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Items: 1 to 50 of 126

1.

Structure of membrane tethers and their role in fusion.

Ungermann C, Kümmel D.

Traffic. 2019 Jul;20(7):479-490. doi: 10.1111/tra.12655. Epub 2019 May 30. Review.

PMID:
31062920
2.

Coming together to define membrane contact sites.

Scorrano L, De Matteis MA, Emr S, Giordano F, Hajnóczky G, Kornmann B, Lackner LL, Levine TP, Pellegrini L, Reinisch K, Rizzuto R, Simmen T, Stenmark H, Ungermann C, Schuldiner M.

Nat Commun. 2019 Mar 20;10(1):1287. doi: 10.1038/s41467-019-09253-3. Review.

3.

The multi-functional SNARE protein Ykt6 in autophagosomal fusion processes.

Kriegenburg F, Bas L, Gao J, Ungermann C, Kraft C.

Cell Cycle. 2019 Mar - Apr;18(6-7):639-651. doi: 10.1080/15384101.2019.1580488. Epub 2019 Mar 17.

4.

Cargo induces retromer-mediated membrane remodeling on membranes.

Purushothaman LK, Ungermann C.

Mol Biol Cell. 2018 Nov 1;29(22):2709-2719. doi: 10.1091/mbc.E18-06-0339. Epub 2018 Sep 6.

5.

A novel in vitro assay reveals SNARE topology and the role of Ykt6 in autophagosome fusion with vacuoles.

Gao J, Reggiori F, Ungermann C.

J Cell Biol. 2018 Oct 1;217(10):3670-3682. doi: 10.1083/jcb.201804039. Epub 2018 Aug 10.

6.

Rab GTPase Function in Endosome and Lysosome Biogenesis.

Langemeyer L, Fröhlich F, Ungermann C.

Trends Cell Biol. 2018 Nov;28(11):957-970. doi: 10.1016/j.tcb.2018.06.007. Epub 2018 Jul 17. Review.

PMID:
30025982
7.

Atg9 proteins, not so different after all.

Ungermann C, Reggiori F.

Autophagy. 2018;14(8):1456-1459. doi: 10.1080/15548627.2018.1477382. Epub 2018 Jul 23.

8.

Lipid trafficking by yeast Snx4 family SNX-BAR proteins promotes autophagy and vacuole membrane fusion.

Ma M, Kumar S, Purushothaman L, Babst M, Ungermann C, Chi RJ, Burd CG.

Mol Biol Cell. 2018 Sep 1;29(18):2190-2200. doi: 10.1091/mbc.E17-12-0743. Epub 2018 Jun 27.

9.

Vps39 Interacts with Tom40 to Establish One of Two Functionally Distinct Vacuole-Mitochondria Contact Sites.

González Montoro A, Auffarth K, Hönscher C, Bohnert M, Becker T, Warscheid B, Reggiori F, van der Laan M, Fröhlich F, Ungermann C.

Dev Cell. 2018 Jun 4;45(5):621-636.e7. doi: 10.1016/j.devcel.2018.05.011.

10.

Atg9 establishes Atg2-dependent contact sites between the endoplasmic reticulum and phagophores.

Gómez-Sánchez R, Rose J, Guimarães R, Mari M, Papinski D, Rieter E, Geerts WJ, Hardenberg R, Kraft C, Ungermann C, Reggiori F.

J Cell Biol. 2018 Aug 6;217(8):2743-2763. doi: 10.1083/jcb.201710116. Epub 2018 May 30.

11.

Coordination of Autophagosome-Lysosome Fusion by Atg8 Family Members.

Kriegenburg F, Ungermann C, Reggiori F.

Curr Biol. 2018 Apr 23;28(8):R512-R518. doi: 10.1016/j.cub.2018.02.034. Review.

12.

Multisubunit tethers in membrane fusion.

Lürick A, Kümmel D, Ungermann C.

Curr Biol. 2018 Apr 23;28(8):R417-R420. doi: 10.1016/j.cub.2017.12.012. Review.

13.

Control of vacuole membrane homeostasis by a resident PI-3,5-kinase inhibitor.

Malia PC, Numrich J, Nishimura T, González Montoro A, Stefan CJ, Ungermann C.

Proc Natl Acad Sci U S A. 2018 May 1;115(18):4684-4689. doi: 10.1073/pnas.1722517115. Epub 2018 Apr 19.

14.

Molecular mechanism to target the endosomal Mon1-Ccz1 GEF complex to the pre-autophagosomal structure.

Gao J, Langemeyer L, Kümmel D, Reggiori F, Ungermann C.

Elife. 2018 Feb 15;7. pii: e31145. doi: 10.7554/eLife.31145.

15.

A guanine nucleotide exchange factor (GEF) limits Rab GTPase-driven membrane fusion.

Langemeyer L, Perz A, Kümmel D, Ungermann C.

J Biol Chem. 2018 Jan 12;293(2):731-739. doi: 10.1074/jbc.M117.812941. Epub 2017 Nov 28.

16.

A tethering complex drives the terminal stage of SNARE-dependent membrane fusion.

D'Agostino M, Risselada HJ, Lürick A, Ungermann C, Mayer A.

Nature. 2017 Nov 30;551(7682):634-638. doi: 10.1038/nature24469. Epub 2017 Nov 1.

PMID:
29088698
17.

Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation.

Sánchez-Wandelmer J, Kriegenburg F, Rohringer S, Schuschnig M, Gómez-Sánchez R, Zens B, Abreu S, Hardenberg R, Hollenstein D, Gao J, Ungermann C, Martens S, Kraft C, Reggiori F.

Nat Commun. 2017 Aug 18;8(1):295. doi: 10.1038/s41467-017-00302-3.

18.

Membrane contact sites.

Kornmann B, Ungermann C.

Biochim Biophys Acta Mol Cell Res. 2017 Sep;1864(9):1435-1438. doi: 10.1016/j.bbamcr.2017.06.014. Epub 2017 Jun 23. No abstract available.

19.

Retromer-driven membrane tubulation separates endosomal recycling from Rab7/Ypt7-dependent fusion.

Purushothaman LK, Arlt H, Kuhlee A, Raunser S, Ungermann C.

Mol Biol Cell. 2017 Mar 15;28(6):783-791. doi: 10.1091/mbc.E16-08-0582. Epub 2017 Jan 18.

20.

Autophagosome Maturation and Fusion.

Reggiori F, Ungermann C.

J Mol Biol. 2017 Feb 17;429(4):486-496. doi: 10.1016/j.jmb.2017.01.002. Epub 2017 Jan 8. Review.

21.

Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1-Ccz1.

Kiontke S, Langemeyer L, Kuhlee A, Schuback S, Raunser S, Ungermann C, Kümmel D.

Nat Commun. 2017 Jan 4;8:14034. doi: 10.1038/ncomms14034.

22.

Multivalent Rab interactions determine tether-mediated membrane fusion.

Lürick A, Gao J, Kuhlee A, Yavavli E, Langemeyer L, Perz A, Raunser S, Ungermann C.

Mol Biol Cell. 2017 Jan 15;28(2):322-332. doi: 10.1091/mbc.E16-11-0764. Epub 2016 Nov 16.

23.

Yeast cell wall integrity sensors form specific plasma membrane microdomains important for signalling.

Kock C, Arlt H, Ungermann C, Heinisch JJ.

Cell Microbiol. 2016 Sep;18(9):1251-67. doi: 10.1111/cmi.12635. Epub 2016 Jul 22.

PMID:
27337501
24.

Vacuole membrane contact sites and domains: emerging hubs to coordinate organelle function with cellular metabolism.

Malia PC, Ungermann C.

Biochem Soc Trans. 2016 Apr 15;44(2):528-33. doi: 10.1042/BST20150277. Review.

PMID:
27068965
25.

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).

Klionsky DJ, Abdelmohsen K, Abe A, Abedin MJ, Abeliovich H, Acevedo Arozena A, Adachi H, Adams CM, Adams PD, Adeli K, Adhihetty PJ, Adler SG, Agam G, Agarwal R, Aghi MK, Agnello M, Agostinis P, Aguilar PV, Aguirre-Ghiso J, Airoldi EM, Ait-Si-Ali S, Akematsu T, Akporiaye ET, Al-Rubeai M, Albaiceta GM, Albanese C, Albani D, Albert ML, Aldudo J, Algül H, Alirezaei M, Alloza I, Almasan A, Almonte-Beceril M, Alnemri ES, Alonso C, Altan-Bonnet N, Altieri DC, Alvarez S, Alvarez-Erviti L, Alves S, Amadoro G, Amano A, Amantini C, Ambrosio S, Amelio I, Amer AO, Amessou M, Amon A, An Z, Anania FA, Andersen SU, Andley UP, Andreadi CK, Andrieu-Abadie N, Anel A, Ann DK, Anoopkumar-Dukie S, Antonioli M, Aoki H, Apostolova N, Aquila S, Aquilano K, Araki K, Arama E, Aranda A, Araya J, Arcaro A, Arias E, Arimoto H, Ariosa AR, Armstrong JL, Arnould T, Arsov I, Asanuma K, Askanas V, Asselin E, Atarashi R, Atherton SS, Atkin JD, Attardi LD, Auberger P, Auburger G, Aurelian L, Autelli R, Avagliano L, Avantaggiati ML, Avrahami L, Awale S, Azad N, Bachetti T, Backer JM, Bae DH, Bae JS, Bae ON, Bae SH, Baehrecke EH, Baek SH, Baghdiguian S, Bagniewska-Zadworna A, Bai H, Bai J, Bai XY, Bailly Y, Balaji KN, Balduini W, Ballabio A, Balzan R, Banerjee R, Bánhegyi G, Bao H, Barbeau B, Barrachina MD, Barreiro E, Bartel B, Bartolomé A, Bassham DC, Bassi MT, Bast RC Jr, Basu A, Batista MT, Batoko H, Battino M, Bauckman K, Baumgarner BL, Bayer KU, Beale R, Beaulieu JF, Beck GR Jr, Becker C, Beckham JD, Bédard PA, Bednarski PJ, Begley TJ, Behl C, Behrends C, Behrens GM, Behrns KE, Bejarano E, Belaid A, Belleudi F, Bénard G, Berchem G, Bergamaschi D, Bergami M, Berkhout B, Berliocchi L, Bernard A, Bernard M, Bernassola F, Bertolotti A, Bess AS, Besteiro S, Bettuzzi S, Bhalla S, Bhattacharyya S, Bhutia SK, Biagosch C, Bianchi MW, Biard-Piechaczyk M, Billes V, Bincoletto C, Bingol B, Bird SW, Bitoun M, Bjedov I, Blackstone C, Blanc L, Blanco GA, Blomhoff HK, Boada-Romero E, Böckler S, Boes M, Boesze-Battaglia K, Boise LH, Bolino A, Boman A, Bonaldo P, Bordi M, Bosch J, Botana LM, Botti J, Bou G, Bouché M, Bouchecareilh M, Boucher MJ, Boulton ME, Bouret SG, Boya P, Boyer-Guittaut M, Bozhkov PV, Brady N, Braga VM, Brancolini C, Braus GH, Bravo-San Pedro JM, Brennan LA, Bresnick EH, Brest P, Bridges D, Bringer MA, Brini M, Brito GC, Brodin B, Brookes PS, Brown EJ, Brown K, Broxmeyer HE, Bruhat A, Brum PC, Brumell JH, Brunetti-Pierri N, Bryson-Richardson RJ, Buch S, Buchan AM, Budak H, Bulavin DV, Bultman SJ, Bultynck G, Bumbasirevic V, Burelle Y, Burke RE, Burmeister M, Bütikofer P, Caberlotto L, Cadwell K, Cahova M, Cai D, Cai J, Cai Q, Calatayud S, Camougrand N, Campanella M, Campbell GR, Campbell M, Campello S, Candau R, Caniggia I, Cantoni L, Cao L, Caplan AB, Caraglia M, Cardinali C, Cardoso SM, Carew JS, Carleton LA, Carlin CR, Carloni S, Carlsson SR, Carmona-Gutierrez D, Carneiro LA, Carnevali O, Carra S, Carrier A, Carroll B, Casas C, Casas J, Cassinelli G, Castets P, Castro-Obregon S, Cavallini G, Ceccherini I, Cecconi F, Cederbaum AI, Ceña V, Cenci S, Cerella C, Cervia D, Cetrullo S, Chaachouay H, Chae HJ, Chagin AS, Chai CY, Chakrabarti G, Chamilos G, Chan EY, Chan MT, Chandra D, Chandra P, Chang CP, Chang RC, Chang TY, Chatham JC, Chatterjee S, Chauhan S, Che Y, Cheetham ME, Cheluvappa R, Chen CJ, Chen G, Chen GC, Chen G, Chen H, Chen JW, Chen JK, Chen M, Chen M, Chen P, Chen Q, Chen Q, Chen SD, Chen S, Chen SS, Chen W, Chen WJ, Chen WQ, Chen W, Chen X, Chen YH, Chen YG, Chen Y, Chen Y, Chen Y, Chen YJ, Chen YQ, Chen Y, Chen Z, Chen Z, Cheng A, Cheng CH, Cheng H, Cheong H, Cherry S, Chesney J, Cheung CH, Chevet E, Chi HC, Chi SG, Chiacchiera F, Chiang HL, Chiarelli R, Chiariello M, Chieppa M, Chin LS, Chiong M, Chiu GN, Cho DH, Cho SG, Cho WC, Cho YY, Cho YS, Choi AM, Choi EJ, Choi EK, Choi J, Choi ME, Choi SI, Chou TF, Chouaib S, Choubey D, Choubey V, Chow KC, Chowdhury K, Chu CT, Chuang TH, Chun T, Chung H, Chung T, Chung YL, Chwae YJ, Cianfanelli V, Ciarcia R, Ciechomska IA, Ciriolo MR, Cirone M, Claerhout S, Clague MJ, Clària J, Clarke PG, Clarke R, Clementi E, Cleyrat C, Cnop M, Coccia EM, Cocco T, Codogno P, Coers J, Cohen EE, Colecchia D, Coletto L, Coll NS, Colucci-Guyon E, Comincini S, Condello M, Cook KL, Coombs GH, Cooper CD, Cooper JM, Coppens I, Corasaniti MT, Corazzari M, Corbalan R, Corcelle-Termeau E, Cordero MD, Corral-Ramos C, Corti O, Cossarizza A, Costelli P, Costes S, Cotman SL, Coto-Montes A, Cottet S, Couve E, Covey LR, Cowart LA, Cox JS, Coxon FP, Coyne CB, Cragg MS, Craven RJ, Crepaldi T, Crespo JL, Criollo A, Crippa V, Cruz MT, Cuervo AM, Cuezva JM, Cui T, Cutillas PR, Czaja MJ, Czyzyk-Krzeska MF, Dagda RK, Dahmen U, Dai C, Dai W, Dai Y, Dalby KN, Dalla Valle L, Dalmasso G, D'Amelio M, Damme M, Darfeuille-Michaud A, Dargemont C, Darley-Usmar VM, Dasarathy S, Dasgupta B, Dash S, Dass CR, Davey HM, Davids LM, Dávila D, Davis RJ, Dawson TM, Dawson VL, Daza P, de Belleroche J, de Figueiredo P, de 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41.

Cellular metabolism regulates contact sites between vacuoles and mitochondria.

Hönscher C, Mari M, Auffarth K, Bohnert M, Griffith J, Geerts W, van der Laan M, Cabrera M, Reggiori F, Ungermann C.

Dev Cell. 2014 Jul 14;30(1):86-94. doi: 10.1016/j.devcel.2014.06.006.

42.

Principles of membrane tethering and fusion in endosome and lysosome biogenesis.

Kümmel D, Ungermann C.

Curr Opin Cell Biol. 2014 Aug;29:61-6. doi: 10.1016/j.ceb.2014.04.007. Epub 2014 May 17. Review.

PMID:
24813801
43.

Dynamic association of the PI3P-interacting Mon1-Ccz1 GEF with vacuoles is controlled through its phosphorylation by the type 1 casein kinase Yck3.

Lawrence G, Brown CC, Flood BA, Karunakaran S, Cabrera M, Nordmann M, Ungermann C, Fratti RA.

Mol Biol Cell. 2014 May;25(10):1608-19. doi: 10.1091/mbc.E13-08-0460. Epub 2014 Mar 12.

44.

Function and regulation of the endosomal fusion and fission machineries.

Gautreau A, Oguievetskaia K, Ungermann C.

Cold Spring Harb Perspect Biol. 2014 Mar 1;6(3). pii: a016832. doi: 10.1101/cshperspect.a016832. Review.

45.

The Mon1-Ccz1 GEF activates the Rab7 GTPase Ypt7 via a longin-fold-Rab interface and association with PI3P-positive membranes.

Cabrera M, Nordmann M, Perz A, Schmedt D, Gerondopoulos A, Barr F, Piehler J, Engelbrecht-Vandré S, Ungermann C.

J Cell Sci. 2014 Mar 1;127(Pt 5):1043-51. doi: 10.1242/jcs.140921. Epub 2014 Jan 10.

46.

A close-up view of membrane contact sites between the endoplasmic reticulum and the endolysosomal system: from yeast to man.

Hönscher C, Ungermann C.

Crit Rev Biochem Mol Biol. 2014 May-Jun;49(3):262-8. doi: 10.3109/10409238.2013.875512. Epub 2014 Jan 2. Review.

PMID:
24382115
47.

Subunit organisation of in vitro reconstituted HOPS and CORVET multisubunit membrane tethering complexes.

Guo Z, Johnston W, Kovtun O, Mureev S, Bröcker C, Ungermann C, Alexandrov K.

PLoS One. 2013 Dec 2;8(12):e81534. doi: 10.1371/journal.pone.0081534. eCollection 2013. Erratum in: PLoS One. 2014;9(1). doi:10.1371/annotation/3b445e95-4f8c-4238-9895-e05f49949f20.

48.

Endocytic Rabs in membrane trafficking and signaling.

Numrich J, Ungermann C.

Biol Chem. 2014 Mar;395(3):327-33. doi: 10.1515/hsz-2013-0258. Review.

PMID:
24158421
49.

Guanine nucleotide exchange factors (GEFs) have a critical but not exclusive role in organelle localization of Rab GTPases.

Cabrera M, Ungermann C.

J Biol Chem. 2013 Oct 4;288(40):28704-12. doi: 10.1074/jbc.M113.488213. Epub 2013 Aug 26.

50.

The N-terminal domains of Vps3 and Vps8 are critical for localization and function of the CORVET tethering complex on endosomes.

Epp N, Ungermann C.

PLoS One. 2013 Jun 20;8(6):e67307. doi: 10.1371/journal.pone.0067307. Print 2013.

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