{"id":101,"date":"2019-11-05T10:02:34","date_gmt":"2019-11-05T09:02:34","guid":{"rendered":"http:\/\/sagoebel.de\/UngermannLab\/Version_B\/?p=101"},"modified":"2025-08-12T14:58:13","modified_gmt":"2025-08-12T12:58:13","slug":"publications","status":"publish","type":"post","link":"https:\/\/www.biochemie.uni-osnabrueck.de\/?p=101","title":{"rendered":"Publications"},"content":{"rendered":"

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PUBLICATIONS<\/h2>\n\n\n\n
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For pdf files, please check Pubmed (by typing in \u201cUngermann-C\u201d) or contact cu@uos.de<\/a><\/em>
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a) Original publications<\/strong><\/h3>\n\n\n\n

(* co-corresponding; # shared first authorship; Reviews found at end under b)<\/a><\/strong><\/h4>\n\n\n\n

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202<\/strong>5<\/h3>\n\n\n\n
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G\u00f3mez-S\u00e1nchez R, Chumpen Ramirez S, Vargas Duarte P, Hu Y, Mari M, Olschewski K, Hardenberg R, Fromme JC, Ungermann C<\/strong>*, Reggiori F* (2025) Establishment of the phagophore-ERES membrane contact site initiates phagophore elongation. Nature Struct Mol Biol, in press, doi: 10.1038\/s41594-025-01621-6<\/p>\n\n\n\n

Gao J*, Rocha C, Franzkoch R, Psathaki OK, Hensel M, Vanni S, Ungermann C*<\/strong> (2025) Any1 is a phospholipid lipid scramblase involved in endosome biogenesis. J Cell Biol 224:e202410013<\/p>\n\n\n\n

K\u00f6nig C, Shvarev D, Gao J, Haar E, Susan N, Auffarth K, Langemeyer L, Moeller A*, Ungermann C*<\/strong> (2025) Vps41 functions as a molecular ruler for HOPS tethering complex-mediated membrane fusion. J Cell Sci 138: jcs263788<\/p>\n\n\n\n

2024<\/strong><\/h3>\n\n\n\n
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Shvarev D**, K\u00f6nig C**, Susan N**, Langemeyer L, Walter S, Perz A, Fr\u00f6hlich F,\u00a0Ungermann C<\/strong>, Moeller A (2024) Structure of the endosomal CORVET tethering complex. Nat. Commun 15:5227\u00a0<\/p>\n\n\n\n

F\u00fcllbrunn N, Nicastro R, Mari M, Griffith J, Herrmann E, Rasche R, Borchers AC, Auffarth K, K\u00fcmmel D, Reggiori F, De Virgilio C, Langemeyer L, Ungermann C<\/strong> (2023) The GTPase activating protein Gyp7 regulated Rab7\/Ypt7 on late endosomes. J Cell Biol 223:e202305038<\/p>\n\n\n\n

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2023<\/strong><\/h3>\n\n\n\n
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\nZhang S, Tong M, Zheng D, Huang H, Li L, , Ungermann C<\/strong> , Pan Y, Luo H, Lei M, Tang Z, Fu W, Chen S, Liu X, Zhong Q (2023) C9orf72 -catalyzed GTP loading of Rab39A enables HOPS-mediated membrane tethering and fusion in mammalian autophagy. Nat. Commun 14: 6360
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\nGrziwa S, Sch\u00e4fer JH, Nicastro R, Arens A, De Virgilio C, Fr\u00f6hlich F, Moeller A, Gao J, Langemeyer L, , Ungermann C*<\/strong> (2023) Yck3 casein kinase-mediated phosphorylation determines Ivy1 localization and function at endosomes and vacuole. J Cell Sci 136: jcs260889
<\/p>\n\nHerrmann E**, Sch\u00e4fer JH**, Wilmes D, , Ungermann C<\/strong> , Moeller A*, K\u00fcmmel D* (2023) Structure of the metazoan Rab7 GEF complex Mon1-Ccz1-Bulli. PNAS 130: e2301908120\nArlt H, Raman B, Filali-Mouncef Y, Hu Y, Leytens A, Hardenberg R, Guimar\u00e3es R, Kriegenburg F, Mari M, Smaczynska-de Rooij II, Ayscough KR, Dengjel J, Ungermann C, Reggiori F (2023) The dynamin Vps1 mediates Atg9 transport to the sites of autophagosome formation. J Biol Chem 299: 104712
<\/p>\n\nBorchers AC, Janz M, Sch\u00e4fer JH, Moeller A, K\u00fcmmel D, Paululat A, , Ungermann C*<\/strong> , Langemeyer, L* (2023) Regulatory sites in the Mon1-Ccz1 complex controle Rab5 to Rab7 transition and endosome maturation. PNAS 130: e2303750120
<\/p>\n\nChumpen Ramirez S**, G\u00f3mez-S\u00e1nchez R**, Verlhac P, Hardenberg R, Margheritis E, Cosentino K, Reggiori F*, , Ungermann C*<\/strong> (2023) Atg9 interactions via its transmembrane domains are required for phagophore expansion during autophagy. Autophagy 19:1459-1478.
<\/p>\n\nHerrmann E, Langemeyer L, Auffarth K, , Ungermann C<\/strong> , K\u00fcmmel D (2023) Targeting of the Mon1-Ccz1 Rab guanine nucleotide exchange factor to distinct organelles by a synergistic protein and lipid code. J Biol Chem 299: 102915.
<\/p>\n\nDeprez MA, Caligaris M, Rosseels J, Hatakeyama R, Ghillebert R, Sampaio-Marques B, Mudholkar K, Eskes E, Meert E, , Ungermann C<\/strong> , Ludovico P, Rospert S, De Virgilio C, Winderickx J (2023) The nutrient-responsive CDK Pho85 primes the Sch9 kinase for its activation by TORC1. Plos Genetics 19: e1010641.\n
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2022<\/strong><\/h3>\n\n\n\n
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\nChumpen Ramirez S#, G\u00f3mez-S\u00e1nchez R#, Verlhac P, Hardenberg R, Margheritis E, Cosentino K, Reggiori F*,, Ungermann C*<\/strong> (2022) Atg9 interactions via its transmembrane domains are required for phagophore expansion during autophagy. Autophagy, in press
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\nShvarev D#, Schoppe J#, K\u00f6nig C#, Perz A, F\u00fcllbrunn N, Kiontke S, Langemeyer L, Januliene D, Schnelle K, K\u00fcmmel D, Fr\u00f6hlich F, Moeller A*,  Ungermann C*<\/strong> (2022) Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery. elife 11:e80901
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\nGao J, Nicastro R, P\u00e9li-Gulli MP, Grziwa S, Chen Z, Kurre R, Piehler J, De Virgilio C, Fr\u00f6hlich F,  Ungermann C*<\/strong>  (2022) The HOPS tethering complex is required to maintain signaling endosome identity and TORC1 activity. J Cell Biol 221, e2021109084
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\nVargas Duarte P, Hardenberg R, Mari M, Walter S, Reggiori F, Fr\u00f6hlich F, Gonz\u00e1lez Montoro A*, Ungermann C*<\/strong>  (2022) The yeast LYST homolog Bph1 is a Rab5 effector and prevents Atg8 lipidation at endosomes. J Cell Sci, 135, jcs259241
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\nEising S, Esch B, W\u00e4lte M, Vargas Duarte P, Walter S,  Ungermann C<\/strong> , Bohnert M, Fr\u00f6hlich F (2022) A lysosomal biogenesis map reveals the cargo spectrum of yeast vacuolar protein targeting pathways. J Cell Biol 221: e2021107148
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\nKlink BU, Herrmann E, Antoni C, Langemeyer L, Kiontke S, Gatsogiannis C,  Ungermann C<\/strong> , Rauner S, K\u00fcmmel D (2022) Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation. Proc Natl Acad Sci USA, 119: e2121494119
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\nDanial JSH, Quintana Y, Ros U, Shalaby R, Marghertis EG, Chumpen Ramirez S,  Ungermann C<\/strong> , Garcia-Saez AJ, Cosentino C (2022) J Phys Chem Lett 13, 822-829
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2021<\/strong><\/h3>\n\n\n\n
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Schoppe J#, Schubert E#, Apelbaum A, Yavavli E, Birkholz O, Stephanowitz H, Han Y, Perz A, Hofnagel O, Liu F, Piehler J, Raunser S*,, Ungermann C*<\/strong>  (2021) Flexible open conformation of the AP-3 complex explains its role in cargo recruitment at the Golgi. J Biol Chem, in press
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Fitzian K, Gonz\u00e1lez Montoro A *, #, Duarte PV #, Auffarth K, Walter S, Fr\u00f6hlich F, Ungermann C*<\/strong>  (2021) Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole. Mol Biol Cell, 32:br14
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Fitzian K, Br\u00fcckner A, Broh\u00e9e L, Zech R, Antoni C, Kiontke S, Gasper R, Linard Matos AL, Beel S, Wilhelm S, Gerke V, , Ungermann C*<\/strong> , Nellist M, Raunser S, Demetriades C, Oeckinghaus A, K\u00fcmmel D (2021) TSC1 binding to lysosomal PIPs is required for TSC complex translocation and mTORC1 regulation. Mol Cell 81, 2705-2721
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F\u00fcllbrunn N #, Li Z #, Jorde L, Richter CP, Kurre R, Langemeyer L, Yu C, Meyer C, Enderlein J , Ungermann C*<\/strong> , Piehler J*, You C* (2021) Nanoscopic anatomy of dynamic multi-protein complexes at membranes resolved by graphene-induced energy transfer. elife 10, e62591
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Chen Z #, Malia PC #, Hatakeyama R, Nicastro R, Hu Z, Peli-Gulli MP, Gao J, Nishimura T, Eskes E, Stefan CJ, Winderickx J, Dengjel J, De Virgilio C* , Ungermann C*<\/strong> (2021) TORC1 determines Fab1 signaling function at signaling endosomes and vacuoles. Current Biology, 31, 297-309
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2020<\/strong><\/h3>\n\n\n\n
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Gao J, Kurre R, Rose J, Walter S, Fr\u00f6hlich F, Piehler J, Reggiori F, Ungermann C<\/strong> (2020) Function of the SNARE Ykt6 on autophagosomes requires the Dsl complex and the Atg1 kinase complex. EMBO Reports, 21, e50733.
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Langemeyer L, Borchers, A-C, Hermann, E, F\u00fcllbrunn, N, Han, Y, Perz, A, Auffarth, K, K\u00fcmmel D, Ungermann C<\/strong> (2020) A conserved and regulated mechanism drives endosomal Rab transition. elife, 9, p191
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Schoppe J, Mari M, Yavavli E, Auffarth K, Cabrera M, Walter S, Fr\u00f6hlich F, D, Ungermann C<\/strong> (2020) AP-3 vesicle uncoating occurs after HOPS-dependent tethering. EMBO J, e105117
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Dehnen, L, Janz M, Verma JK, Psathaki OE, Langemeyer L, Fr\u00f6hlich F, D, Ungermann C*<\/strong> , Paululat A* (2020) A trimeric metazoan Rab7 GEF complex is crucial for endocytosis and scavenger function. J Cell Sci, 133, 13, jcs 247080
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2018<\/strong><\/h3>\n\n\n\n
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Gao J, Reggiori F, Ungermann C<\/strong> (2018) A novel in vitro assay reveals SNARE topology and the role of Ykt6 in autophagosome fusion with vacuoles. J Cell Biol, in doi: 10.1083\/jcb.201804039
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Ma M, Kumar S, Purushothaman L, Babst M, Ungermann<\/strong> C, Chi RJ, Burd CG (2018) Lipid trafficking by yeast Snx4 family SNX-BAR proteins promote autophagy and vacuole membrane fusion. Mol Biol Cell, in press, doi: 10.1091\/mbc.E17-12-0743
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Gonz\u00e1lez-Montoro A*, Auffarth K, H\u00f6nscher C, Bohnert M, Becker T, Warscheid B, Reggiori F, van der Laan M, Fr\u00f6hlich F, Ungermann C*<\/strong> (2018). Vps39 interacts with Tom40 to establish one of two functionally distinct vacuole-mitochondria contact sites. Dev Cell 45, 621-637 (*co-corresponding)
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G\u00f3mez-S\u00e1nchez R, Rose J, Guimar\u00e3es R, Mari M, Papinski D, Rieter E, Geerts WJ, Hardenberg R, Kraft C, Ungermann C*<\/strong>, Reggiori F* (2018). Atg9 establishes Atg2-dependent contact sites between the ER and phagophores. J Cell Biol, in press (*co-corresponding)
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Malia PC, Numrich J, Nishimura T, Gonz\u00e1lez-Montoro A, Stefan CJ, Ungermann C<\/strong> (2018) Control of vacuole membrane homeostasis by a resident PI-3,5-kinase inhibitor. PNAS 115, 4684-4689.
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Gao J, Langemeyer L, K\u00fcmmel D, Reggiori F, Ungermann C<\/strong> (2018). Molecular mechanism to target the endosomal Mon1-Ccz1 GEF complex to the pre-autophagosomal structure. eLife 7, 765.
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Langemeyer L, Perz A, K\u00fcmmel D, Ungermann C<\/strong> (2018) A guanine nucleotide exchange factor (GEF) limits Rab GTPase driven membrane fusion. J Biol Chem 293, 731\u2013739.<\/p>\n\n\n\n \n\n\n\n

2017<\/strong><\/h3>\n\n\n\n
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D\u2019Agostino M, Risselada HJ, L\u00fcrick A, Ungermann C<\/strong>, Mayer A (2017) A tethering complex drives the terminal stage of membrane fusion. Nature 551, 634-638.
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Sanchez-Wandelmer J, Kriegenburg F, Rohringer S, Schuschnig M, G\u00f3mez-S\u00e1nchez R, Zens B, Abreu S, Hardenberg R, Hollenstein D, Gao J, Ungermann C<\/strong>, Martens S, Kraft C, Reggiori F (2017) Nature commun 8, 295. doi: 10.1038\/s41467-017-00302-3
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Puroshothaman LK #, Arlt H*, #, Kuhlee A, Raunser S, Ungermann C*<\/strong> (2017) Retromer-driven membrane tubulation separates endosomal recycling from Rab7\/Ypt7-dependent fusion. Mol Biol Cell 28, 783-791
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L\u00fcrick A, Gao J, Kuhlee A, Yavavli E, Langemeyer L, Perz A, Raunser S, Ungermann C<\/strong> (2017) Multivalent Rab interactions determine tether-mediated membrane fusion. Mol Biol Cell 28, 322-332.
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Kiontke S, Langemeyer L, Kuhlee A, Schuback S, Rauner S, Ungermann C<\/strong>, K\u00fcmmel D (2017) Architecture and mechanism of the late endosomal Ypt7\/Rab7 guanine nucleotide exchange factor complex Mon1-Ccz1. Nat Commun, 8:14034. doi: 10.1038\/ncomms14034.<\/p>\n\n\n\n \n\n\n\n

2016<\/strong><\/h3>\n\n\n\n
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Kock C, Arlt H, Ungermann C<\/strong>, Heinisch JJ (2016) Yeast cell wall integrity sensors form specific plama membrane microdomains important for signaling. Cell Microbiol 18, 1251-67.
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Klionsky DJ et al. (2016) Guidelines for the use and interpretation of assays monitoring autophagy (3rd edition). Autophagy 12, 1-222.<\/p>\n\n\n\n \n\n\n\n

2015<\/strong><\/h3>\n\n\n\n
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Edvardson S, Gerhard F, Jalas C, Lachmann J, Golan D, Rivas M , Shaag A, Ungermann C<\/strong>, Orly E (2015) Hypomyelination and developmental delay associated with VPS11 mutation in Ashkenazi-Jewish patients. J Med Gen 52, 749-753.
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Rana M, Lachmann J, Ungermann C <\/strong>(2015) Identification of a Rab GAP cascade that controls recycling of the Rab5 GTPase Vps21 from the vacuole. Mol Biol Cell 26, 2535-49.
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Numrich J, P\u00e9li-Gulli MP, Arlt H, Sardu A, Griffith J, Levine T, Engelbrecht-Vandr\u00e9 S, Reggiori F, DeVirgilio C, Ungermann C <\/strong>(2015) The I-BAR protein Ivy1 is an effector of the Rab7 GTPase Ypt7 involved in vacuole membrane homeostasis. J Cell Sci 128, 2278-92.
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L\u00fcrick A, Kuhlee A, Br\u00f6cker C, Raunser S, Ungermann C<\/strong> (2015) The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion. J Biol Chem 9, 5405-5413.
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Arlt H, Reggiori F, Ungermann C <\/strong>(2015) The retromer complex cooperates with the dynamic Vps1 in the retrieval of transmembrane proteins from the vacuole. J Cell Sci 128, 645-655.
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Arlt H, Auffarth K, Kurre R, Lisse D, Piehler J, Ungermann C<\/strong> (2015) Spatio-temporal dynamics of membrane remodeling and fusion proteins during endocytic transport. Mol Biol Cell 26, 1357-1370.
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Wetzel J, Herrmann S, Swapna LS, Prusty D, Peter AT, Kono M, Saini S, Nellimarla S, Wong TW, Wilcke L, Ramsay O, Cabrera A, Biller L, Heincke D, Mossman K, Spielmann T, Ungermann C<\/strong>, Parkinson J, Gilberger TW (2015) The role of palmitoylation for protein recruitment to the inner membrane complex of the malaria parasite. J Biol Chem 290, 1712-1728.<\/p>\n\n\n\n \n\n\n\n

2014<\/strong><\/h3>\n\n\n\n
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Behrmann H, L\u00fcrick A, Kuhlee A, Balderhaar HK, Br\u00f6cker C, K\u00fcmmel D, Engelbrecht-Vandr\u00e9 S, Gohlke U, Raunser S, Heinemann U*, Ungermann C<\/strong>* (2014) Structural identification of the Vps18 \u03b2\u2212propeller reveals a critical role in the HOPS complex stability and function. J Biol Chem 289, 33503-33512. (*co-corresponding)
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Auffarth K, Arlt H, Lachmann J, Cabrera M, Ungermann C<\/strong> (2014) Tracking of the dynamic localization of the Rab-specific HOPS subunits reveal their distinct interaction with Ypt7 and vacuoles. Cell Logist 4, e29191.
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H\u00f6nscher C, Mari M, Auffarth K, Bohnert M, Griffith J, Geerts W, van der Laan M, Cabrera M, Reggiori F, Ungermann C<\/strong>  (2014) Cellular metabolism regulates contact sites between vacuoles and mitochondria. Dev Cell 30, 86-94
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Lawrence G, Brown CC, Flood BA, Karunakaran S, Cabrera M, Nordmann M, Ungermann C<\/strong>, Fratti RA (2014) Dynamic association of the PI3P-interacting Mon1-Ccz1 GEF with vacuoles is controlled through its phosphorylation by the type-1 casein kinase Yck3. Mol Biol Cell 25, 1608-1619.
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Cabrera M, Nordmann M, Perz A, Schmedt D, Gerondopoulos A, Barr F, Piehler J, Engelbrecht-Vandr\u00e9 S, Ungermann C<\/strong> (2014) The Mon1-Ccz1 GEF activates the Rab7 GTPase Ypt7 via a longin-fold-Rab interface and association with PI3P-positive membranes. J Cell Sci 127, 1043-51.
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Lachmann J, Glaubke E, Moore PS, Ungermann C<\/strong> (2014) The Vps39-like TRAP1 is an effector of Rab5 and likely the missing Vps3 subunit of human CORVET. Cell Logistics 4, e970840.<\/p>\n\n\n\n \n\n\n\n

2013<\/strong><\/h3>\n\n\n\n
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Guo Z, Johnston W, Kovtun O, Mureev S, Br\u00f6cker C, Ungermann C<\/strong>, Alexandrov K (2013) Subunit organization of in vitro reconstituted HOPS and CORVET multisubunit membrane tethering complexes. PLoS One 8, e81534
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Cabrera M, Ungermann C<\/strong>  (2013). Guanine nucleotide exchange factors (GEFs) have a critical but not exclusive role in organelle localization of Rab GTPases. J Biol Chem 288, 28704\u201328712.
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Guo Z, Johnston W, Kovtun O, Mureev S, Br\u00f6cker C, Ungermann C<\/strong> , and Alexandrov K (2013). Subunit Organisation of In Vitro Reconstituted HOPS and CORVET Multisubunit Membrane Tethering Complexes. PLoS ONE, 8, e81534.
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Epp N, Ungermann C<\/strong>  (2013). The N-Terminal Domains of Vps3 and Vps8 Are Critical for Localization and Function of the CORVET Tethering Complex on Endosomes. PLoS ONE 8, e67307.
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kleine Balderhaar H, Lachmann J, Yavavli E, Br\u00f6cker C, L\u00fcrick A, Ungermann C<\/strong>  (2013) The CORVET tethering complex promotes tethering and fusion of Rab5\/Vps21-positive membranes. PNAS 110, 3823-8.
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John Peter AT, Lachmann J, Rana M, Bunge M, Cabrera M*, Ungermann C<\/strong>* (2013) The evolutionarily conserved BLOC-1 complex controls endosomal maturation by recruiting the Rab5 GTPase activating protein Msb3. J Cell Biol 201, 97-111. (*co-corresponding)
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Cabrera M, Arlt H, Epp N, Lachmann J, Griffith J, Perz A, Reggiori F, Ungermann C<\/strong> (2013) Functional separation of endosomal fusion factors and the CORVET tethering complex in endosomal biogenesis. J Biol Chem, 288, 5166-75.
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Rieter E, Vinke F, Bakula D, Cebollero E, Ungermann C<\/strong>, Projkas-Cezanne T, Reggiori F (2013) Atg18 function in autophagy is regulated by specific sites within its \uf062-propeller. J Cell Sci 126, 593-604<\/p>\n\n\n\n \n\n\n\n

2012<\/strong><\/h3>\n\n\n\n
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Cabrera A, Herrmann S, Warszta D, Santos JM, John Peter AT, Kono M, Debrouver S, Jacobs T, Spielmann T, Ungermann C<\/strong>, Soldati-Favre D, and Gilberger TW (2012) Dissection of the minimal sequence requirements for rhoptry membrane targeting in the malaria parasite. Traffic 13, 1335-50.
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Bonfils G, Jaquenoud M, Bontron S, Ostrowicz C, Ungermann C<\/strong>, and De Virgilio C (2012) Leucyl-tRNA synthetase controls TORC1 via the EGO complex. Mol Cell 46, 105-110.
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Lachmann J, Barr FA, Ungermann C<\/strong> (2012) The Msb3\/Gyp3 GAP controls the activity of the Rab GTPases Vps21 and Ypt7 at endosomes and vacuoles. Mol Biol Cell 23, 2516-26.
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Br\u00f6cker C, Kuhlee A, Gatsogiannis C, kleine Balderhaar H, H\u00f6nscher C, Engelbrecht-Vandr\u00e9 S, Ungermann C<\/strong>*, and Raunser S* (2012) Molecular architecture of the HOPS tethering complex. PNAS 109, 1991-1996 (*co-corresponding)<\/p>\n\n\n\n \n\n\n\n

2011<\/strong><\/h3>\n\n\n\n
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Kama R, Kanneganti V, Ungermann C<\/strong>, and Gerst JE (2011) The yeast Batten disease orthologue Btn1 controls endosome-Golgi retrograde transport via SNARE assembly. J Cell Biol 195, 203-215.
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Arlt H, Perz A, Ungermann C<\/strong> (2011) An overexpression screen in Saccharomyces cerevisiae identifies novel genes that affect endocytic protein trafficking. Traffic 12, 1592-1603.
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Kr\u00e4mer L, Ungermann C<\/strong> (2011) HOPS drives vacuole fusion by binding the vacuole SNARE complex and the Vam7 PX domain via two distinct sites. Mol Biol Cell 22, 2601-2611.
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Meiringer CT, Rethmeier R, Auffarth K, Wilson J, Perz A, Barlowe C, Schmitt HD, and Ungermann C<\/strong> (2011) The Dsl1 tethering complex is a resident ER complex, which interacts with five snares – implications for fusion and fusion regulation. J Biol Chem 286, 25039-46.<\/p>\n\n\n\n \n\n\n\n

2010<\/strong><\/h3>\n\n\n\n
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Cabrera M #, Langemeyer L #, Mari M, Rethmeier R, Orban I, Perz A, Br\u00f6cker C, Griffith J, Klose D, Steinhoff HJ, Reggiori F, Engelbrecht-Vandr\u00e9 S*, Ungermann C<\/strong>* (2010) Phosphorylation of a membrane curvature\u2013sensing motif switches function of the HOPS subunit Vps41 in membrane tethering. J Cell Biol 191, 845-859. (*co-corresponding)
<\/p>\n\n\n\n

kleine Balderhaar H, Arlt H, Ostrowicz CW, Br\u00f6cker C, S\u00fcndermann F, Brandt R, Babst M, Ungermann C<\/strong> (2010) The Rab GTPase Ypt7 is linked to retromer-mediated receptor recycling and fusion at the yeast late endosome. J Cell Sci 123, 4085-94.
<\/p>\n\n\n\n

Nordmann M, Cabrera M, Perz A, Br\u00f6cker C, Ostrowicz CW, Engelbrecht-Vandr\u00e9 S, Ungermann C<\/strong> (2010) The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7. Curr Biol 20, 1654-59.<\/p>\n\n\n\n \n\n\n\n

2009<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Markgraf D, Peplowska K, Mari M, Griffith J, Reggiori F*, Ungermann C<\/strong>* (2009) Direct interaction of the CORVET subunit Vps8 and the Rab5 GTPase Vps21 tethers late endosomal compartments. Mol Biol Cell 20, 5276-5289. (*co-corresponding)
<\/p>\n\n\n\n

Hou H, John Peter AT, Meiringer C, Subramanian K, Ungermann C<\/strong> (2009) Sorting of palmitoylated proteins in a network of DHHC acyltransferases with overlapping specificity. Traffic 10, 1061-73.
<\/p>\n\n\n\n

Cabrera M, Ostrowicz CW, Mari M, LaGrassa T, Reggiori F, Ungermann C<\/strong> (2009). Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites. Mol Biol Cell 20, 1937-48.<\/p>\n\n\n\n \n\n\n\n

2008<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Meiringer C, Auffarth K, Hou H, Ungermann C<\/strong>  (2008). Depalmitoylation of the SNARE Ykt6 prevents its entry into the multivesicular body pathway. Traffic 9, 1511-21.
<\/p>\n\n\n\n

Takeda K, Cabrera M, Rohde J, Bausch D, Jensen ON, Ungermann C<\/strong> (2008) The vacuolar V(1)\/V(0)-ATPase is involved in the release of the HOPS subunit Vps41 from vacuoles vacuole fragmentation and fusion. FEBS Lett, 582, 1558-63.
<\/p>\n\n\n\n

Pylypenko O, Sch\u00f6nichen A, Ludwig D, Ungermann C<\/strong>, Goody RS, Rak A, Geyer M (2008), Farnesylation of the SNARE protein Ykt6 increases ist stability and helical folding. J Mol Biol 377, 1334-45.<\/p>\n\n\n\n \n\n\n\n

2007<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Peplowska C, Markgraf DM, Ostrowicz CF, Bange G, Ungermann C<\/strong> (2007) The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev Cell 12, 739-750. <\/p>\n\n\n\n \n\n\n\n

2006<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Hofmann M, Peplowska K, Rohde J, Poschner BC, Ungermann C<\/strong>, Langosch D (2006) Self-interaction of a SNARE transmembrane domain promotes hemifusion-to-fusion transition. J Mol Biol 346, 1048-1060.
<\/p>\n\n\n\n

Roy R, Peplowka K, Rohde J, Ungermann C<\/strong>, Langosch D (2006) Role of the Vam3p transmembrane segment in homodimerization and SNARE complex formation, Biochemistry 45, 7654-7660.
<\/p>\n\n\n\n

Subramanian K, Dietrich LE, Hou H, LaGrassa C, Meiringer C, Ungermann C<\/strong> (2006) Palmitoylation determines the function of Vac8 at the yeast vacuole. J Cell Sci 119, 2477-2485.
<\/p>\n\n\n\n

Meiringer CT, Ungermann C<\/strong> (2006) Probing protein palmitoylation at yeast vacuoles, Methods 40, 171-176.<\/p>\n\n\n\n \n\n\n\n

2005<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Hou H, Subramanian K, LaGrassa TJ, Markgraf D, Dietrich LE, Decker N, Ungermann C<\/strong>   (2005) The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8. PNAS 102, 17366-17371.
<\/p>\n\n\n\n

Dietrich LE, LaGrassa TJ, Rohde J, Cristodero M, Meiringer CT, Ungermann C<\/strong> (2005), ATP-independent control of Vac8 palmitoylation by a SNARE sub-complex on yeast vacuoles. J Biol Chem 280, 15348-55.
<\/p>\n\n\n\n

Dietrich LE, Peplowska K, LaGrassa T, Rohde J, Ungermann C<\/strong> (2005) The SNARE Ykt6 is released from yeast vacuoles during an early stage of fusion. EMBO Rep 6, 245-250.
<\/p>\n\n\n\n

LaGrassa T, Ungermann C<\/strong> (2005) The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex. J Cell Biol 168, 401-414.
<\/p>\n\n\n\n

Peplowska K, Ungermann C<\/strong> (2005) Expanding dynamin: from fission to fusion. Nat Cell Biol 7, 103-104.<\/p>\n\n\n\n

2006<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Hofmann M, Peplowska K, Rohde J, Poschner BC, Ungermann C<\/strong>, Langosch D (2006) Self-interaction of a SNARE transmembrane domain promotes hemifusion-to-fusion transition. J Mol Biol 346, 1048-1060.
<\/p>\n\n\n\n

Roy R, Peplowka K, Rohde J, Ungermann C<\/strong>, Langosch D (2006) Role of the Vam3p transmembrane segment in homodimerization and SNARE complex formation, Biochemistry 45, 7654-7660.
<\/p>\n\n\n\n

Subramanian K, Dietrich LE, Hou H, LaGrassa C, Meiringer C, Ungermann C<\/strong> (2006) Palmitoylation determines the function of Vac8 at the yeast vacuole. J Cell Sci 119, 2477-2485.
<\/p>\n\n\n\n

Meiringer CT, Ungermann C<\/strong> (2006) Probing protein palmitoylation at yeast vacuoles, Methods 40, 171-176.<\/p>\n\n\n\n \n\n\n\n

2005<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Hou H, Subramanian K, LaGrassa TJ, Markgraf D, Dietrich LE, Decker N, Ungermann C<\/strong>   (2005) The DHHC protein Pfa3 affects vacuole-associated palmitoylation of the fusion factor Vac8. PNAS 102, 17366-17371.
<\/p>\n\n\n\n

Dietrich LE, LaGrassa TJ, Rohde J, Cristodero M, Meiringer CT, Ungermann C<\/strong> (2005), ATP-independent control of Vac8 palmitoylation by a SNARE sub-complex on yeast vacuoles. J Biol Chem 280, 15348-55.
<\/p>\n\n\n\n

Dietrich LE, Peplowska K, LaGrassa T, Rohde J, Ungermann C<\/strong> (2005) The SNARE Ykt6 is released from yeast vacuoles during an early stage of fusion. EMBO Rep 6, 245-250.
<\/p>\n\n\n\n

LaGrassa T, Ungermann C<\/strong> (2005) The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex. J Cell Biol 168, 401-414.
<\/p>\n\n\n\n

Peplowska K, Ungermann C<\/strong> (2005) Expanding dynamin: from fission to fusion. Nat Cell Biol 7, 103-104.<\/p>\n\n\n\n \n\n\n\n

2004<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Faergeman N, Feddersen S, Christiansen JK, Larsen MK, Schneiter R, Ungermann C<\/strong>, Mutenda, K., Roepstorff, P., and Knudsen, J. (2004)  Acyl-CoA-binding protein, Acb1p, is required for normal vacuole function and ceramide synthesis in Saccharomyces cerevisiae. Biochem J 380, 907-918.
<\/p>\n\n\n\n

Dietrich LE, Gurezka R, Veit M, Ungermann C<\/strong> (2004) The SNARE Ykt6 mediates protein palmitoylation during an early stage of yeast vacuole fusion. EMBO J 23, 45-53.<\/p>\n\n\n\n \n\n\n\n

2003<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Veit M, Dietrich LE, Ungermann C<\/strong> (2003) Biochemical characterization of the vacuolar palmitoyl acyltransferase. FEBS letters 540, 101-105.
<\/p>\n\n\n\n

Rohde J, Dietrich L, Langosch D, Ungermann C<\/strong> (2002) The transmembrane domain of Vam3 affects the composition of cis- and trans-SNARE complexes in homotypic vacuole fusion. J. Biol. Chem. 278, 1656-1662.<\/p>\n\n\n\n \n\n\n\n

2002<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Boeddinghaus C, Merz AJ, Laage R, Ungermann C<\/strong> (2002) A cycle of Vam7p release from and PtdIns-3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion. J Cell Biol 157, 79-89. <\/p>\n\n\n\n \n\n\n\n

2001<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Laage R, Ungermann C<\/strong> (2001) The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion. Mol Biol Cell 12, 3375-3385.
<\/p>\n\n\n\n

Veit M, Laage R, Dietrich L, Wang L, Ungermann C<\/strong> (2001) Vac8p-release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion. EMBO J 20, 3145-3155.
<\/p>\n\n\n\n

Takita Y, Engestrom L, Ungermann C<\/strong>, and Cunningham KW (2001) Inhibition of the Ca2+-ATPase Pmc1p by the v-SNARE protein Nyv1p. J Biol Chem 276, 6200-6206.<\/p>\n\n\n\n \n\n\n\n

2000<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Ungermann C<\/strong>, Price A, Wickner W (2000) A new role for a SNARE protein as a regulator of the Ypt\/Rab-dependent stage of docking. PNAS 97, 8889-8891.
<\/p>\n\n\n\n

Wang L, Ungermann C<\/strong>, and Wickner W (2000) The docking of primed vacuoles can be reversibly arrested  by excess Sec17p (a-SNAP). J Biol Chem 275, 22862-22867.
<\/p>\n\n\n\n

Price AE, Wickner W, Ungermann C<\/strong> (2000) Proteins needed for vesicle budding from the Golgi are also required for the docking step of homotypic vacuole fusion. J Cell Biol 148, 1223-1230.
<\/p>\n\n\n\n

Price AE, Seals D, Wickner W, Ungermann C<\/strong> (2000) The docking stage of yeast vacuole fusion requires the transfer of proteins from the cis-SNARE complex to a Rab\/Ypt protein. J Cell Biol 148, 1231-38.<\/p>\n\n\n\n \n\n\n\n

1999<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Ungermann C<\/strong>, Wickner W, Xu Z (1999) Vacuole acidification is required for trans-SNARE pairing, LMA1 release and homotypic fusion. PNAS 96, 11194-11199.
<\/p>\n\n\n\n

Ungermann C<\/strong>, Fischer von Mollard G, Jensen O, Stevens TH, Wickner W (1999) Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are required for homotypic fusion. J Cell Biol 145, 1435-1442.<\/p>\n\n\n\n \n\n\n\n

1998<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Ungermann C<\/strong>, Sato K, Wickner W (1998) Defining the roles of trans SNARE pairs. Nature 396, 543-548.
<\/p>\n\n\n\n

Ungermann C<\/strong>, Wickner W (1998). Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. EMBO J 17, 3269-3276.
<\/p>\n\n\n\n

Ungermann C<\/strong>, Nichols BN, Pelham HRB, Wickner W (1998). A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated organelles, is disassembled and activated for docking and fusion. J Cell Biol 140, 61-69.
<\/p>\n\n\n\n

Gaume B, Klaus C, Ungermann C<\/strong>, Guiard B, Neupert W, and Brunner M (1998) Unfolding of preproteins upon import into mitochondria. EMBO J 17, 6497-6507.<\/p>\n\n\n\n \n\n\n\n

1997<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Nichols BN, Ungermann C<\/strong>, Pelham HRB, Wickner W, and Haas A (1997) Homotypic vacuolar fusion mediated by v-and t-SNAREs. Nature 387, 199-202.
<\/p>\n\n\n\n

Gieffers C, Korioth F,  Heimann P, Ungermann C<\/strong>, and Frey J (1997) Mitofilin is a transmembrane protein of the inner mitochondrial membrane expressed as two isoforms. Exp Cell Res, 232, 395-9.<\/p>\n\n\n\n \n\n\n\n

1996 and before<\/strong><\/h3>\n\n\n\n
\n\n\n\n \n\n\n\n

Wheeler LJ, Ray NB, Ungermann C<\/strong>, Hendricks SP, Bernard MA, Hanson EA, and Mathews CK (1996). T4 Phage Gene 32 Protein as a Candidate Organizing Factor for the dNTP Synthetase Complex. J Biol Chem 271, 11156-11162.
<\/p>\n\n\n\n

Ungermann C<\/strong>, Guiard B, Neupert W, and Cyr DM (1996) The \u2206 and Hsp70\/MIM44 dependent Reaction Cycle in Driving Early Steps of Protein Translocation into Mitochondria. EMBO J 15, 735-744.
<\/p>\n\n\n\n

Ungermann C<\/strong>, Neupert W, Cyr DM (1994). The Role of Hsp70 in Conferring Unidirectionality on Protein Translocation into Mitochondria. Science 266, 1250-1253.
<\/p>\n\n\n\n

Mathews CK, Wheeler LJ, Ungermann C<\/strong>, Young JP, and Ray NB (1993). Enzyme Interactions Involving T4-phage Coded Thymidylate Synthase and Deoxyhydroxymethylase. Adv Med Exp Biol 338, 563-570.<\/p>\n\n\n\n \n<\/div>\n\n\n\n

<\/div>\n<\/div>\n\n\n\n
\n
<\/div>\n\n\n\n
\n

a) Reviews<\/strong><\/h3>\n\n\n\n \n\n\n\n

<\/p>\n\n\n\n

Ungermann C<\/strong>, Moeller A (2025) Structuring of the endolysosomal system by HOPS and CORVET complexes. Curr Opin Cell Biol 94:102504.<\/p>\n\n\n\n

Galic M, Ungermann C<\/strong>, Cosentino K (2023) Highlight: on the past and future of cellular microcompartments. Biol Chem 404: 377-378.<\/p>\n\n\n\n

K\u00fcmmel D, Herrmann E, Langemeyer L, Ungermann C<\/strong> (2023) Molecular insights into endolysosomal microcompartment formation and maintenance. Biol Chem 404: 441-454.<\/p>\n\n\n\n

Langemeyer L, Ungermann C<\/strong> (2022) Vesicle transport: Exocyst follows PIP2 to tether membranes. Curr Biol 32: R748-750.<\/p>\n\n\n\n

Bottanelli F, Spang A, Stefan C, Ungermann C<\/strong> (2021) Meeting report \u2013 An online gathering about the latest on Molecular Membrane Biology. J Biol Chem 97, 101334.<\/p>\n\n\n\n

Borchers AC, Langemeyer L, Ungermann C<\/strong> (2021) Who\u2019s in control? Principles of Rab GTPase activation in endolysosomal membrane trafficking and beyond. J Cell Biol 220, e202105120.<\/p>\n\n\n\n

Langemeyer L, Fr\u00f6hlich F, Ungerman C<\/strong> (2018) Rab GTPase function in endosome and lysosome biogenesis. Trends Cell Biol, doi: 10.1080\/15548627.2018.1477382.
<\/p>\n\n\n\n

Ungermann C<\/strong>, Reggiori F (2018) <\/strong>Atg9 protein, not so different after all. Autophagy, in press
<\/p>\n\n\n\n

Kriegenburg F, Ungermann C<\/strong>, Reggiori F (2018) Coordination of autophagosome-lysosome fusion by Atg8 family members. Curr Biol 28, R512-518.
<\/p>\n\n\n\n

L\u00fcrick A, K\u00fcmmel D, Ungermann C<\/strong> (2018) Multisubunit tethers in membrane fusion. Curr Biol 28, R417-420.
<\/p>\n\n\n\n

Kornmann B, Ungermann C<\/strong> (2017) Membrane contact sites. Biochim Biophys Acta 1864, 1435-1438.
<\/p>\n\n\n\n

Reggiori F, Ungermann C<\/strong> (2017) Autophagosome maturation and fusion. J Mol Biol, in press
<\/p>\n\n\n\n

Malia PC, Ungermann C<\/strong> (2016) Vacuole membrane contact sites and domains: emerging hubs to coordinate organelle function with cellular metabolism. Biochem Soc Trans 44, 528-533.
<\/p>\n\n\n\n

Gonz\u00e1lez Montoro A, Ungermann C<\/strong> (2015) StARTing to understand membrane contact sites. Trends Cell Biol 25, 497-498.
<\/p>\n\n\n\n

Kuhlee A, Raunser S, Ungermann C<\/strong> (2015) Functional homologies in vesicle tethering. Febs Letters 589, 2487-2497.
<\/p>\n\n\n\n

Langemeyer L, Ungermann C<\/strong> (2015) BORC and BLOC-1: Shared subunits in trafficking complexes. Dev Cell 33, 121-122.
<\/p>\n\n\n\n

Ungermann C<\/strong> (2015) vCLAMPs \u2013 an intimate link between vacuoles and mitochondria. Curr Opin Cell Biol 25, 30-36.
<\/p>\n\n\n\n

K\u00fcmmel D, Ungermann C<\/strong> (2014) Principles of membrane tethering and fusion in endosome and lysosome biogenesis. Curr Opin Cell Biol 29, 61-66.
<\/p>\n\n\n\n

Gautreau A, Oguievetskaia K, Ungermann C<\/strong> (2014) Function and regulation of the endosomal fusion and fission machineries. Cold Spring Harb Perspect Biol 6, pii: a016832
<\/p>\n\n\n\n

H\u00f6nscher C, Ungermann C<\/strong> (2014) A close-up view of membrane contact sites between the endoplasmic reticulum and the endolysosomal system: From yeast to man. Crit Rev Biochem Mol Biol 49, 262-268.
<\/p>\n\n\n\n

Numrich J, Ungermann C<\/strong> (2014) Endocytic Rabs in membrane trafficking and signaling. Biol Chem 395, 327-33.
<\/p>\n\n\n\n

Holthuis J, Ungermann C<\/strong> (2013) Cellular Microcompartments constitute general suborganellar functional units in cells. Biol Chem 394, 151-161.
<\/p>\n\n\n\n

kleine Balderhaar HJ, Ungermann C<\/strong> (2013) CORVET and HOPS tethering complexes \u2013 coordinators of endosome and lysosome fusion. J Cell Sci 126, 1307-1316.
<\/p>\n\n\n\n

Reggiori F, Ungermann C<\/strong> (2012) A dimer to bridge early autophagosomal membranes. Cell 151, 1403-05.
<\/p>\n\n\n\n

Epp N, Rethmeier R, Kr\u00e4mer L, Ungermann C<\/strong> (2011) Membrane dynamics and fusion at late endosomes and vacuoles – Rab regulation, multisubunit tethering complexes and SNAREs. EJCB 90, 779-785.
<\/p>\n\n\n\n

Lachmann J, Ungermann C<\/strong>, and Engelbrecht-Vandr\u00e9 S (2011) Rab GTPases and tethering in the yeast endocytic pathway. Small GTPases, 2, 182-186.
<\/p>\n\n\n\n

Br\u00f6cker C, Engelbrecht-Vandr\u00e9 S, Ungermann C<\/strong> (2010) Multisubunit tethering complexes and their role in membrane fusion, Curr Biol 20, R943-952.
<\/p>\n\n\n\n

Cabrera M, Ungermann C<\/strong> (2010) Guiding endosomal maturation, Cell 141, 404-406.
<\/p>\n\n\n\n

Cabrera M, Ungermann C<\/strong> (2009), Purification and in vitro analysis of yeast vacuoles, Methods Enzymol 451,177-96.
<\/p>\n\n\n\n

Peplowska K, Cabrera M, Ungermann C<\/strong> (2008) UVRAG reveals its second nature. Nat Cell Biol 10, 759-61.
<\/p>\n\n\n\n

Ostrowicz CF, Meiringer CM, Ungermann C<\/strong> (2008) Yeast vacuole fusion: A model system for eukaryotic endomembrane dynamics. Autophagy 4, 1-15.
<\/p>\n\n\n\n

Langosch D, Hoffmann M, Ungermann C<\/strong> (2007) The role of transmembrane domains in membrane fusion. Cell Mol Life Sci 64, 850-864.
<\/p>\n\n\n\n

Markgraf DM, Peplowska K, Ungermann C<\/strong> (2007) Rab cascades and tethering factors in the endomembrane system. FEBS letters 581, 2125-2130.
<\/p>\n\n\n\n

Meiringer CT, Ungermann C<\/strong> (2006) Probing protein palmitoylation at yeast vacuoles. Methods 40, 171-176.
<\/p>\n\n\n\n

Ungermann C<\/strong> , Langosch D (2005) Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing. J Cell Sci 118, 3819-3828.
<\/p>\n\n\n\n

Peplowska K, Ungermann C<\/strong> (2005) Expanding dynamin: from fission to fusion. Nat Cell Biol 7, 103-104.
<\/p>\n\n\n\n

Rossi V, Banfield DK, Vacca M, Dietrich LE, Ungermann C<\/strong>, D\u2019Esposito M, Galli T, and Filippini F (2004) Longins and their longin domain: regulated SNAREs and multifunctional SNARE regulators. Trends Biochem Sci 29, 682-688.
<\/p>\n\n\n\n

Dietrich LE, Ungermann C<\/strong> (2004) On the mechanism of protein palmitoylation. EMBO Rep 5, 1053-1057.
<\/p>\n\n\n\n

Dietrich L, Boeddinghaus C, LaGrassa T, Ungermann C<\/strong> (2003) Control of eukaryotic membrane fusion by the N-terminal domains of SNARE proteins. BBA rev membranes 1641, 111-119.
<\/p>\n\n\n\n

Ungermann C<\/strong>, Neupert W, Cyr DM (1995) Regulation of Protein Transport through Mitochondrial Membranes.  Journal of NIH Research 6, 7, 60.
<\/p>\n\n\n\n

Cyr DM, Ungermann C<\/strong>, and Neupert, W (1995) Analysis of Mitochondrial Protein Import with Translocation Intermediates. Meth Enz, 260, 241-252.<\/p>\n<\/div>\n\n\n\n

<\/div>\n<\/div>\n\n\n\n

<\/p>\n\n\n\n

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