, C., Pollakis, G., Paxton, W. A., Braakman, L. J., Berkhout, B., & Sanders, R. W. (2009). Optimization of human immunodeficiency virus type 1 envelope glycoproteins with V1/V2 deleted, using virus evolution. Journal of Virology, 83(1), 368-383.
Braakman, L. J. (2009). Entering a new era with Ero. Nature Reviews Molecular Cell Biology, 10, 503-503.
van Anken, E., Pena, F., Hafkemeijer, N., Christis, C., Romijn, E. P., Grauschopf, U., Oorschot, V. M. J., Pertel, T., Engels, S., Ora, A., Lastun, V., Glockshuber, R., Klumperman, J., Heck, A. J. R., Luban, J., & Braakman, I. (2009). Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1. Proceedings of the National Academy of Sciences of the United States of America, 106(40), 17019-17024.
Balch, W. E., Braakman, L. J., Frizzell, R., Guggino, W., Lukacs, G., Penland, C., Skach, W., Sorscher, E., Thomas, P., & Pollard, H. (2009). The folding biology of cystic fibrosis: a consortium-based approach to disease. In M. Ramirez-Alvarado, J. W. Kelly, & C. M. Dobson (Eds.), Protein misfolding diseases : current and emerging principles and therapies Wiley.

Overige resultaten

van Meegen, M. A., Terheggen - Lagro, S. W. J., Hoelen, H. M., Braakman, I., Coffer, P. J., van der Ent, C. K., & Beekman, J. M. (2009). Analysis of CFTR expression in immune cell subsets of peripheral blood. Abstract from ECFC, Brest.

2008

Wetenschappelijke publicaties

Braakman, I., & Otsu, M. (2008). Biochemistry. Cargo load reduction. Science (New York, N.Y.), 321(5888), 499-500. https://doi.org/10.1126/science.1162125
Liscaljet, I. M., Kleizen, B., & Braakman, I. (2008). Studying Protein Folding in Vivo. In J. Buchner, & T. Kiefhaber (Eds.), Protein Folding Handbook (Vol. 1, pp. 73-104). Wiley - VCH Verlag GmbH & CO. KGaA. https://doi.org/10.1002/9783527619498.ch36
van Anken, E., Sanders, R. W., Liscaljet, I. M., Land, A., Bontjer, I., Tillemans, S., Nabatov, A. A., Paxton, W. A., Berkhout, B., & Braakman, L. J. (2008). Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the hiv-1 envelope glycoprotein. Molecular Biology of the Cell, 19, 4298-4309.
https://dspace.library.uu.nl/bitstream/handle/1874/32180/van%2520Anken%2520et%2520al%2C%25202008.pdf?sequence=2
Tabak, H. F., van der Zand, A., & Braakman, L. J. (2008). Peroxisomes: minted by the ER. Current Opinion in Cell Biology, 20, 393-400.
https://dspace.library.uu.nl/bitstream/handle/1874/33030/Tabak%2C%2520van%2520der%2520Zand%2520and%2520Braakman%2C%25202008.pdf?sequence=1
Sanders, R. W., Hsu, S. T., van Anken, E., Liscaljet, I. M., Dankers, M., Bontjer, I., Land, A., Braakman, L. J., Bonvin, A. M. J. J., & Berkhout, B. (2008). Evolution rescues folding of Human Immunodeficiency Virus-1 envelope glycoprotein GP120 lacking a conserved disulfide bond. Molecular Biology of the Cell, 19(11), 4707-4716. https://doi.org/10.1091/mbc.e08-07-0670
Christis, C., Lubsen, N. H., & Braakman, I. (2008). Protein folding includes oligomerization – examples from the endoplasmic reticulum and cytosol. The FEBS journal, 275, 4700-4727.
https://dspace.library.uu.nl/bitstream/handle/1874/33033/Christis%2C%2520Lubsen%2520and%2520Braakman%2C%25202008.pdf?sequence=1
Sanders, R. W., van Anken, E., Nabatov, A. A., Liscaljet, I. M., Bontjer, I., Eggink, D., Melchers, M., Busser, E., Dankers, M. M., de Groot, F., Braakman, L. J., Berkhout, B., & Paxton, W. A. (2008). The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion. Retrovirology, 5, 10.
https://dspace.library.uu.nl/bitstream/handle/1874/32181/Sanders%2520et%2520al.%2C%25202008%2520%282%29.pdf?sequence=1
Braakman, I., & Otsu, M. (2008). Cargo load reduction. Science, 321, 499-500.
https://dspace.library.uu.nl/bitstream/handle/1874/33034/Braakman%2520and%2520Otsu%2C%25202008.pdf?sequence=1

2006

Wetenschappelijke publicaties

de Jonge, W., Tabak, H. F., & Braakman, I. (2006). Chaperone proteins and peroxisomal protein import. Tijdschrift: tijdelijk onbekend, 16, 149-183.
https://dspace.library.uu.nl/bitstream/handle/1874/19166/45%2520Jonge%2520TiCG%252006.pdf?sequence=1
Piersma, D., Berns, E. M. J. J., Verhoef-Post, M., Uitterlinden, A. G., Braakman, L. J., Pols, H. A. P., & Themmen, A. P. N. (2006). A Common Polymorphism Renders the Luteinizing Hormone Receptor Protein More Active by Improving Signal Peptide Function and Predicts Adverse Outcome in Breast Cancer Patients. Journal of Clinical Endocrinology and Metabolism, 91(4), 1470-1476.
https://dspace.library.uu.nl/bitstream/handle/1874/20028/47%2520Piersma%2520JCEM%252006.pdf?sequence=1
Benham, A. M., Kleizen, B., Sitia, R., & Braakman, I. (2006). Conformation dependent redox sensing of the human ER protein Ero1-Lα. Journal of Biological Chemistry.
van der Zand, A., Braakman, I., Geuze, H. J., & Tabak, H. F. (2006). The return of the peroxisome. Journal of Cell Science, 119(6), 989-994.
https://dspace.library.uu.nl/bitstream/handle/1874/19284/46%2520Zand%2520JCS%252006.pdf?sequence=1
Tabak, H. F., Hoepfner, D., van der Zand, A., Geuze, H. J., Braakman, L. J., & Huynen, M. A. (2006). Formation of peroxisomes: Present and past. Biochimica et Biophysica Acta-Molecular Cell Research, 1763(12), 1647-1654.
https://dspace.library.uu.nl/bitstream/handle/1874/19277/49%2520Tabak%2520BBA%252006.pdf?sequence=1
Kleizen, B., van Vlijmen, T., de Jonge, H. R., & Braakman, L. J. (2006). Folding of CFTR is predominantly cotranslational. Molecular Cell, 20, 277-287.

2005

Wetenschappelijke publicaties

Maggioni, M. C., & Braakman, L. J. (2005). Synthesis and quality control of viral membrane proteins. Current Topics in Microbiology and Immunology, 285, 175-198.
https://dspace.library.uu.nl/bitstream/handle/1874/14676/36%2520Maggioni%2520CTMI%2520%2705.pdf?sequence=1
Hoepfner, D., Schildknegt, D., Braakman, L. J., Philippsen, P., & Tabak, H. F. (2005). Contribution of the endoplasmic reticulum to peroxisome formation. Cell, 122(1), 85-95.
Kleizen, B., van Vlijmen, T., de Jonge, H., & Braakman, I. (2005). CFTR folds predominantly co-translational. Molecular Cell, 20(2), 277-287.
https://dspace.library.uu.nl/bitstream/handle/1874/7721/42%2520Kleizen%2520MollCell%252005.pdf?sequence=2
van Anken, E., & Braakman, I. (2005). Endoplasmic reticulum stress and the making of a professional secretory cell. Critical Reviews in Biochemistry and Molecular Biology, 40(5), 269-283.
https://dspace.library.uu.nl/bitstream/handle/1874/14798/44%2520Anken%2520CRBMB%252040%2805%29%252005.pdf?sequence=1
Romijn, E. P., Christis, C., Wieffer, M., Gouw, J. W., Fullaondo, A., van der Sluijs, P., Braakman, L. J., & Heck, A. J. R. (2005). Expression Clustering Reveals Detailed Co-expression Patterns of Functionally Related Proteins during B Cell Differentiation. Molecular & Cellular Proteomics, 4, 1297-1310.
Maggioni, M. C., Liscaljet, I. M., & Braakman, L. J. (2005). A critical step in the folding of influenza virus HA determined with a novel folding assay. Nature Structural and Molecular Biology, 12(3), 258-263.
https://dspace.library.uu.nl/bitstream/handle/1874/14674/39%2520Maggioni%2520NSMB%2520%2705.pdf?sequence=3
van Anken, E., & Braakman, I. (2005). Versatility of the ER protein folding factory. Critical Reviews in Biochemistry and Molecular Biology, 40, 191-228.
https://dspace.library.uu.nl/bitstream/handle/1874/14799/43%2520Anken%2520CRBMB%2520%2705.pdf?sequence=1

2004

Wetenschappelijke publicaties

Kleizen, B., & Braakman, I. (2004). Erratum: Protein folding and quality control in the endoplasmic reticulum (Current Opinion in Cell Biology PII: S0955-0674(04)00081-X and DOI: 10.1016/j.ceb.2004.06.012). Current Opinion in Cell Biology, 16(5), 597. https://doi.org/10.1016/j.ceb.2004.08.003
Kleizen, B., & Braakman, I. (2004). Protein folding in the ER. Current Opinion in Cell Biology, 16(4), 343-349.
Kleizen, B., & Braakman, L. J. (2004). Protein folding and quality control in the endoplasmic reticulum. Current Opinion in Cell Biology, 16(5), 343-349.
Gent, J. C. M., & Braakman, L. J. (2004). Low-density lipoprotein receptor structure and folding. Cellular and Molecular Life Sciences, 61((19-20)), 2461-2470.

2003

Wetenschappelijke publicaties

Van der Vlies, D., Makkinje, M., Jansens, A., Braakman, I., Verkleij, A. J., Wirtz, K. W. A., & Post, J. A. (2003). Oxidation of ER resident proteins upon oxidative stress: Effects of altering cellular redox/antioxidant status and implications for protein maturation. Antioxidants and Redox Signaling, 5(4), 381-387.
Sitia, R., & Braakman, I. (2003). Quality control in the endoplasmic reticulum protein factory. Nature, 426, 891-894.
Tabak, H. F., Murk, J. L. A. N., Braakman, L. J., & Geuze, H. J. (2003). Peroxisomes start their life in the endoplasmic reticulum. Traffic, 4, 512-518.
Land, A., Zonneveld, D., & Braakman, L. J. (2003). Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage. FASEB Journal, 17(9), 1058-1067.
Jansens, A., & Braakman, I. (2003). Pulse-chase labeling techniques for the analysis of protein maturation and degradation. In P. Bross, & N. Gregersen (Eds.), Protein misfolding and disease (pp. 133-145). Humana Press.
Jansens, A., & Braakman, L. J. (2003). Puls-chase labeling techniques for the analysis of protein maturation and degradation. Methods in Molecular Biology, 232, 133-145.
van Anken, E., Romijn, E. P., Maggioni, M. C., Mezghrani, A., Sitia, R., Braakman, L. J., & Heck, A. J. R. (2003). Sequential Waves of Functionally Related Proteins Are Expressed When B Cells Prepare for Antibody Secretion. Immunity, 18, 243-253.
Vlies, D., Langelaar-Makkinje, M., Jansens, A., Braakman, L. J., Verkleij, A. J., Wirtz, K. W. A., & Post, J. A. (2003). Oxidation of ER resident proteins upon oxidative stress: effects of altering cellular redox/antioxydant status and implications for proteins maturation. Antioxidants & redox signaling, 5, 381-387.
https://dspace.library.uu.nl/bitstream/handle/1874/14951/5.van%2520der%2520Vlies%25202003%2520pp%2520381-7.pdf?sequence=1

2002

Wetenschappelijke publicaties

Jansens, A., van Duijn, E., & Braakman, L. J. (2002). Coordinated nonvectorial folding in a newly synthesized multidomain protein. Science, 298(5602), 2401-2403.

2001

Wetenschappelijke publicaties

Mezghrani, A., Fassio, A., Benham, A. M., Simmen, T., Braakman, L. J., & Sitia, R. (2001). Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO Journal, 20(22), 6288-6296.
Land, A., & Braakman, L. J. (2001). Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasic reticulum. Biochimie, 83(8), 783-790.
Mezghrani, A., Fassio, A., Benham, A. M., Simmen, T., Braakman, L. J., & Sitia, R. (2001). n of oxidative protein folding and PDI redox state in mammalian cells. EMBO Journal, 20, 6288-6296.
Braakman, L. J. (2001). A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination. EMBO Reports, 2(8), 666-668.
Tabak, H. F., & Braakman, I. (2001). Bakkersgist: een model voor een neurologische ziekte? In R. Lieverse, & J. J. E. van Everdingen (Eds.), Gekkekoeienziekte. De BSE voorbij? (pp. 37-41). Belvédère/Medidact.

2000

Wetenschappelijke publicaties

Benham, A. M., Cabibbo, A., Fassio, A., Bulleid, N., Sitia, R., & Braakman, I. (2000). The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lα. EMBO Journal, 19(17), 4493-4502. https://doi.org/10.1093/emboj/19.17.4493
Kleizen, B., Braakman, L. J., & de Jonge, H. R. (2000). Regulated trafficking of the CTR chloride channel. European Journal of Cell Biology, 79(8), 544-556.
Distel, B., Braakman, L. J., & Tabak, H. F. (2000). Transactions at the peroxisomal membrane. Subcellular biochemistry, 34, 322.
Benham, A. M., Cabibbo, A., Fassio, A., Bulleid, N., Sitia, R., & Braakman, L. J. (2000). The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha. EMBO Journal, 19(17), 4493-4502.
Ermonval, M., Duvet, S., Zonneveld, D., Cacan, R., Buttin, G., & Braakman, L. J. (2000). Truncated N-glycans affect protein folding in the ER of CHO-derived mutant cell lines withot preventing calnexin binding. Glycobiology, 10(1), 77-87.
Braakman, L. J., & van Anken, E. (2000). Folding of viral envelope glycoproteins in the endoplasmic reticulum. Traffic, 1(7), 533-539.
Benham, A. M., & Braakman, L. J. (2000). Glycoprotein folding in the endoplasmic reticulum. Critical Reviews in Biochemistry and Molecular Biology, 35(6), 433-473.

1999

Wetenschappelijke publicaties

Das, A. T., Braakman, I., Klaver, B., & Berkhout, B. (1999). HIV-1 evolves into a nonsyncytium-inducing virus upon prolonged culture in vitro. Virology, 263(1), 55-69. https://www.sciencedirect.com/science/article/pii/S0042682299998987?via%3Dihub
Tabak, H. F., Braakman, L. J., & Distel, B. (1999). Peroxisomes: somple in function but complex in maintenance. Trends in Cell Biology, 9(11), 447-453.

1998

Wetenschappelijke publicaties

Hettema, E. H., Ruigrok, C. C. M., Koerkamp, M. G., Van Den Berg, M., Tabak, H. F., Distel, B., & Braakman, I. (1998). The cytosolic DnaJ-like protein Djp1p is involved specifically in peroxisomal protein import. Journal of Cell Biology, 142(2), 421-434. https://doi.org/10.1083/jcb.142.2.421
Gowing, H., Braakman, L. J., Hagenbeek, A., Lawler, M., McCann, S. R., Pamphilon, D. H., & Martens, A. C. M. (1998). Influence of ultraviolet-B irradiation on engraftment, graft-versus-host disease and graft-versus-leukemia effect in a rat model for allogeneic bone marrow transplantation. Bone Marrow Transplantation, 21, 801-807.
van Weering, D. H., Moen, T. C., Braakman, L. J., Baas, P. D., & Bos, J. L. (1998). Expression of the receptor kinase Ret on the plasma membrane is dependent on extracellular calcium. Journal of Biological Chemistry, 273(20), 12077-12081.
Hettema, E. H., Ruigrok, C. C., Koerkamp, M. G., van den Berg, M., Tabak, H. F., Distel, B., & Braakman, L. J. (1998). The cytosolic Dna-J-like protein djp1p is involved specifically in peroxisomal protein import. Journal of Cell Biology, 142(2), 421-434.

1997

Wetenschappelijke publicaties

Zhang, J. X., Braakman, L. J., Matlack, K. E., & Helenius, A. (1997). uality control in the secretory pathway: the role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations. Molecular Biology of the Cell, 8(10), 1943-1954.

1995

Wetenschappelijke publicaties

Chen, W., Helenius, J., Braakman, L. J., & Helenius, A. (1995). Cotranslational folding and calnexin binding during glycoproteins synthesis. Proceedings of the National Academy of Sciences of the United States of America, 92(14), 6229-6233.

1994

Wetenschappelijke publicaties

Hammond, C., Braakman, I., & Helenius, A. (1994). Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proceedings of the National Academy of Sciences of the United States of America, 91(3), 913-917. https://doi.org/10.1073/pnas.91.3.913
Hammond, C., Braakman, L. J., & Helenius, A. (1994). Role of the N-linked oligosaccharide recognition, glucose trimming, and calnexin in glyco-protein folding and quality control. Proceedings of the National Academy of Sciences of the United States of America, 91(3), 913-917.

1993

Wetenschappelijke publicaties

De Silva, A., Braakman, I., & Helenius, A. (1993). Posttranslational folding of vesicular stomatitis virus G protein in the ER: Involvement of noncovalent and covalent complexes. Journal of Cell Biology, 120(3), 647-655. https://doi.org/10.1083/jcb.120.3.647
Tatu, U., Braakman, L. J., & Helenius, A. (1993). Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells. EMBO Journal, 12(5), 2151-2157.
da Silva, A., Braakman, L. J., & Helenius, A. (1993). The endoplasmic reticulum as a protein-folding compartment. Journal of Cell Biology, 120(3), 647-655.

1992

Wetenschappelijke publicaties

Braakman, I., Helenius, J., & Helenius, A. (1992). Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature, 356(6366), 260-262. https://doi.org/10.1038/356260a0
Helenius, A., Marquardt, T., & Braakman, L. J. (1992). The endoplasmic reticulum as a protein-folding compartment. Trends in Cell Biology, 2(8), 227-231.
Braakman, L. J., Helenius, J., & Helenius, A. (1992). Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. Nature, 356(6366), 260-262.

1991

Wetenschappelijke publicaties

Braakman, I., Keij, J., Hardonk, M. J., Meijer, D. K., & Groothuis, G. M. (1991). Separation of periportal and perivenous rat hepatocytes by fluorescence-activated cell sorting: confirmation with colloidal gold as an exogenous marker. Hepatology, 13(1), 73-82. https://pubmed.ncbi.nlm.nih.gov/1988347/
Braakman, L. J., Hoover-Litty, H., Wagner, K. R., & Helenius, A. (1991). Folding of influenza hemagglutinin in the endoplasmic reticulum. Journal of Cell Biology, 114(3), 401-411.
Braakman, L. J., Keij, J., Hardonk, M. J., Meijer, D. K., & Groothuis, G. M. (1991). Separation of hepatocytes of different acinar zones by flow cytometry. Hepatology, 13(1), 73-82.

1989

Wetenschappelijke publicaties

Thalhammer, T., Gessl, A., Braakman, I., & Graf, J. (1989). Separation of hepatocytes of different acinar zones by flow cytometry. Cytometry, 10(6), 772-778. https://doi.org/10.1002/cyto.990100615
Braakman, L. J., Groothuis, G. M., & Meijer, D. K. (1989). Zonal compartmentation of perfused rat liver: plasma reappearance of rhodamine B explained. Journal of Pharmacology and Experimental Therapeutics, 249(3), 869-873. https://pubmed.ncbi.nlm.nih.gov/2732948/
Braakman, L. J., Verest, O., Pijning, T., Meijer, D. K., & Groothuis, G. M. (1989). Zonal distribution of the cation lucigenin in the rat liver: influence of taurocholate. Molecular Pharmacology, 36(4), 532-536.
Thalhammer, T., Gessl, A., Braakman, L. J., & Graf, J. (1989). Separation of hepatocytes of differen acinar zones by flow cytometry. Cytometry, 10(6), 772-778.
Braakman, L. J., Pijning, T., Verest, O., Weert, B., Meijer, D. K., & Groothuis, G. M. (1989). Vesicular uptake system for the cation lucigenin in the rat hepatocyte. Molecular Pharmacology, 36(4), 537-542.

1988

Wetenschappelijke publicaties

van der Sluijs, P., Braakman, I., Meijer, D. K., & Groothuis, G. M. (1988). Heterogeneous acinar localization of the asialoglycoprotein internalization system in rat hepatocytes. Hepatology, 8(6), 1521-1529. http://10.1002/hep.1840080609

1987

Wetenschappelijke publicaties

Braakman, I., Groothuis, G. M., & Meijer, D. K. (1987). Acinar redistribution and heterogeneity in transport of the organic cation rhodamine B in rat liver. Hepatology, 7(5), 849-855. https://doi.org/10.1002/hep.1840070510

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