Year |
Citation |
Score |
2022 |
Leary KA, Hawkins WD, Andhare D, Popelka H, Klionsky DJ, Ragusa MJ. Atg23 is a vesicle-tethering protein. Autophagy. 1-2. PMID 35867625 DOI: 10.1080/15548627.2022.2105107 |
0.385 |
|
2022 |
Leary KA, Ragusa MJ. Characterization of Protein-Membrane Interactions in Yeast Autophagy. Cells. 11. PMID 35741004 DOI: 10.3390/cells11121876 |
0.328 |
|
2022 |
Hawkins WD, Leary KA, Andhare D, Popelka H, Klionsky DJ, Ragusa MJ. Dimerization-dependent membrane tethering by Atg23 is essential for yeast autophagy. Cell Reports. 39: 110702. PMID 35443167 DOI: 10.1016/j.celrep.2022.110702 |
0.381 |
|
2022 |
Reinhart EF, Katzenell S, Andhare D, Bauer KM, Ragusa MJ. A Comparative Analysis of the Membrane Binding and Remodeling Properties of Two Related Sorting Nexin Complexes Involved in Autophagy. Biochemistry. PMID 35421303 DOI: 10.1021/acs.biochem.2c00007 |
0.429 |
|
2021 |
Klionsky DJ, Abdel-Aziz AK, Abdelfatah S, Abdellatif M, Abdoli A, Abel S, Abeliovich H, Abildgaard MH, Abudu YP, Acevedo-Arozena A, Adamopoulos IE, Adeli K, Adolph TE, Adornetto A, Aflaki E, ... ... Ragusa MJ, et al. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition). Autophagy. 1-382. PMID 33634751 DOI: 10.1080/15548627.2020.1797280 |
0.497 |
|
2021 |
Popelka H, Reinhart EF, Padma Metur S, Leary KA, Ragusa MJ, Klionsky DJ. Membrane binding and homodimerization of Atg16 via two distinct protein regions is essential for autophagy in yeast. Journal of Molecular Biology. 166809. PMID 33484718 DOI: 10.1016/j.jmb.2021.166809 |
0.446 |
|
2020 |
Reinhart EF, Litt NA, Katzenell S, Pellegrini M, Yamamoto A, Ragusa MJ. A highly conserved glutamic acid in ALFY inhibits membrane binding to aid in aggregate clearance. Traffic (Copenhagen, Denmark). PMID 33225481 DOI: 10.1111/tra.12771 |
0.394 |
|
2020 |
Margolis HK, Katzenell S, Leary KA, Ragusa MJ. The Third Coiled Coil Domain of Atg11 Is Required for Shaping Mitophagy Initiation Sites. Journal of Molecular Biology. PMID 32896530 DOI: 10.1016/J.Jmb.2020.08.025 |
0.499 |
|
2019 |
Barczewski AH, Ragusa MJ, Mierke DF, Pellegrini M. Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO. Journal of Visualized Experiments : Jove. PMID 31929506 DOI: 10.3791/60339 |
0.489 |
|
2019 |
Carpenter JM, Zhong F, Ragusa MJ, Louro RO, Hogan DA, Pletneva EV. Structure and redox properties of the diheme electron carrier cytochrome c from Pseudomonas aeruginosa. Journal of Inorganic Biochemistry. 203: 110889. PMID 31707335 DOI: 10.1016/J.Jinorgbio.2019.110889 |
0.346 |
|
2019 |
Bauer KM, Dicovitsky R, Pellegrini M, Zhaxybayeva O, Ragusa MJ. The structure of a highly conserved picocyanobacterial protein reveals a Tudor domain with an RNA binding function. The Journal of Biological Chemistry. PMID 31391250 DOI: 10.1074/Jbc.Ra119.007938 |
0.384 |
|
2019 |
Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. Autophagy. 1-14. PMID 31352862 DOI: 10.1080/15548627.2019.1648117 |
0.536 |
|
2019 |
Barczewski AH, Ragusa MJ, Mierke DF, Pellegrini M. The IKK-binding domain of NEMO is an irregular coiled coil with a dynamic binding interface. Scientific Reports. 9: 2950. PMID 30814588 DOI: 10.1038/S41598-019-39588-2 |
0.497 |
|
2019 |
Bauer K, Pelligrini M, Ragusa M. Solution structure of the Tudor domain of PSHCP Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb6Nnb/Pdb |
0.416 |
|
2018 |
Xia X, Katzenell S, Reinhart EF, Bauer KM, Pellegrini M, Ragusa MJ. A Pseudo-Receiver Domain in Atg32 is Required for Mitophagy. Autophagy. PMID 29909755 DOI: 10.1080/15548627.2018.1472838 |
0.537 |
|
2018 |
Popelka H, Klionsky DJ, Ragusa MJ. An atypical BAR domain protein in autophagy. Autophagy. 1-2. PMID 29799763 DOI: 10.1080/15548627.2018.1445915 |
0.561 |
|
2017 |
Popelka H, Damasio A, Hinshaw JE, Klionsky DJ, Ragusa MJ. Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction. Proceedings of the National Academy of Sciences of the United States of America. PMID 29114050 DOI: 10.1073/Pnas.1708367114 |
0.593 |
|
2017 |
Xia X, Pellegrini M, Ragusa MJ. Backbone and side chain resonance assignments for a structured domain within Atg32. Biomolecular Nmr Assignments. PMID 28766175 DOI: 10.1007/S12104-017-9750-Y |
0.473 |
|
2017 |
Xia X, Pellegrini M, Ragusa M. 1H, 13C, and 15N backbone and side chain resonance assignments for a structured domain in atg32 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27081 |
0.367 |
|
2016 |
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, ... ... Ragusa MJ, et al. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy. 12: 1-222. PMID 26799652 DOI: 10.1080/15548627.2015.1100356 |
0.548 |
|
2015 |
Köfinger J, Ragusa MJ, Lee IH, Hummer G, Hurley JH. Solution structure of the Atg1 complex: implications for the architecture of the phagophore assembly site. Structure (London, England : 1993). 23: 809-18. PMID 25817386 DOI: 10.1016/J.Str.2015.02.012 |
0.743 |
|
2015 |
Koefinger J, Ragusa MJ, Hummer G, Hurley JH. Autophagy: Solution Structure of the Atg17-Atg29-Atg31-Atg1-Atg13 Complex Biophysical Journal. 108: 343a. DOI: 10.1016/J.Bpj.2014.11.1882 |
0.53 |
|
2014 |
Stjepanovic G, Davies CW, Stanley RE, Ragusa MJ, Kim do J, Hurley JH. Assembly and dynamics of the autophagy-initiating Atg1 complex. Proceedings of the National Academy of Sciences of the United States of America. 111: 12793-8. PMID 25139988 DOI: 10.1073/Pnas.1407214111 |
0.755 |
|
2014 |
Stanley RE, Ragusa MJ, Hurley JH. The beginning of the end: how scaffolds nucleate autophagosome biogenesis. Trends in Cell Biology. 24: 73-81. PMID 23999079 DOI: 10.1016/J.Tcb.2013.07.008 |
0.728 |
|
2013 |
Jao CC, Ragusa MJ, Stanley RE, Hurley JH. What the N-terminal domain of Atg13 looks like and what it does: a HORMA fold required for PtdIns 3-kinase recruitment. Autophagy. 9: 1112-4. PMID 23670046 DOI: 10.4161/Auto.24896 |
0.747 |
|
2013 |
Jao CC, Ragusa MJ, Stanley RE, Hurley JH. A HORMA domain in Atg13 mediates PI 3-kinase recruitment in autophagy. Proceedings of the National Academy of Sciences of the United States of America. 110: 5486-91. PMID 23509291 DOI: 10.1073/Pnas.1220306110 |
0.748 |
|
2012 |
Ragusa MJ, Stanley RE, Hurley JH. Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis. Cell. 151: 1501-12. PMID 23219485 DOI: 10.1016/J.Cell.2012.11.028 |
0.747 |
|
2012 |
Baskaran S, Ragusa MJ, Hurley JH. How Atg18 and the WIPIs sense phosphatidylinositol 3-phosphate. Autophagy. 8: 1851-2. PMID 22996041 DOI: 10.4161/Auto.22077 |
0.685 |
|
2012 |
Baskaran S, Ragusa MJ, Boura E, Hurley JH. Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs in autophagy. Molecular Cell. 47: 339-48. PMID 22704557 DOI: 10.1016/J.Molcel.2012.05.027 |
0.73 |
|
2011 |
Dancheck B, Ragusa MJ, Allaire M, Nairn AC, Page R, Peti W. Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex. Biochemistry. 50: 1238-46. PMID 21218781 DOI: 10.1021/Bi101774G |
0.483 |
|
2011 |
Ragusa MJ, Allaire M, Nairn AC, Page R, Peti W. Flexibility in the PP1:spinophilin holoenzyme. Febs Letters. 585: 36-40. PMID 21094159 DOI: 10.1016/J.Febslet.2010.11.022 |
0.38 |
|
2010 |
Marsh JA, Dancheck B, Ragusa MJ, Allaire M, Forman-Kay JD, Peti W. Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. Structure (London, England : 1993). 18: 1094-103. PMID 20826336 DOI: 10.1016/J.Str.2010.05.015 |
0.423 |
|
2010 |
Bollen M, Peti W, Ragusa MJ, Beullens M. The extended PP1 toolkit: designed to create specificity. Trends in Biochemical Sciences. 35: 450-8. PMID 20399103 DOI: 10.1016/J.Tibs.2010.03.002 |
0.393 |
|
2010 |
Ragusa MJ, Dancheck B, Critton DA, Nairn AC, Page R, Peti W. Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nature Structural & Molecular Biology. 17: 459-64. PMID 20305656 DOI: 10.1038/Nsmb.1786 |
0.4 |
|
2009 |
Sterne-Marr R, Leahey PA, Bresee JE, Dickson HM, Ho W, Ragusa MJ, Donnelly RM, Amie SM, Krywy JA, Brookins-Danz ED, Orakwue SC, Carr MJ, Yoshino-Koh K, Li Q, Tesmer JJ. GRK2 activation by receptors: role of the kinase large lobe and carboxyl-terminal tail. Biochemistry. 48: 4285-93. PMID 19338266 DOI: 10.1021/Bi900151G |
0.435 |
|
2007 |
Ju T, Ragusa MJ, Hudak J, Nairn AC, Peti W. Structural characterization of the neurabin sterile alpha motif domain. Proteins. 69: 192-8. PMID 17600833 DOI: 10.1002/Prot.21513 |
0.388 |
|
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