| Year |
Citation |
Score |
| 2020 |
Rotundo RL. Acetylcholinesterase at the Neuromuscular Junction. Neuroscience Letters. 135157. PMID 32540360 DOI: 10.1016/j.neulet.2020.135157 |
0.544 |
|
| 2018 |
Garcia S, Nissanka N, Mareco EA, Rossi S, Peralta S, Diaz F, Rotundo RL, Carvalho RF, Moraes CT. Overexpression of PGC-1α in aging muscle enhances a subset of young-like molecular patterns. Aging Cell. PMID 29427317 DOI: 10.1111/Acel.12707 |
0.403 |
|
| 2017 |
Rotundo RL. Biogenesis, assembly and trafficking of acetylcholinesterase. Journal of Neurochemistry. PMID 28326552 DOI: 10.1111/jnc.13982 |
0.478 |
|
| 2015 |
Ruiz CA, Rossi SG, Rotundo RL. Rescue and Stabilization of Acetylcholinesterase in Skeletal Muscle by N-terminal Peptides Derived from the Noncatalytic Subunits. The Journal of Biological Chemistry. 290: 20774-81. PMID 26139603 DOI: 10.1074/Jbc.M115.653741 |
0.744 |
|
| 2014 |
Wenz T, Rossi SG, Rotundo RL, Spiegelman BM, Moraes CT. Erratum: Increased muscle pgc-1αexpression protects from sarcopenia and metabolic disease during aging (Proceedings of the National Academy of Sciences of the United States of America (2009) 106 (20405-20410)) Proceedings of the National Academy of Sciences of the United States of America. 111. DOI: 10.1073/Pnas.1419095111 |
0.314 |
|
| 2013 |
Wang X, Pickrell AM, Rossi SG, Pinto M, Dillon LM, Hida A, Rotundo RL, Moraes CT. Transient systemic mtDNA damage leads to muscle wasting by reducing the satellite cell pool. Human Molecular Genetics. 22: 3976-86. PMID 23760083 DOI: 10.1093/Hmg/Ddt251 |
0.406 |
|
| 2012 |
Amenta AR, Creely HE, Mercado ML, Hagiwara H, McKechnie BA, Lechner BE, Rossi SG, Wang Q, Owens RT, Marrero E, Mei L, Hoch W, Young MF, McQuillan DJ, Rotundo RL, et al. Biglycan is an extracellular MuSK binding protein important for synapse stability. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 32: 2324-34. PMID 22396407 DOI: 10.1523/Jneurosci.4610-11.2012 |
0.721 |
|
| 2011 |
Marrero E, Rossi SG, Darr A, Tsoulfas P, Rotundo RL. Translational regulation of acetylcholinesterase by the RNA-binding protein Pumilio-2 at the neuromuscular synapse. The Journal of Biological Chemistry. 286: 36492-9. PMID 21865157 DOI: 10.1074/Jbc.M111.285510 |
0.746 |
|
| 2010 |
Rotundo RL. Neuromuscular Junction (NMJ): Acetylcholinesterases Encyclopedia of Neuroscience. 551-558. DOI: 10.1016/B978-008045046-9.01284-5 |
0.35 |
|
| 2009 |
Wenz T, Rossi SG, Rotundo RL, Spiegelman BM, Moraes CT. Increased muscle PGC-1alpha expression protects from sarcopenia and metabolic disease during aging. Proceedings of the National Academy of Sciences of the United States of America. 106: 20405-10. PMID 19918075 DOI: 10.1073/Pnas.0911570106 |
0.376 |
|
| 2009 |
Ruiz CA, Rotundo RL. Limiting role of protein disulfide isomerase in the expression of collagen-tailed acetylcholinesterase forms in muscle. The Journal of Biological Chemistry. 284: 31753-63. PMID 19758986 DOI: 10.1074/Jbc.M109.038471 |
0.75 |
|
| 2009 |
Ruiz CA, Rotundo RL. Dissociation of transcription, translation, and assembly of collagen-tailed acetylcholinesterase in skeletal muscle. The Journal of Biological Chemistry. 284: 21488-95. PMID 19509281 DOI: 10.1074/Jbc.M109.030049 |
0.75 |
|
| 2008 |
Rotundo RL, Ruiz CA, Marrero E, Kimbell LM, Rossi SG, Rosenberry T, Darr A, Tsoulfas P. Assembly and regulation of acetylcholinesterase at the vertebrate neuromuscular junction. Chemico-Biological Interactions. 175: 26-9. PMID 18599029 DOI: 10.1016/J.Cbi.2008.05.025 |
0.725 |
|
| 2005 |
Rotundo RL, Rossi SG, Kimbell LM, Ruiz C, Marrero E. Targeting acetylcholinesterase to the neuromuscular synapse. Chemico-Biological Interactions. 157: 15-21. PMID 16289417 DOI: 10.1016/J.Cbi.2005.10.007 |
0.729 |
|
| 2004 |
Kimbell LM, Ohno K, Engel AG, Rotundo RL. C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse. The Journal of Biological Chemistry. 279: 10997-1005. PMID 14702351 DOI: 10.1074/Jbc.M305462200 |
0.731 |
|
| 2003 |
Rotundo RL. Expression and localization of acetylcholinesterase at the neuromuscular junction. Journal of Neurocytology. 32: 743-66. PMID 15034265 DOI: 10.1023/B:NEUR.0000020621.58197.d4 |
0.579 |
|
| 2003 |
Rossi SG, Dickerson IM, Rotundo RL. Localization of the calcitonin gene-related peptide receptor complex at the vertebrate neuromuscular junction and its role in regulating acetylcholinesterase expression. The Journal of Biological Chemistry. 278: 24994-5000. PMID 12707285 DOI: 10.1074/jbc.M211379200 |
0.532 |
|
| 2002 |
Arikawa-Hirasawa E, Rossi SG, Rotundo RL, Yamada Y. Absence of acetylcholinesterase at the neuromuscular junctions of perlecan-null mice. Nature Neuroscience. 5: 119-23. PMID 11802174 DOI: 10.1038/nn801 |
0.601 |
|
| 2001 |
Drapeau P, Buss RR, Ali DW, Legendre P, Rotundo RL. Limits to the development of fast neuromuscular transmission in zebrafish. Journal of Neurophysiology. 86: 2951-6. PMID 11731551 DOI: 10.1152/Jn.2001.86.6.2951 |
0.524 |
|
| 2001 |
Jacobson C, Côté PD, Rossi SG, Rotundo RL, Carbonetto S. The dystroglycan complex is necessary for stabilization of acetylcholine receptor clusters at neuromuscular junctions and formation of the synaptic basement membrane. The Journal of Cell Biology. 152: 435-50. PMID 11157973 DOI: 10.1083/Jcb.152.3.435 |
0.722 |
|
| 2000 |
Adams ME, Kramarcy N, Krall SP, Rossi SG, Rotundo RL, Sealock R, Froehner SC. Absence of alpha-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin. The Journal of Cell Biology. 150: 1385-98. PMID 10995443 DOI: 10.1083/jcb.150.6.1385 |
0.382 |
|
| 2000 |
Rossi SG, Vazquez AE, Rotundo RL. Local control of acetylcholinesterase gene expression in multinucleated skeletal muscle fibers: individual nuclei respond to signals from the overlying plasma membrane. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 20: 919-28. PMID 10648696 DOI: 10.1523/Jneurosci.20-03-00919.2000 |
0.493 |
|
| 1999 |
Peng HB, Xie H, Rossi SG, Rotundo RL. Acetylcholinesterase clustering at the neuromuscular junction involves perlecan and dystroglycan. The Journal of Cell Biology. 145: 911-21. PMID 10330416 DOI: 10.1083/jcb.145.4.911 |
0.624 |
|
| 1998 |
Rotundo RL, Rossi SG, Peng HB. Targeting acetylcholinesterase molecules to the neuromuscular synapse. Journal of Physiology, Paris. 92: 195-8. PMID 9789807 DOI: 10.1016/S0928-4257(98)80009-0 |
0.525 |
|
| 1998 |
Lee RK, Jasmin BJ, Rotundo RL. Chapter 10 Development of the neuromuscular junction Principles of Medical Biology. 11: 187-207. DOI: 10.1016/S1569-2582(98)80025-1 |
0.529 |
|
| 1998 |
Rossi S, Katz S, Rotundo R. Control of acetylcholinesterase gene expression in tissue-cultured skeletal muscle: Opposite regulation by protein kinases A and C Journal of Physiology-Paris. 92: 486-487. DOI: 10.1016/S0928-4257(99)80102-8 |
0.382 |
|
| 1997 |
Rotundo RL, Rossi SG, Anglister L. Transplantation of quail collagen-tailed acetylcholinesterase molecules onto the frog neuromuscular synapse. The Journal of Cell Biology. 136: 367-74. PMID 9015307 DOI: 10.1083/jcb.136.2.367 |
0.508 |
|
| 1996 |
Rossi SG, Rotundo RL. Transient interactions between collagen-tailed acetylcholinesterase and sulfated proteoglycans prior to immobilization on the extracellular matrix. The Journal of Biological Chemistry. 271: 1979-87. PMID 8567647 DOI: 10.1074/jbc.271.4.1979 |
0.42 |
|
| 1993 |
Jasmin BJ, Lee RK, Rotundo RL. Compartmentalization of acetylcholinesterase mRNA and enzyme at the vertebrate neuromuscular junction. Neuron. 11: 467-77. PMID 8398140 DOI: 10.1016/0896-6273(93)90151-G |
0.498 |
|
| 1993 |
Rossi SG, Rotundo RL. Localization of "non-extractable" acetylcholinesterase to the vertebrate neuromuscular junction. The Journal of Biological Chemistry. 268: 19152-9. PMID 8360197 |
0.461 |
|
| 1992 |
Rossi SG, Rotundo RL. Cell surface acetylcholinesterase molecules on multinucleated myotubes are clustered over the nucleus of origin. The Journal of Cell Biology. 119: 1657-67. PMID 1469054 DOI: 10.1083/Jcb.119.6.1657 |
0.494 |
|
| 1990 |
Rotundo RL. Nucleus-specific translation and assembly of acetylcholinesterase in multinucleated muscle cells. The Journal of Cell Biology. 110: 715-9. PMID 2307705 DOI: 10.1083/Jcb.110.3.715 |
0.558 |
|
| 1989 |
Fernandez-Valle C, Rotundo RL. Regulation of acetylcholinesterase synthesis and assembly by muscle activity. Effects of tetrodotoxin. The Journal of Biological Chemistry. 264: 14043-9. PMID 2760056 |
0.783 |
|
| 1989 |
Rotundo RL, Thomas K, Porter-Jordan K, Benson RJ, Fernandez-Valle C, Fine RE. Intracellular transport, sorting, and turnover of acetylcholinesterase. Evidence for an endoglycosidase H-sensitive form in Golgi apparatus, sarcoplasmic reticulum, and clathrin-coated vesicles and its rapid degradation by a non-lysosomal mechanism. The Journal of Biological Chemistry. 264: 3146-52. PMID 2563379 |
0.731 |
|
| 1989 |
Thomas K, Navarro J, Benson RJ, Campbell KP, Rotundo RL, Fine RE. Newly synthesized calsequestrin, destined for the sarcoplasmic reticulum, is contained in early/intermediate Golgi-derived clathrin-coated vesicles. The Journal of Biological Chemistry. 264: 3140-5. PMID 2563378 |
0.373 |
|
| 1988 |
Rotundo RL. Biogenesis of acetylcholinesterase molecular forms in muscle. Evidence for a rapidly turning over, catalytically inactive precursor pool. The Journal of Biological Chemistry. 263: 19398-406. PMID 3198632 |
0.487 |
|
| 1988 |
Rotundo RL, Gomez AM, Fernandez-Valle C, Randall WR. Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene. Proceedings of the National Academy of Sciences of the United States of America. 85: 7805-9. PMID 3174665 DOI: 10.1073/Pnas.85.20.7805 |
0.766 |
|
| 1987 |
Rotundo RL, Carbonetto ST. Neurons segregate clusters of membrane-bound acetylcholinesterase along their neurites. Proceedings of the National Academy of Sciences of the United States of America. 84: 2063-7. PMID 3470777 DOI: 10.1073/Pnas.84.7.2063 |
0.636 |
|
| 1984 |
Rotundo RL. Asymmetric acetylcholinesterase is assembled in the Golgi apparatus. Proceedings of the National Academy of Sciences of the United States of America. 81: 479-83. PMID 6582503 DOI: 10.1073/Pnas.81.2.479 |
0.545 |
|
| 1984 |
Rotundo RL. Purification and properties of the membrane-bound form of acetylcholinesterase from chicken brain. Evidence for two distinct polypeptide chains. The Journal of Biological Chemistry. 259: 13186-94. PMID 6208193 |
0.342 |
|
| 1982 |
Rotundo RL, Fambrough DM. Synthesis, transport, and fate of acetylcholinesterase and acetylcholine receptors in cultured muscle. Progress in Clinical and Biological Research. 91: 259-86. PMID 7146002 |
0.606 |
|
| 1980 |
Rotundo RL, Fambrough DM. Secretion of acetylcholinesterase: relation to acetylcholine receptor metabolism. Cell. 22: 595-602. PMID 7448874 |
0.627 |
|
| 1980 |
Rotundo RL, Fambrough DM. Synthesis, transport and fate of acetylcholinesterase in cultured chick embryos muscle cells. Cell. 22: 583-94. PMID 7448873 |
0.648 |
|
| 1979 |
Rotundo RL, Fambrough DM. Molecular forms of chicken embryo acetylcholinesterase in vitro and in vivo. Isolation and characterization. The Journal of Biological Chemistry. 254: 4790-9. PMID 571440 |
0.629 |
|
| 1976 |
Pfeifer WD, Rotundo R, Myers M, Denenberg VH. Stimulation in infancy: unique effects of handling. Physiology & Behavior. 17: 781-4. PMID 1026986 DOI: 10.1016/0031-9384(76)90040-8 |
0.369 |
|
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