Abteilung Langer

Publikationen

Small heat shock proteins operate as molecular chaperones in the mitochondrial intermembrane space

  • Adriaenssens, E.
  • Asselbergh, B.
  • Rivera-Mejias, P.
  • Bervoets, S.
  • Vendredy, L.
  • De Winter, V.
  • Spaas, K.
  • de Rycke, R.
  • van Isterdael, G.
  • Impens, F.
  • Langer, T.
  • Timmerman, V.
(2023) Nat Cell Biol

Monoamine oxidase A-dependent ROS formation modulates human cardiomyocyte differentiation through AKT and WNT activation

  • Di Sante, M.
  • Antonucci, S.
  • Pontarollo, L.
  • Cappellaro, I.
  • Segat, F.
  • Deshwal, S.
  • Greotti, E.
  • Grilo, L. F.
  • Menabo, R.
  • Di Lisa, F.
  • Kaludercic, N.
(2023) Basic Res Cardiol, 118, 1, 4

Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7

  • Deshwal, S.
  • Onishi, M.
  • Tatsuta, T.
  • Bartsch, T.
  • Cors, E.
  • Ried, K.
  • Lemke, K.
  • Nolte, H.
  • Giavalisco, P.
  • Langer, T.
(2023) Nat Cell Biol

Human mitochondria require mtRF1 for translation termination at non-canonical stop codons

  • Kruger, A.
  • Remes, C.
  • Shiriaev, D. I.
  • Liu, Y.
  • Spahr, H.
  • Wibom, R.
  • Atanassov, I.
  • Nguyen, M. D.
  • Cooperman, B. S.
  • Rorbach, J.
(2023) Nat Commun, 14, 1, 30

An intermolecular hydrogen bonded network in the PRELID-TRIAP protein family plays a role in lipid sensing

  • Miliara, X.
  • Tatsuta, T.
  • Eiyama, A.
  • Langer, T.
  • Rouse, S. L.
  • Matthews, S.
(2023) Biochim Biophys Acta Proteins Proteom, 1871, 1, 140867

Chemical Blockage of the Mitochondrial Rhomboid Protease PARL by Novel Ketoamide Inhibitors Reveals Its Role in PINK1/Parkin-Dependent Mitophagy

  • Polachova, E.
  • Bach, K.
  • Heuten, E.
  • Stanchev, S.
  • Ticha, A.
  • Lampe, P.
  • Majer, P.
  • Langer, T.
  • Lemberg, M. K.
  • Strisovsky, K.
(2022) J Med Chem

Lyve-1 deficiency enhances the hepatic immune microenvironment entailing altered susceptibility to melanoma liver metastasis

  • Jauch, A. S.
  • Wohlfeil, S. A.
  • Weller, C.
  • Dietsch, B.
  • Hafele, V.
  • Stojanovic, A.
  • Kittel, M.
  • Nolte, H.
  • Cerwenka, A.
  • Neumaier, M.
  • Schledzewski, K.
  • Sticht, C.
  • Reiners-Koch, P. S.
  • Goerdt, S.
  • Geraud, C.
(2022) Cancer Cell Int, 22, 1, 398

Targeting of Scavenger Receptors Stabilin-1 and Stabilin-2 Ameliorates Atherosclerosis by a Plasma Proteome Switch Mediating Monocyte/Macrophage Suppression

  • Manta, C. P.
  • Leibing, T.
  • Friedrich, M.
  • Nolte, H.
  • Adrian, M.
  • Schledzewski, K.
  • Krzistetzko, J.
  • Kirkamm, C.
  • David Schmid, C.
  • Xi, Y.
  • Stojanovic, A.
  • Tonack, S.
  • de la Torre, C.
  • Hammad, S.
  • Offermanns, S.
  • Kruger, M.
  • Cerwenka, A.
  • Platten, M.
  • Goerdt, S.
  • Geraud, C.
(2022) Circulation, 146, 23, 1783-1799

NIK/MAP3K14 in hepatocytes orchestrates NASH to hepatocellular carcinoma progression via JAK2/STAT5 inhibition

  • Vesting, A. J.
  • Jais, A.
  • Klemm, P.
  • Steuernagel, L.
  • Wienand, P.
  • Fog-Tonnesen, M.
  • Hvid, H.
  • Schumacher, A. L.
  • Kukat, C.
  • Nolte, H.
  • Georgomanolis, T.
  • Altmuller, J.
  • Pasparakis, M.
  • Schmidt, A.
  • Kruger, M.
  • Supprian, M. S.
  • Waisman, A.
  • Straub, B. K.
  • Raschzok, N.
  • Bernier, M.
  • Birkenfeld, A. L.
  • Hovelmeyer, N.
  • Bruning, J. C.
  • Wunderlich, F. T.
(2022) Mol Metab, 66, 101626

OMA1-mediated integrated stress response protects against ferroptosis in mitochondrial cardiomyopathy

  • Ahola, S.
  • Rivera Mejias, P.
  • Hermans, S.
  • Chandragiri, S.
  • Giavalisco, P.
  • Nolte, H.
  • Langer, T.
(2022) Cell Metab, 34, 11, 1875-1891 e7

Disease causing mutation (P178L) in mitochondrial transcription factor A results in impaired mitochondrial transcription initiation

  • Mehmedovic, M.
  • Martucci, M.
  • Spahr, H.
  • Ishak, L.
  • Mishra, A.
  • Sanchez-Sandoval, M. E.
  • Pardo-Hernandez, C.
  • Peter, B.
  • van den Wildenberg, S. M.
  • Falkenberg, M.
  • Farge, G.
(2022) Biochim Biophys Acta Mol Basis Dis, 166467

CLUH controls astrin-1 expression to couple mitochondrial metabolism to cell cycle progression

  • Schatton, D.
  • Di Pietro, G.
  • Szczepanowska, K.
  • Veronese, M.
  • Marx, M. C.
  • Braunohler, K.
  • Barth, E.
  • Muller, S.
  • Giavalisco, P.
  • Langer, T.
  • Trifunovic, A.
  • Rugarli, E. I.
(2022) Elife, 11

FGF21 modulates mitochondrial stress response in cardiomyocytes only under mild mitochondrial dysfunction

  • Croon, M.
  • Szczepanowska, K.
  • Popovic, M.
  • Lienkamp, C.
  • Senft, K.
  • Brandscheid, C. P.
  • Bock, T.
  • Gnatzy-Feik, L.
  • Ashurov, A.
  • Acton, R. J.
  • Kaul, H.
  • Pujol, C.
  • Rosenkranz, S.
  • Kruger, M.
  • Trifunovic, A.
(2022) Sci Adv, 8, 14, eabn7105

Therapeutic Treatment of Superoxide Dismutase 1 (G93A) Amyotrophic Lateral Sclerosis Model Mice with Medical Ozone Decelerates Trigeminal Motor Neuron Degeneration, …

  • Bette, M.
  • Cors, E.
  • Kresse, C.
  • Schutz, B.
(2022) Int J Mol Sci, 23, 6

The mechanosensor Filamin A/Cheerio promotes tumorigenesis via specific interactions with components of the cell cortex

  • Külshammer, E.
  • Kilinc, M.
  • Csordás, G.
  • Bresser, T.
  • Nolte, H.
  • Uhlirova, M.
(2022) Febs j

Metabolic control of adult neural stem cell self-renewal by the mitochondrial protease YME1L

  • Wani, G. A.
  • Sprenger, H. G.
  • Ndoci, K.
  • Chandragiri, S.
  • Acton, R. J.
  • Schatton, D.
  • Kochan, S. M. V.
  • Sakthivelu, V.
  • Jevtic, M.
  • Seeger, J. M.
  • Muller, S.
  • Giavalisco, P.
  • Rugarli, E. I.
  • Motori, E.
  • Langer, T.
  • Bergami, M.
(2022) Cell Rep, 38, 7, 110370

Activation of Akt-mTORC1 signalling reverts cancer-dependent muscle wasting

  • Geremia, A.
  • Sartori, R.
  • Baraldo, M.
  • Nogara, L.
  • Balmaceda, V.
  • Dumitras, G. A.
  • Ciciliot, S.
  • Scalabrin, M.
  • Nolte, H.
  • Blaauw, B.
(2022) J Cachexia Sarcopenia Muscle, 13, 1, 648-661

Activation of Akt-mTORC1 signalling reverts cancer-dependent muscle wasting

  • Geremia, A.
  • Sartori, R.
  • Baraldo, M.
  • Nogara, L.
  • Balmaceda, V.
  • Dumitras, G. A.
  • Ciciliot, S.
  • Scalabrin, M.
  • Nolte, H.
  • Blaauw, B.
(2022) J Cachexia Sarcopenia Muscle, 13, 1, 648-661

Defining the interactome of the human mitochondrial ribosome identifies SMIM4 and TMEM223 as respiratory chain assembly factors

  • Dennerlein, S.
  • Poerschke, S.
  • Oeljeklaus, S.
  • Wang, C.
  • Richter-Dennerlein, R.
  • Sattmann, J.
  • Bauermeister, D.
  • Hanitsch, E.
  • Stoldt, S.
  • Langer, T.
  • Jakobs, S.
  • Warscheid, B.
  • Rehling, P.
(2021) eLife, 10, e68213

MIROs and DRP1 drive mitochondrial-derived vesicle biogenesis and promote quality control

  • Konig, T.
  • Nolte, H.
  • Aaltonen, M. J.
  • Tatsuta, T.
  • Krols, M.
  • Stroh, T.
  • Langer, T.
  • McBride, H. M.
(2021) Nat Cell Biol, 23, 12, 1271-1286

Mitochondrial metabolism coordinates stage-specific repair processes in macrophages during wound healing

  • Willenborg, S.
  • Sanin, D. E.
  • Jais, A.
  • Ding, X.
  • Ulas, T.
  • Nuechel, J.
  • Popovic, M.
  • MacVicar, T.
  • Langer, T.
  • Schultze, J. L.
  • Gerbaulet, A.
  • Roers, A.
  • Pearce, E. J.
  • Bruning, J. C.
  • Trifunovic, A.
  • Eming, S. A.
(2021) Cell Metab, 33, 12, 2398-2414.e9

IL-17B/RB Activation in Pancreatic Stellate Cells Promotes Pancreatic Cancer Metabolism and Growth

  • Li, J.
  • Wu, X.
  • Schiffmann, L.
  • MacVicar, T.
  • Zhou, C.
  • Wang, Z.
  • Li, D.
  • Camacho, O. V.
  • Heuchel, R.
  • Odenthal, M.
  • Hillmer, A.
  • Quaas, A.
  • Zhao, Y.
  • Bruns, C. J.
  • Popp, F. C.
(2021) Cancers (Basel), 13, 21

Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion

  • Škerlová, J.
  • Berndtsson, J.
  • Nolte, H.
  • Ott, M.
  • Stenmark, P.
(2021) Nat Commun, 12, 1, 5277

Metabolism and Innate Immunity Meet at the Mitochondria

  • Bahat, A.
  • MacVicar, T.
  • Langer, T.
(2021) Front Cell Dev Biol, 9, 720490

Mechanometabolism: Mitochondria promote resilience under pressure

  • MacVicar, T.
  • Langer, T.
(2021) Curr Biol, 31, 13, R859-R861

Protein Import Assay into Mitochondria Isolated from Human Cells

  • Murschall, L. M.
  • Peker, E.
  • MacVicar, T.
  • Langer, T.
  • Riemer, J.
(2021) Bio Protoc, 11, 12, e4057

High-throughput screening identifies suppressors of mitochondrial fragmentation in OPA1 fibroblasts

  • Cretin, E.
  • Lopes, P.
  • Vimont, E.
  • Tatsuta, T.
  • Langer, T.
  • Gazi, A.
  • Sachse, M.
  • Yu-Wai-Man, P.
  • Reynier, P.
  • Wai, T.
(2021) EMBO Mol Med, 13, 6, e13579

ComplexFinder: A software package for the analysis of native protein complex fractionation experiments

  • Nolte, H.
  • Langer, T.
(2021) Biochim Biophys Acta Bioenerg, 1862, 8, 148444

Cellular pyrimidine imbalance triggers mitochondrial DNA–dependent innate immunity

  • Sprenger, H.-G.
  • MacVicar, T.
  • Bahat, A.
  • Fiedler, K. U.
  • Hermans, S.
  • Ehrentraut, D.
  • Ried, K.
  • Milenkovic, D.
  • Bonekamp, N.
  • Larsson, N.-G.
  • Nolte, H.
  • Giavalisco, P.
  • Langer, T.
(2021) Nature Metabolism, 3, 5, 636-650

The ER protein Ema19 facilitates the degradation of non-imported mitochondrial precursor proteins

  • Laborenz, J.
  • Bykov, Y. S.
  • Knoringer, K.
  • Raschle, M.
  • Filker, S.
  • Prescianotto-Baschong, C.
  • Spang, A.
  • Tatsuta, T.
  • Langer, T.
  • Storchova, Z.
  • Schuldiner, M.
  • Herrmann, J. M.
(2021) Mol Biol Cell, 32, 8, 664-674

Phosphoproteomics of the developing heart identifies PERM1 - An outer mitochondrial membrane protein

  • Aravamudhan, S.
  • Turk, C.
  • Bock, T.
  • Keufgens, L.
  • Nolte, H.
  • Lang, F.
  • Krishnan, R. K.
  • Konig, T.
  • Hammerschmidt, P.
  • Schindler, N.
  • Brodesser, S.
  • Rozsivalova, D. H.
  • Rugarli, E.
  • Trifunovic, A.
  • Bruning, J.
  • Langer, T.
  • Braun, T.
  • Kruger, M.
(2021) J Mol Cell Cardiol, 154, 41-59

Disturbed intramitochondrial phosphatidic acid transport impairs cellular stress signaling

  • Eiyama, A.
  • Aaltonen, M. J.
  • Nolte, H.
  • Tatsuta, T.
  • Langer, T.
(2021) J Biol Chem, 296, 100335

Hepatic FTO is dispensable for the regulation of metabolism but counteracts HCC development in vivo

  • Mittenbühler, M. J.
  • Saedler, K.
  • Nolte, H.
  • Kern, L.
  • Zhou, J.
  • Qian, S. B.
  • Meder, L.
  • Ullrich, R. T.
  • Brüning, J. C.
  • Wunderlich, F. T.
(2020) Mol Metab, 42, 101085

Targeting Glutaminolysis: New Perspectives to Understand Cancer Development and Novel Strategies for Potential Target Therapies

  • Wang, Z.
  • Liu, F.
  • Fan, N.
  • Zhou, C.
  • Li, D.
  • Macvicar, T.
  • Dong, Q.
  • Bruns, C. J.
  • Zhao, Y.
(2020) Front Oncol, 10, 589508

The C-terminal region of the oxidoreductase MIA40 stabilizes its cytosolic precursor during mitochondrial import

  • Murschall, L. M.
  • Gerhards, A.
  • MacVicar, T.
  • Peker, E.
  • Hasberg, L.
  • Wawra, S.
  • Langer, T.
  • Riemer, J.
(2020) BMC Biol, 18, 1, 96

Regulation of mitochondrial plasticity by the i-AAA protease YME1L

  • Ohba, Y.
  • MacVicar, T.
  • Langer, T.
(2020) Biol Chem, 401, 6-7, 877-890

Mitochondrial Proteases: Multifaceted Regulators of Mitochondrial Plasticity

  • Deshwal, S.
  • Fiedler, K. U.
  • Langer, T.
(2020) Annu Rev Biochem, 89, 501-528

A nutritional memory effect counteracts benefits of dietary restriction in old mice

  • Hahn, O.
  • Drews, L. F.
  • Nguyen, A.
  • Tatsuta, T.
  • Gkioni, L.
  • Hendrich, O.
  • Zhang, Q.
  • Langer, T.
  • Pletcher, S.
  • Wakelam, M. J. O.
  • Beyer, A.
  • Gronke, S.
  • Partridge, L.
(2019) Nat Metab, 1, 11, 1059-1073

Lipid signalling drives proteolytic rewiring of mitochondria by YME1L

  • MacVicar, T.
  • Ohba, Y.
  • Nolte, H.
  • Mayer, F. C.
  • Tatsuta, T.
  • Sprenger, H. G.
  • Lindner, B.
  • Zhao, Y.
  • Li, J.
  • Bruns, C.
  • Kruger, M.
  • Habich, M.
  • Riemer, J.
  • Schwarzer, R.
  • Pasparakis, M.
  • Henschke, S.
  • Bruning, J. C.
  • Zamboni, N.
  • Langer, T.
(2019) Nature, 575, 7782, 361-365

The mitochondrial intermembrane space-facing proteins Mcp2 and Tgl2 are involved in yeast lipid metabolism

  • Odendall, F.
  • Backes, S.
  • Tatsuta, T.
  • Weill, U.
  • Schuldiner, M.
  • Langer, T.
  • Herrmann, J. M.
  • Rapaport, D.
  • Dimmer, K. S.
(2019) Mol Biol Cell, 30, 21, 2681-2694

The Good and the Bad of Mitochondrial Breakups

  • Sprenger, H. G.
  • Langer, T.
(2019) Trends Cell Biol, 29, 11, 888-900

Walter Neupert (1939-2019), a pioneer of mitochondrial biogenesis and morphology

  • Lill, R.
  • Langer, T.
  • Herrmann, J. M.
(2019) EMBO J, 38, 17, e103100

Astrocyte-specific deletion of the mitochondrial m-AAA protease reveals glial contribution to neurodegeneration

  • Murru, S.
  • Hess, S.
  • Barth, E.
  • Almajan, E. R.
  • Schatton, D.
  • Hermans, S.
  • Brodesser, S.
  • Langer, T.
  • Kloppenburg, P.
  • Rugarli, E. I.
(2019) Glia, 67, 8, 1526-1541

Mitochondrial Proteolysis and Metabolic Control

  • Ahola, S.
  • Langer, T.
  • MacVicar, T.
(2019) Cold Spring Harb Perspect Biol, 11, 7

CerS6-Derived Sphingolipids Interact with Mff and Promote Mitochondrial Fragmentation in Obesity

  • Hammerschmidt, P.
  • Ostkotte, D.
  • Nolte, H.
  • Gerl, M. J.
  • Jais, A.
  • Brunner, H. L.
  • Sprenger, H. G.
  • Awazawa, M.
  • Nicholls, H. T.
  • Turpin-Nolan, S. M.
  • Langer, T.
  • Kruger, M.
  • Brugger, B.
  • Bruning, J. C.
(2019) Cell, 177, 6, 1536-1552 e23

Structural determinants of lipid specificity within Ups/PRELI lipid transfer proteins

  • Miliara, X.
  • Tatsuta, T.
  • Berry, J. L.
  • Rouse, S. L.
  • Solak, K.
  • Chorev, D. S.
  • Wu, D.
  • Robinson, C. V.
  • Matthews, S.
  • Langer, T.
(2019) Nat Commun, 10, 1, 1130

ROMO1 is a constituent of the human presequence translocase required for YME1L protease import

  • Richter, F.
  • Dennerlein, S.
  • Nikolov, M.
  • Jans, D. C.
  • Naumenko, N.
  • Aich, A.
  • MacVicar, T.
  • Linden, A.
  • Jakobs, S.
  • Urlaub, H.
  • Langer, T.
  • Rehling, P.
(2019) J Cell Biol, 218, 2, 598-614

Food Perception Primes Hepatic ER Homeostasis via Melanocortin-Dependent Control of mTOR Activation

  • Brandt, C.
  • Nolte, H.
  • Henschke, S.
  • Engstrom Ruud, L.
  • Awazawa, M.
  • Morgan, D. A.
  • Gabel, P.
  • Sprenger, H. G.
  • Hess, M. E.
  • Gunther, S.
  • Langer, T.
  • Rahmouni, K.
  • Fenselau, H.
  • Kruger, M.
  • Bruning, J. C.
(2018) Cell, 175, 5, 1321-1335 e20

Lipin1 deficiency causes sarcoplasmic reticulum stress and chaperone-responsive myopathy

  • Rashid, T.
  • Nemazanyy, I.
  • Paolini, C.
  • Tatsuta, T.
  • Crespin, P.
  • de Villeneuve, D.
  • Brodesser, S.
  • Benit, P.
  • Rustin, P.
  • Baraibar, M. A.
  • Agbulut, O.
  • Olivier, A.
  • Protasi, F.
  • Langer, T.
  • Chrast, R.
  • de Lonlay, P.
  • de Foucauld, H.
  • Blaauw, B.
  • Pende, M.
(2018) EMBO J, 38, 1, e99576

Loss of the mitochondrial i-AAA protease YME1L leads to ocular dysfunction and spinal axonopathy

  • Sprenger, H. G.
  • Wani, G.
  • Hesseling, A.
  • Konig, T.
  • Patron, M.
  • MacVicar, T.
  • Ahola, S.
  • Wai, T.
  • Barth, E.
  • Rugarli, E. I.
  • Bergami, M.
  • Langer, T.
(2018) EMBO Mol Med, 11, 1, e9288

Hepatic leptin receptor expression can partially compensate for IL-6Rα deficiency in DEN-induced hepatocellular carcinoma

  • Mittenbühler, M. J.
  • Sprenger, H. G.
  • Gruber, S.
  • Wunderlich, C. M.
  • Kern, L.
  • Brüning, J. C.
  • Wunderlich, F. T.
(2018) Mol Metab, 17: 122-133

Modular ssDNA binding and inhibition of telomerase activity by designer PPR proteins

  • Spahr, H.
  • Chia, T.
  • Lingford, J. P.
  • Siira, S. J.
  • Cohen, S. B.
  • Filipovska, A.
  • Rackham, O.
(2018) Nat Commun, 9(1): 2212

m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration

  • Patron, M.
  • Sprenger, H. G.
  • Langer, T.
(2018) Cell Res, 28, 3, 296-306

PARL partitions the lipid transfer protein STARD7 between the cytosol and mitochondria

  • Saita, S.
  • Tatsuta, T.
  • Lampe, P. A.
  • Konig, T.
  • Ohba, Y.
  • Langer, T.
(2018) EMBO J, 37, 4, e97909

Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the TIM22 Protein Translocase in Mitochondria

  • Vukotic, M.
  • Nolte, H.
  • Konig, T.
  • Saita, S.
  • Ananjew, M.
  • Kruger, M.
  • Tatsuta, T.
  • Langer, T.
(2017) Mol Cell, 67, 3, 471-483 e7

Prohibitins

  • Tatsuta, T.
  • Langer, T.
(2017) Curr Biol, 27, 13, R629-R631

PARL mediates Smac proteolytic maturation in mitochondria to promote apoptosis

  • Saita, S.
  • Nolte, H.
  • Fiedler, K. U.
  • Kashkar, H.
  • Venne, A. S.
  • Zahedi, R. P.
  • Kruger, M.
  • Langer, T.
(2017) Nat Cell Biol, 19, 4, 318-328

Intramitochondrial phospholipid trafficking

  • Tatsuta, T.
  • Langer, T.
(2017) Biochim Biophys Acta, 1862, 1, 81-89

The Mitochondrial m-AAA Protease Prevents Demyelination and Hair Greying

  • Wang, S.
  • Jacquemyn, J.
  • Murru, S.
  • Martinelli, P.
  • Barth, E.
  • Langer, T.
  • Niessen, C. M.
  • Rugarli, E. I.
(2016) PLoS Genet, 12, 12, e1006463

The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i-AAA protease YME1L

  • Wai, T.
  • Saita, S.
  • Nolte, H.
  • Muller, S.
  • Konig, T.
  • Richter-Dennerlein, R.
  • Sprenger, H. G.
  • Madrenas, J.
  • Muhlmeister, M.
  • Brandt, U.
  • Kruger, M.
  • Langer, T.
(2016) EMBO Rep, 17, 12, 1844-1856

The m-AAA Protease Associated with Neurodegeneration Limits MCU Activity in Mitochondria

  • Koenig, T.
  • Troder, S. E.
  • Bakka, K.
  • Korwitz, A.
  • Richter-Dennerlein, R.
  • Lampe, P. A.
  • Patron, M.
  • Muhlmeister, M.
  • Guerrero-Castillo, S.
  • Brandt, U.
  • Decker, T.
  • Lauria, I.
  • Paggio, A.
  • Rizzuto, R.
  • Rugarli, E. I.
  • De Stefani, D.
  • Langer, T.
(2016) Mol Cell, 64, 1, 148-162

Deficiency of HTRA2/Omi is associated with infantile neurodegeneration and 3-methylglutaconic aciduria

  • Mandel, H.
  • Saita, S.
  • Edvardson, S.
  • Jalas, C.
  • Shaag, A.
  • Goldsher, D.
  • Vlodavsky, E.
  • Langer, T.
  • Elpeleg, O.
(2016) J Med Genet, 53, 10, 690-6

Homozygous YME1L1 mutation causes mitochondriopathy with optic atrophy and mitochondrial network fragmentation

  • Hartmann, B.
  • Wai, T.
  • Hu, H.
  • MacVicar, T.
  • Musante, L.
  • Fischer-Zirnsak, B.
  • Stenzel, W.
  • Graf, R.
  • van den Heuvel, L.
  • Ropers, H. H.
  • Wienker, T. F.
  • Hubner, C.
  • Langer, T.
  • Kaindl, A. M.
(2016) Elife, 5

OPA1 processing in cell death and disease - the long and short of it

  • MacVicar, T.
  • Langer, T.
(2016) J Cell Sci, 129, 12, 2297-306

MICOS and phospholipid transfer by Ups2-Mdm35 organize membrane lipid synthesis in mitochondria

  • Aaltonen, M. J.
  • Friedman, J. R.
  • Osman, C.
  • Salin, B.
  • di Rago, J. P.
  • Nunnari, J.
  • Langer, T.
  • Tatsuta, T.
(2016) J Cell Biol, 213, 5, 525-34

Mitochondrial Dynamics and Metabolic Regulation

  • Wai, T.
  • Langer, T.
(2016) Trends Endocrinol Metab, 27, 2, 105-17

Loss of OMA1 delays neurodegeneration by preventing stress-induced OPA1 processing in mitochondria

  • Korwitz, A.
  • Merkwirth, C.
  • Richter-Dennerlein, R.
  • Troder, S. E.
  • Sprenger, H. G.
  • Quiros, P. M.
  • Lopez-Otin, C.
  • Rugarli, E. I.
  • Langer, T.
(2016) J Cell Biol, 212, 2, 157-66

Interaction of MDM33 with mitochondrial inner membrane homeostasis pathways in yeast

  • Klecker, T.
  • Wemmer, M.
  • Haag, M.
  • Weig, A.
  • Bockler, S.
  • Langer, T.
  • Nunnari, J.
  • Westermann, B.
(2015) Sci Rep, 5, 18344

A novel prohibitin-binding compound induces the mitochondrial apoptotic pathway through NOXA and BIM upregulation

  • Moncunill-Massaguer, C.
  • Saura-Esteller, J.
  • Perez-Perarnau, A.
  • Palmeri, C. M.
  • Nunez-Vazquez, S.
  • Cosialls, A. M.
  • Gonzalez-Girones, D. M.
  • Pomares, H.
  • Korwitz, A.
  • Preciado, S.
  • Albericio, F.
  • Lavilla, R.
  • Pons, G.
  • Langer, T.
  • Iglesias-Serret, D.
  • Gil, J.
(2015) Oncotarget, 6, 39, 41750-65

Imbalanced OPA1 processing and mitochondrial fragmentation cause heart failure in mice

  • Wai, T.
  • Garcia-Prieto, J.
  • Baker, M. J.
  • Merkwirth, C.
  • Benit, P.
  • Rustin, P.
  • Ruperez, F. J.
  • Barbas, C.
  • Ibanez, B.
  • Langer, T.
(2015) Science, 350, 6265, aad0116

Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes

  • Miliara, X.
  • Garnett, J. A.
  • Tatsuta, T.
  • Abid Ali, F.
  • Baldie, H.
  • Perez-Dorado, I.
  • Simpson, P.
  • Yague, E.
  • Langer, T.
  • Matthews, S.
(2015) EMBO Rep, 16, 7, 824-35

Transcriptional activation of LON Gene by a new form of mitochondrial stress: A role for the nuclear respiratory factor 2 in StAR overload response (SOR)

  • Bahat, A.
  • Perlberg, S.
  • Melamed-Book, N.
  • Isaac, S.
  • Eden, A.
  • Lauria, I.
  • Langer, T.
  • Orly, J.
(2015) Mol Cell Endocrinol, 408, 62-72

New roles for mitochondrial proteases in health, ageing and disease

  • Quiros, P. M.
  • Langer, T.
  • Lopez-Otin, C.
(2015) Nat Rev Mol Cell Biol, 16, 6, 345-59

Stomatin-like protein 2 is required for in vivo mitochondrial respiratory chain supercomplex formation and optimal cell function

  • Mitsopoulos, P.
  • Chang, Y. H.
  • Wai, T.
  • Konig, T.
  • Dunn, S. D.
  • Langer, T.
  • Madrenas, J.
(2015) Mol Cell Biol, 35, 10, 1838-47

An atypical form of AOA2 with myoclonus associated with mutations in SETX and AFG3L2

  • Mancini, C.
  • Orsi, L.
  • Guo, Y.
  • Li, J.
  • Chen, Y.
  • Wang, F.
  • Tian, L.
  • Liu, X.
  • Zhang, J.
  • Jiang, H.
  • Nmezi, B. S.
  • Tatsuta, T.
  • Giorgio, E.
  • Di Gregorio, E.
  • Cavalieri, S.
  • Pozzi, E.
  • Mortara, P.
  • Caglio, M. M.
  • Balducci, A.
  • Pinessi, L.
  • Langer, T.
  • Padiath, Q. S.
  • Hakonarson, H.
  • Zhang, X.
  • Brusco, A.
(2015) BMC Med Genet, 16, 16

Inhibition of insulin/IGF-1 receptor signaling protects from mitochondria-mediated kidney failure

  • Ising, C.
  • Koehler, S.
  • Brahler, S.
  • Merkwirth, C.
  • Hohne, M.
  • Baris, O. R.
  • Hagmann, H.
  • Kann, M.
  • Fabretti, F.
  • Dafinger, C.
  • Bloch, W.
  • Schermer, B.
  • Linkermann, A.
  • Bruning, J. C.
  • Kurschat, C. E.
  • Muller, R. U.
  • Wiesner, R. J.
  • Langer, T.
  • Benzing, T.
  • Brinkkoetter, P. T.
(2015) EMBO Mol Med, 7, 3, 275-87

Organization of Mitochondrial Gene Expression in Two Distinct Ribosome-Containing Assemblies

  • Kehrein, K.
  • Schilling, R.
  • Moller-Hergt, B. V.
  • Wurm, C. A.
  • Jakobs, S.
  • Lamkemeyer, T.
  • Langer, T.
  • Ott, M.
(2015) Cell Rep, 10, 6, 843-853

DNAJC19, a mitochondrial cochaperone associated with cardiomyopathy, forms a complex with prohibitins to regulate cardiolipin remodeling

  • Richter-Dennerlein, R.
  • Korwitz, A.
  • Haag, M.
  • Tatsuta, T.
  • Dargazanli, S.
  • Baker, M.
  • Decker, T.
  • Lamkemeyer, T.
  • Rugarli, E. I.
  • Langer, T.
(2014) Cell Metab, 20, 1, 158-71

SPG7 variant escapes phosphorylation-regulated processing by AFG3L2, elevates mitochondrial ROS, and is associated with multiple clinical phenotypes

  • Almontashiri, N. A.
  • Chen, H. H.
  • Mailloux, R. J.
  • Tatsuta, T.
  • Teng, A. C.
  • Mahmoud, A. B.
  • Ho, T.
  • Stewart, N. A.
  • Rippstein, P.
  • Harper, M. E.
  • Roberts, R.
  • Willenborg, C.
  • Erdmann, J.
  • C. ARDIoGRAM Consortium
  • Pastore, A.
  • McBride, H. M.
  • Langer, T.
  • Stewart, A. F.
(2014) Cell Rep, 7, 3, 834-47

Loss of the m-AAA protease subunit AFG(3)L(2) causes mitochondrial transport defects and tau hyperphosphorylation

  • Kondadi, A. K.
  • Wang, S.
  • Montagner, S.
  • Kladt, N.
  • Korwitz, A.
  • Martinelli, P.
  • Herholz, D.
  • Baker, M. J.
  • Schauss, A. C.
  • Langer, T.
  • Rugarli, E. I.
(2014) EMBO J, 33, 9, 1011-26

Familial Alzheimer's disease-associated presenilin-1 alters cerebellar activity and calcium homeostasis

  • Sepulveda-Falla, D.
  • Barrera-Ocampo, A.
  • Hagel, C.
  • Korwitz, A.
  • Vinueza-Veloz, M. F.
  • Zhou, K.
  • Schonewille, M.
  • Zhou, H.
  • Velazquez-Perez, L.
  • Rodriguez-Labrada, R.
  • Villegas, A.
  • Ferrer, I.
  • Lopera, F.
  • Langer, T.
  • De Zeeuw, C. I.
  • Glatzel, M.
(2014) J Clin Invest, 124, 4, 1552-67

Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics

  • Baker, M. J.
  • Lampe, P. A.
  • Stojanovski, D.
  • Korwitz, A.
  • Anand, R.
  • Tatsuta, T.
  • Langer, T.
(2014) EMBO J, 33, 6, 578-93

The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission

  • Anand, R.
  • Wai, T.
  • Baker, M. J.
  • Kladt, N.
  • Schauss, A. C.
  • Rugarli, E.
  • Langer, T.
(2014) J Cell Biol, 204, 6, 919-29

Dynamic survey of mitochondria by ubiquitin

  • Escobar-Henriques, M.
  • Langer, T.
(2014) EMBO Rep, 15, 3, 231-43

StAR enhances transcription of genes encoding the mitochondrial proteases involved in its own degradation

  • Bahat, A.
  • Perlberg, S.
  • Melamed-Book, N.
  • Lauria, I.
  • Langer, T.
  • Orly, J.
(2014) Mol Endocrinol, 28, 2, 208-24

Mitochondrial lipid trafficking

  • Tatsuta, T.
  • Scharwey, M.
  • Langer, T.
(2014) Trends Cell Biol, 24, 1, 44-52

The seven wonders of ubiquitin: a multi-interview: Personal insights into the ubiquitin field. Interview by Nonia Pariente

  • Dikic, I.
  • Harper, W.
  • Hay, R.
  • Langer, T.
  • Rape, M.
  • Sixma, T.
  • Walczak, H.
(2014) EMBO Rep, 15, 1, 7-11

Mitochondrial lipid transport at a glance

  • Scharwey, M.
  • Tatsuta, T.
  • Langer, T.
(2013) J Cell Sci, 126, Pt 23, 5317-23

Loss of prohibitin induces mitochondrial damages altering beta-cell function and survival and is responsible for gradual diabetes development

  • Supale, S.
  • Thorel, F.
  • Merkwirth, C.
  • Gjinovci, A.
  • Herrera, P. L.
  • Scorrano, L.
  • Meda, P.
  • Langer, T.
  • Maechler, P.
(2013) Diabetes, 62, 10, 3488-99

TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid

  • Potting, C.
  • Tatsuta, T.
  • Konig, T.
  • Haag, M.
  • Wai, T.
  • Aaltonen, M. J.
  • Langer, T.
(2013) Cell Metab, 18, 2, 287-95

The E3 ligase parkin maintains mitochondrial integrity by increasing linear ubiquitination of NEMO

  • Muller-Rischart, A. K.
  • Pilsl, A.
  • Beaudette, P.
  • Patra, M.
  • Hadian, K.
  • Funke, M.
  • Peis, R.
  • Deinlein, A.
  • Schweimer, C.
  • Kuhn, P. H.
  • Lichtenthaler, S. F.
  • Motori, E.
  • Hrelia, S.
  • Wurst, W.
  • Trumbach, D.
  • Langer, T.
  • Krappmann, D.
  • Dittmar, G.
  • Tatzelt, J.
  • Winklhofer, K. F.
(2013) Mol Cell, 49, 5, 908-21

Two deubiquitylases act on mitofusin and regulate mitochondrial fusion along independent pathways

  • Anton, F.
  • Dittmar, G.
  • Langer, T.
  • Escobar-Henriques, M.
(2013) Mol Cell, 49, 3, 487-98

Proteolytic control of mitochondrial function and morphogenesis

  • Anand, R.
  • Langer, T.
  • Baker, M. J.
(2013) Biochim Biophys Acta, 1833, 1, 195-204

Rushhour – Phospholipidtransport an mitochondrialen Membranen.

  • Potting, C.
  • Langer, T.
(2013) Biospektrum: 19-21

ATP23 Peptidase

  • Wilmes, C.
  • Langer, T.
(2013) Handbook of Proteo¬lytic Enzymes (Third Ed): 1688-1690

The mitochondrial amidoxime-reducing component (mARC1) is a novel signal-anchored protein of the outer mitochondrial membrane

  • Klein, J. M.
  • Busch, J. D.
  • Potting, C.
  • Baker, M. J.
  • Langer, T.
  • Schwarz, G.
(2012) J Biol Chem, 287, 51, 42795-803

Impaired folding of the mitochondrial small TIM chaperones induces clearance by the i-AAA protease

  • Baker, M. J.
  • Mooga, V. P.
  • Guiard, B.
  • Langer, T.
  • Ryan, M. T.
  • Stojanovski, D.
(2012) J Mol Biol, 424, 5, 227-39

Loss of prohibitin membrane scaffolds impairs mitochondrial architecture and leads to tau hyperphosphorylation and neurodegeneration

  • Merkwirth, C.
  • Martinelli, P.
  • Korwitz, A.
  • Morbin, M.
  • Bronneke, H. S.
  • Jordan, S. D.
  • Rugarli, E. I.
  • Langer, T.
(2012) PLoS Genet, 8, 11, e1003021

Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein

  • Connerth, M.
  • Tatsuta, T.
  • Haag, M.
  • Klecker, T.
  • Westermann, B.
  • Langer, T.
(2012) Science, 338, 6108, 815-8

AFG3L2 supports mitochondrial protein synthesis and Purkinje cell survival

  • Almajan, E. R.
  • Richter, R.
  • Paeger, L.
  • Martinelli, P.
  • Barth, E.
  • Decker, T.
  • Larsson, N. G.
  • Kloppenburg, P.
  • Langer, T.
  • Rugarli, E. I.
(2012) J Clin Invest, 122, 11, 4048-58

Mitochondrial quality control: a matter of life and death for neurons

  • Rugarli, E. I.
  • Langer, T.
(2012) EMBO J, 31, 6, 1336-49

Mitochondrial AAA proteases--towards a molecular understanding of membrane-bound proteolytic machines

  • Gerdes, F.
  • Tatsuta, T.
  • Langer, T.
(2012) Biochim Biophys Acta, 1823, 1, 49-55

The i-AAA Protease

  • Wai, T.
  • Langer, T.
(2012) Handbook of Proteo¬lytic Enzymes (Third Ed): 1-7

Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases

  • Pierson, T. M.
  • Adams, D.
  • Bonn, F.
  • Martinelli, P.
  • Cherukuri, P. F.
  • Teer, J. K.
  • Hansen, N. F.
  • Cruz, P.
  • Mullikin For The Nisc Comparative Sequencing Program, J. C.
  • Blakesley, R. W.
  • Golas, G.
  • Kwan, J.
  • Sandler, A.
  • Fuentes Fajardo, K.
  • Markello, T.
  • Tifft, C.
  • Blackstone, C.
  • Rugarli, E. I.
  • Langer, T.
  • Gahl, W. A.
  • Toro, C.
(2011) PLoS Genet, 7, 10, e1002325

The mitochondrial electron transport chain is dispensable for proliferation and differentiation of epidermal progenitor cells

  • Baris, O. R.
  • Klose, A.
  • Kloepper, J. E.
  • Weiland, D.
  • Neuhaus, J. F.
  • Schauen, M.
  • Wille, A.
  • Muller, A.
  • Merkwirth, C.
  • Langer, T.
  • Larsson, N. G.
  • Krieg, T.
  • Tobin, D. J.
  • Paus, R.
  • Wiesner, R. J.
(2011) Stem Cells, 29, 9, 1459-68

Targeting capacity and conservation of PreP homologues localization in mitochondria of different species

  • Alikhani, N.
  • Berglund, A. K.
  • Engmann, T.
  • Spanning, E.
  • Vogtle, F. N.
  • Pavlov, P.
  • Meisinger, C.
  • Langer, T.
  • Glaser, E.
(2011) J Mol Biol, 410, 3, 400-10

Quality control of mitochondrial proteostasis

  • Baker, M. J.
  • Tatsuta, T.
  • Langer, T.
(2011) Cold Spring Harb Perspect Biol, 3, 7

Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria

  • Bonn, F.
  • Tatsuta, T.
  • Petrungaro, C.
  • Riemer, J.
  • Langer, T.
(2011) EMBO J, 30, 13, 2545-56

Ugo1 and Mdm30 act sequentially during Fzo1-mediated mitochondrial outer membrane fusion

  • Anton, F.
  • Fres, J. M.
  • Schauss, A.
  • Pinson, B.
  • Praefcke, G. J.
  • Langer, T.
  • Escobar-Henriques, M.
(2011) J Cell Sci, 124, Pt 7, 1126-35

Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease

  • Lee, S.
  • Augustin, S.
  • Tatsuta, T.
  • Gerdes, F.
  • Langer, T.
  • Tsai, F. T.
(2011) J Biol Chem, 286, 6, 4404-11

Making heads or tails of phospholipids in mitochondria

  • Osman, C.
  • Voelker, D. R.
  • Langer, T.
(2011) J Cell Biol, 192, 1, 7-16

The life of proteins: the good, the mostly good and the ugly

  • Morimoto, R. I.
  • Driessen, A. J.
  • Hegde, R. S.
  • Langer, T.
(2011) Nat Struct Mol Biol, 18, 1, 1-4

Highlight: The biology of aging: mechanisms and intervention

  • Bruning, J.
  • Langer, T.
  • Trifunovic, A.
(2010) Biol Chem, 391, 10, 1113

Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35

  • Potting, C.
  • Wilmes, C.
  • Engmann, T.
  • Osman, C.
  • Langer, T.
(2010) EMBO J, 29, 17, 2888-98

A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP phosphatase Gep4

  • Osman, C.
  • Haag, M.
  • Wieland, F. T.
  • Brugger, B.
  • Langer, T.
(2010) EMBO J, 29, 12, 1976-87

Functional evaluation of paraplegin mutations by a yeast complementation assay

  • Bonn, F.
  • Pantakani, K.
  • Shoukier, M.
  • Langer, T.
  • Mannan, A. U.
(2010) Hum Mutat, 31, 5, 617-21

Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28

  • Di Bella, D.
  • Lazzaro, F.
  • Brusco, A.
  • Plumari, M.
  • Battaglia, G.
  • Pastore, A.
  • Finardi, A.
  • Cagnoli, C.
  • Tempia, F.
  • Frontali, M.
  • Veneziano, L.
  • Sacco, T.
  • Boda, E.
  • Brussino, A.
  • Bonn, F.
  • Castellotti, B.
  • Baratta, S.
  • Mariotti, C.
  • Gellera, C.
  • Fracasso, V.
  • Magri, S.
  • Langer, T.
  • Plevani, P.
  • Di Donato, S.
  • Muzi-Falconi, M.
  • Taroni, F.
(2010) Nat Genet, 42, 4, 313-21

Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1

  • Ehses, S.
  • Raschke, I.
  • Mancuso, G.
  • Bernacchia, A.
  • Geimer, S.
  • Tondera, D.
  • Martinou, J. C.
  • Westermann, B.
  • Rugarli, E. I.
  • Langer, T.
(2009) J Cell Biol, 187, 7, 1023-36

Prohibitins and the functional compartmentalization of mitochondrial membranes

  • Osman, C.
  • Merkwirth, C.
  • Langer, T.
(2009) J Cell Sci, 122, Pt 21, 3823-30

AAA proteases in mitochondria: diverse functions of membrane-bound proteolytic machines

  • Tatsuta, T.
  • Langer, T.
(2009) Res Microbiol, 160, 9, 711-7

Autocatalytic processing of m-AAA protease subunits in mitochondria

  • Koppen, M.
  • Bonn, F.
  • Ehses, S.
  • Langer, T.
(2009) Mol Biol Cell, 20, 19, 4216-24

An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases

  • Augustin, S.
  • Gerdes, F.
  • Lee, S.
  • Tsai, F. T.
  • Langer, T.
  • Tatsuta, T.
(2009) Mol Cell, 35, 5, 574-85

SLP-2 is required for stress-induced mitochondrial hyperfusion

  • Tondera, D.
  • Grandemange, S.
  • Jourdain, A.
  • Karbowski, M.
  • Mattenberger, Y.
  • Herzig, S.
  • Da Cruz, S.
  • Clerc, P.
  • Raschke, I.
  • Merkwirth, C.
  • Ehses, S.
  • Krause, F.
  • Chan, D. C.
  • Alexander, C.
  • Bauer, C.
  • Youle, R.
  • Langer, T.
  • Martinou, J. C.
(2009) EMBO J, 28, 11, 1589-600

The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria

  • Osman, C.
  • Haag, M.
  • Potting, C.
  • Rodenfels, J.
  • Dip, P. V.
  • Wieland, F. T.
  • Brugger, B.
  • Westermann, B.
  • Langer, T.
(2009) J Cell Biol, 184, 4, 583-96

Prohibitin function within mitochondria: essential roles for cell proliferation and cristae morphogenesis

  • Merkwirth, C.
  • Langer, T.
(2009) Biochim Biophys Acta, 1793, 1, 27-32

The recognition of substrates by AAA proteases in mitochondria.

  • Graef, M.
  • Langer, T.
  • Engmann, T.
(2009) ATP-dependent proteases: 179-195

Mitofusin 2 builds a bridge between ER and mitochondria

  • Merkwirth, C.
  • Langer, T.
(2008) Cell, 135, 7, 1165-7

Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondria

  • Merkwirth, C.
  • Dargazanli, S.
  • Tatsuta, T.
  • Geimer, S.
  • Lower, B.
  • Wunderlich, F. T.
  • von Kleist-Retzow, J. C.
  • Waisman, A.
  • Westermann, B.
  • Langer, T.
(2008) Genes Dev, 22, 4, 476-88

Quality control of mitochondria: protection against neurodegeneration and ageing

  • Tatsuta, T.
  • Langer, T.
(2008) EMBO J, 27, 2, 306-14

Studying proteolysis within mitochondria

  • Tatsuta, T.
  • Langer, T.
(2007) Methods Mol Biol, 372, 343-60

OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria

  • Duvezin-Caubet, S.
  • Koppen, M.
  • Wagener, J.
  • Zick, M.
  • Israel, L.
  • Bernacchia, A.
  • Jagasia, R.
  • Rugarli, E. I.
  • Imhof, A.
  • Neupert, W.
  • Langer, T.
  • Reichert, A. S.
(2007) Mol Biol Cell, 18, 9, 3582-90

Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases

  • Koppen, M.
  • Langer, T.
(2007) Crit Rev Biochem Mol Biol, 42, 3, 221-42

Substrate recognition by AAA+ ATPases: distinct substrate binding modes in ATP-dependent protease Yme1 of the mitochondrial intermembrane space

  • Graef, M.
  • Seewald, G.
  • Langer, T.
(2007) Mol Cell Biol, 27, 7, 2476-85

m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria

  • Tatsuta, T.
  • Augustin, S.
  • Nolden, M.
  • Friedrichs, B.
  • Langer, T.
(2007) EMBO J, 26, 2, 325-35

Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase

  • Osman, C.
  • Wilmes, C.
  • Tatsuta, T.
  • Langer, T.
(2007) Mol Biol Cell, 18, 2, 627-35

Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia

  • Koppen, M.
  • Metodiev, M. D.
  • Casari, G.
  • Rugarli, E. I.
  • Langer, T.
(2007) Mol Cell Biol, 27, 2, 758-67

Substrate specific consequences of central pore mutations in the i-AAA protease Yme1 on substrate engagement

  • Graef, M.
  • Langer, T.
(2006) J Struct Biol, 156, 1, 101-8

Nonredundant roles of mitochondria-associated F-box proteins Mfb1 and Mdm30 in maintenance of mitochondrial morphology in yeast

  • Durr, M.
  • Escobar-Henriques, M.
  • Merz, S.
  • Geimer, S.
  • Langer, T.
  • Westermann, B.
(2006) Mol Biol Cell, 17, 9, 3745-55

Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1

  • Escobar-Henriques, M.
  • Westermann, B.
  • Langer, T.
(2006) J Cell Biol, 173, 5, 645-50

Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia

  • Rugarli, E. I.
  • Langer, T.
(2006) Trends Mol Med, 12, 6, 262-9

Mitochondrial shaping cuts

  • Escobar-Henriques, M.
  • Langer, T.
(2006) Biochim Biophys Acta, 1763, 5-6, 422-9

Evidence for a novel mitochondria-to-nucleus signalling pathway in respiring cells lacking i-AAA protease and the ABC-transporter Mdl1

  • Arnold, I.
  • Wagner-Ecker, M.
  • Ansorge, W.
  • Langer, T.
(2006) Gene, 367, 74-88

Quality control in the mitochondrion

  • Nolden, M.
  • Kisters-Woike, B.
  • Langer, T.
  • Graef, M.
(2006) Topics in Current Genetics 16: 119-147

The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria

  • Nolden, M.
  • Ehses, S.
  • Koppen, M.
  • Bernacchia, A.
  • Rugarli, E. I.
  • Langer, T.
(2005) Cell, 123, 2, 277-89

Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria

  • Kambacheld, M.
  • Augustin, S.
  • Tatsuta, T.
  • Muller, S.
  • Langer, T.
(2005) J Biol Chem, 280, 20, 20132-9

Characterization of peptides released from mitochondria: evidence for constant proteolysis and peptide efflux

  • Augustin, S.
  • Nolden, M.
  • Muller, S.
  • Hardt, O.
  • Arnold, I.
  • Langer, T.
(2005) J Biol Chem, 280, 4, 2691-9

Formation of membrane-bound ring complexes by prohibitins in mitochondria

  • Tatsuta, T.
  • Model, K.
  • Langer, T.
(2005) Mol Biol Cell, 16, 1, 248-59

Reversible assembly of the ATP-binding cassette transporter Mdl1 with the F1F0-ATP synthase in mitochondria

  • Galluhn, D.
  • Langer, T.
(2004) J Biol Chem, 279, 37, 38338-45

Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits

  • Korbel, D.
  • Wurth, S.
  • Kaser, M.
  • Langer, T.
(2004) EMBO Rep, 5, 7, 698-703

PIM1 mitochondrial endopeptidase

  • Langer, T.
(2004) Handbook of Proteolytic Enzymes, 2: 2004-2006

Protein quality control in mitochondria and neurodegeneration in hereditary spastic paraplegia

  • Bross, P.
  • Rugarli, E. I.
  • Casari, G.
  • Langer, T.
(2004) Topics Curr. Gen, 8, 97-121

Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia

  • Atorino, L.
  • Silvestri, L.
  • Koppen, M.
  • Cassina, L.
  • Ballabio, A.
  • Marconi, R.
  • Langer, T.
  • Casari, G.
(2003) J Cell Biol, 163, 4, 777-87

Oma1, a novel membrane-bound metallopeptidase in mitochondria with activities overlapping with the m-AAA protease

  • Kaser, M.
  • Kambacheld, M.
  • Kisters-Woike, B.
  • Langer, T.
(2003) J Biol Chem, 278, 47, 46414-23

Membrane protein degradation by AAA proteases in mitochondria

  • Arnold, I.
  • Langer, T.
(2002) Biochim Biophys Acta, 1592, 1, 89-96

MAP-1 and IAP-1, two novel AAA proteases with catalytic sites on opposite membrane surfaces in mitochondrial inner membrane of Neurospora crassa

  • Klanner, C.
  • Prokisch, H.
  • Langer, T.
(2001) Mol Biol Cell, 12, 9, 2858-69

AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis

  • Langer, T.
  • Kaser, M.
  • Klanner, C.
  • Leonhard, K.
(2001) Biochem Soc Trans, 29, Pt 4, 431-6

Structural requirements of Tom40 for assembly into preexisting TOM complexes of mitochondria

  • Rapaport, D.
  • Taylor, R. D.
  • Kaser, M.
  • Langer, T.
  • Neupert, W.
  • Nargang, F. E.
(2001) Mol Biol Cell, 12, 5, 1189-98

Role of the ABC transporter Mdl1 in peptide export from mitochondria

  • Young, L.
  • Leonhard, K.
  • Tatsuta, T.
  • Trowsdale, J.
  • Langer, T.
(2001) Science, 291, 5511, 2135-8

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding

  • Krzewska, J.
  • Langer, T.
  • Liberek, K.
(2001) FEBS Lett, 489, 1, 92-6

Export von Peptiden aus Mitochondrien – ein neuer intrazellulärer Transportweg

  • Langer, T.
(2001) Biologie in unserer Zeit, 5: 330-331

Protein degradation in mitochondria

  • Kaser, M.
  • Langer, T.
(2000) Semin Cell Dev Biol, 11, 3, 181-90

AAA proteases: cellular machines for degrading membrane proteins

  • Langer, T.
(2000) Trends Biochem Sci, 25, 5, 247-51

Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface

  • Leonhard, K.
  • Guiard, B.
  • Pellecchia, G.
  • Tzagoloff, A.
  • Neupert, W.
  • Langer, T.
(2000) Mol Cell, 5, 4, 629-38

The chaperonin-related protein Tcm62p ensures mitochondrial gene expression under heat stress

  • Klanner, C.
  • Neupert, W.
  • Langer, T.
(2000) FEBS Lett, 470, 3, 365-9

ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae

  • Van Dyck, L.
  • Langer, T.
(1999) Cell Mol Life Sci, 56, 9-10, 825-42

Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria

  • Steglich, G.
  • Neupert, W.
  • Langer, T.
(1999) Mol Cell Biol, 19, 5, 3435-42

Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease

  • Leonhard, K.
  • Stiegler, A.
  • Neupert, W.
  • Langer, T.
(1999) Nature, 398, 6725, 348-51

Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae

  • van Dyck, L.
  • Dembowski, M.
  • Neupert, W.
  • Langer, T.
(1998) FEBS Lett, 438, 3, 250-4

The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease

  • Arlt, H.
  • Steglich, G.
  • Perryman, R.
  • Guiard, B.
  • Neupert, W.
  • Langer, T.
(1998) EMBO J, 17, 16, 4837-47

ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system

  • Savel'ev, A. S.
  • Novikova, L. A.
  • Kovaleva, I. E.
  • Luzikov, V. N.
  • Neupert, W.
  • Langer, T.
(1998) J Biol Chem, 273, 32, 20596-602

The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondria

  • van Dyck, L.
  • Neupert, W.
  • Langer, T.
(1998) Genes Dev, 12, 10, 1515-24

Autocatalytic processing of the ATP-dependent PIM1 protease: crucial function of a pro-region for sorting to mitochondria

  • Wagner, I.
  • van Dyck, L.
  • Savel'ev, A. S.
  • Neupert, W.
  • Langer, T.
(1997) EMBO J, 16, 24, 7317-25

Molecular chaperones in biology and medicine at Obernai

  • Bergeron, J. J.
  • Craig, E. A.
  • Horwich, A. L.
  • Langer, T.
  • Multhoff, G.
  • Smith, D. F.
  • Hightower, L. E.
(1997) Cell Stress Chaperones, 2, 4, 220-8

Saccharomyces cerevisiae Hsp78

  • Schmitt, M.
  • Langer, T.
(1997) Guidebook to Molecular Chaperones and Protein Folding Catalysts: 251-253

Functions of molecular chaperones in the biogenesis of mitochondria.

  • Langer, T.
  • Schwarz, E.
  • Neupert, W.
(1997) Guidebook to Molecular Chaperones and Protein Folding Catalysts: 499-506

Saccharomyces cerevisiae Hsp60

  • Langer, T.
  • Neupert, W.
(1997) Guidebook to Molecular Chaperones and Protein Folding Catalysts: 189-190

Degradation of membrane proteins by AAA proteases in mitochondria

  • Langer, T.
  • Leonhard, K.
  • Arlt, H.
  • Perryman, R.
  • Neupert, W.
(1997) Proteolysis in Cell func¬tions: 323-331

Regulated protein degradation in mitochondria

  • Langer, T.
  • Neupert, W.
(1996) Experientia, 52, 12, 1069-76

Mechanisms of protein import into mitochondria

  • Stuart, R. A.
  • Ono, H.
  • Langer, T.
  • Neupert, W.
(1996) Cell Struct Funct, 21, 5, 403-6

The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria

  • Schmitt, M.
  • Neupert, W.
  • Langer, T.
(1996) J Cell Biol, 134, 6, 1375-86

AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria

  • Leonhard, K.
  • Herrmann, J. M.
  • Stuart, R. A.
  • Mannhaupt, G.
  • Neupert, W.
  • Langer, T.
(1996) EMBO J, 15, 16, 4218-29

The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria

  • Arlt, H.
  • Tauer, R.
  • Feldmann, H.
  • Neupert, W.
  • Langer, T.
(1996) Cell, 85, 6, 875-85

Substitution of PIM1 protease in mitochondria by Escherichia coli Lon protease

  • Teichmann, U.
  • van Dyck, L.
  • Guiard, B.
  • Fischer, H.
  • Glockshuber, R.
  • Neupert, W.
  • Langer, T.
(1996) J Biol Chem, 271, 17, 10137-42

Chaperone function on Crete: a meeting report

  • Langer, T.
  • Buchner, J.
  • Bukau, B.
(1996) Cell Stress Chaperones, 1, 1, 5-12

Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation

  • Prip-Buus, C.
  • Westerman, B.
  • Schmitt, M.
  • Langer, T.
  • Neupert, W.
  • Schwarz, E.
(1996) FEBS Lett, 380, 1-2, 142-6

Chaperonin mediated folding and assembly of proteins in mitochondria.

  • Langer, T.
  • Neupert, W.
(1996) The Chaperonins: 91-106

Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70

  • Schmitt, M.
  • Neupert, W.
  • Langer, T.
(1995) EMBO J, 14, 14, 3434-44

Proteolytic breakdown of membrane-associated polypeptides in mitochondria of Saccharomyces cerevisiae

  • Langer, T.
  • Pajic, A.
  • Wagner, I.
  • Neupert, W.
(1995) Methods Enzymol, 260, 495-503

Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria

  • Wagner, I.
  • Arlt, H.
  • van Dyck, L.
  • Langer, T.
  • Neupert, W.
(1994) EMBO J, 13, 21, 5135-45

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

  • Szabo, A.
  • Langer, T.
  • Schroder, H.
  • Flanagan, J.
  • Bukau, B.
  • Hartl, F. U.
(1994) Proc Natl Acad Sci U S A, 91, 22, 10345-9

Yta10p, a member of a novel ATPase family in yeast, is essential for mitochondrial function

  • Tauer, R.
  • Mannhaupt, G.
  • Schnall, R.
  • Pajic, A.
  • Langer, T.
  • Feldmann, H.
(1994) FEBS Lett, 353, 2, 197-200

Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria

  • Pajic, A.
  • Tauer, R.
  • Feldmann, H.
  • Neupert, W.
  • Langer, T.
(1994) FEBS Lett, 353, 2, 201-6

DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70

  • Cyr, D. M.
  • Langer, T.
  • Douglas, M. G.
(1994) Trends Biochem Sci, 19, 4, 176-81

Molecular chaperones in protein folding: the art of avoiding sticky situations

  • Hartl, F. U.
  • Hlodan, R.
  • Langer, T.
(1994) Trends Biochem Sci, 19, 1, 20-5

Chaperoning mitochondrial biogenesis.

  • Langer, T.
  • Neupert, W.
(1994) Heat Shock Proteins: Structure, Function, and Regulation: 53-83

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

  • Martin, J.
  • Mayhew, M.
  • Langer, T.
  • Hartl, F. U.
(1993) Nature, 366, 6452, 228-33

Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides

  • Hendrick, J. P.
  • Langer, T.
  • Davis, T. A.
  • Hartl, F. U.
  • Wiedmann, M.
(1993) Proc Natl Acad Sci U S A, 90, 21, 10216-20

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage

  • Schroder, H.
  • Langer, T.
  • Hartl, F. U.
  • Bukau, B.
(1993) EMBO J, 12, 11, 4137-44

A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins

  • Gambill, B. D.
  • Voos, W.
  • Kang, P. J.
  • Miao, B.
  • Langer, T.
  • Craig, E. A.
  • Pfanner, N.
(1993) J Cell Biol, 123, 1, 109-17

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

  • Langer, T.
  • Pfeifer, G.
  • Martin, J.
  • Baumeister, W.
  • Hartl, F. U.
(1992) EMBO J, 11, 13, 4757-65

Formation and quantification of protein complexes between peroxisomal alcohol oxidase and GroEL

  • Evers, M. E.
  • Langer, T.
  • Harder, W.
  • Hartl, F. U.
  • Veenhuis, M.
(1992) FEBS Lett, 305, 1, 51-4

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

  • Langer, T.
  • Lu, C.
  • Echols, H.
  • Flanagan, J.
  • Hayer, M. K.
  • Hartl, F. U.
(1992) Nature, 356, 6371, 683-9

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

  • Martin, J.
  • Langer, T.
  • Boteva, R.
  • Schramel, A.
  • Horwich, A. L.
  • Hartl, F. U.
(1991) Nature, 352, 6330, 36-42

Heat shock proteins hsp60 and hsp70: their roles in folding, assembly and membrane translocation of proteins

  • Langer, T.
  • Neupert, W.
(1991) Curr Top Microbiol Immunol, 167, 3-30

Lactate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui

  • Hecht, K.
  • Langer, T.
  • Wrba, A.
  • Jaenicke, R.
(1990) Biol Chem Hoppe Seyler, 371, 6, 515-9