Year |
Citation |
Score |
2024 |
Mackness BC, Morgan BR, Deveau LM, Kathuria SV, Zitzewitz JA, Massi F. A hydrophobic core stabilizes the residual structure in the RRM2 intermediate state of the ALS-linked protein TDP-43. Biorxiv : the Preprint Server For Biology. PMID 38915526 DOI: 10.1101/2024.06.12.598648 |
0.302 |
|
2021 |
Morgan BR, Massi F. The Role of Substrate Mediated Allostery in the Catalytic Competency of the Bacterial Oligosaccharyltransferase PglB. Frontiers in Molecular Biosciences. 8: 740904. PMID 34604309 DOI: 10.3389/fmolb.2021.740904 |
0.317 |
|
2020 |
Tavella D, Ertekin A, Schaal H, Ryder SP, Massi F. A Disorder-to-Order Transition Mediates RNA Binding of the Caenorhabditis elegans Protein MEX-5. Biophysical Journal. PMID 32294479 DOI: 10.1016/J.Bpj.2020.02.032 |
0.36 |
|
2019 |
Basak S, Nobrega RP, Tavella D, Deveau LM, Koga N, Tatsumi-Koga R, Baker D, Massi F, Matthews CR. Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed βα protein. Proceedings of the National Academy of Sciences of the United States of America. PMID 30877249 DOI: 10.1073/Pnas.1818744116 |
0.313 |
|
2018 |
Tavella D, Zitzewitz JA, Massi F. Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis. Biophysical Journal. PMID 30309612 DOI: 10.1016/J.Bpj.2018.09.011 |
0.38 |
|
2018 |
Massi F, Peng JW. Characterizing Protein Dynamics with NMR R 1ρ Relaxation Experiments. Methods in Molecular Biology (Clifton, N.J.). 1688: 205-221. PMID 29151211 DOI: 10.1007/978-1-4939-7386-6_10 |
0.302 |
|
2017 |
Morgan BR, Zitzewitz JA, Massi F. Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43. Biophysical Journal. 113: 540-549. PMID 28793209 DOI: 10.1016/J.Bpj.2017.06.049 |
0.369 |
|
2016 |
Tavella D, Deveau LM, Whitfield TW, Massi F. Structural basis of the disorder in the tandem zinc finger domain of the RNA-binding protein Tristetraprolin. Journal of Chemical Theory and Computation. PMID 27487322 DOI: 10.1021/Acs.Jctc.6B00150 |
0.609 |
|
2016 |
Deveau LM, Massi F. RNA-Binding Domain Disorder Modulates the RNA Destabilizing Activity in the TTP Family of Proteins Biophysical Journal. 110: 557a. DOI: 10.1016/J.Bpj.2015.11.2981 |
0.365 |
|
2016 |
Morgan BR, Massi F. Origins of Catalytic Specificity in Bacterial Oligosaccharyltransferase Biophysical Journal. 110: 548a. DOI: 10.1016/J.Bpj.2015.11.2932 |
0.337 |
|
2015 |
Deveau LM, Massi F. Three residues make an evolutionary switch for folding and RNA-destabilizing activity in the TTP family of proteins. Acs Chemical Biology. PMID 26551835 DOI: 10.1021/Acschembio.5B00639 |
0.376 |
|
2015 |
Morgan BR, Deveau LM, Massi F. Probing the structural and dynamical effects of the charged residues of the TZF domain of TIS11d. Biophysical Journal. 108: 1503-15. PMID 25809263 DOI: 10.1016/J.Bpj.2015.01.039 |
0.387 |
|
2014 |
Zearfoss NR, Deveau LM, Clingman CC, Schmidt E, Johnson ES, Massi F, Ryder SP. A conserved three-nucleotide core motif defines Musashi RNA binding specificity. The Journal of Biological Chemistry. 289: 35530-41. PMID 25368328 DOI: 10.1074/Jbc.M114.597112 |
0.338 |
|
2014 |
Laine JM, Amat M, Morgan BR, Royer WE, Massi F. Insight into the allosteric mechanism of Scapharca dimeric hemoglobin. Biochemistry. 53: 7199-210. PMID 25356908 DOI: 10.1021/Bi500591S |
0.345 |
|
2013 |
Gangadhara BN, Laine JM, Kathuria SV, Massi F, Matthews CR. Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein. Journal of Molecular Biology. 425: 1065-81. PMID 23333740 DOI: 10.1016/J.Jmb.2013.01.002 |
0.32 |
|
2011 |
Stewart MD, Morgan B, Massi F, Igumenova TI. Probing the determinants of diacylglycerol binding affinity in the C1B domain of protein kinase Cα. Journal of Molecular Biology. 408: 949-70. PMID 21419781 DOI: 10.1016/J.Jmb.2011.03.020 |
0.383 |
|
2010 |
Ryder SP, Massi F. Insights into the structural basis of RNA recognition by STAR domain proteins. Advances in Experimental Medicine and Biology. 693: 37-53. PMID 21189684 DOI: 10.1007/978-1-4419-7005-3_3 |
0.339 |
|
2010 |
Morgan BR, Massi F. A computational study of RNA binding and specificity in the tandem zinc finger domain of TIS11d. Protein Science : a Publication of the Protein Society. 19: 1222-34. PMID 20506496 DOI: 10.1002/Pro.401 |
0.391 |
|
2006 |
Massi F, Wang C, Palmer AG. Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase. Biochemistry. 45: 10787-94. PMID 16953564 DOI: 10.1021/Bi060764C |
0.366 |
|
2005 |
Massi F, Grey MJ, Palmer AG. Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments. Protein Science : a Publication of the Protein Society. 14: 735-42. PMID 15722448 DOI: 10.1110/Ps.041139505 |
0.349 |
|
2003 |
Massi F, Palmer AG. Temperature dependence of NMR order parameters and protein dynamics. Journal of the American Chemical Society. 125: 11158-9. PMID 16220912 DOI: 10.1021/Ja035605K |
0.331 |
|
2003 |
Massi F, Straub JE. Structural and dynamical analysis of the hydration of the Alzheimer's beta-amyloid peptide. Journal of Computational Chemistry. 24: 143-53. PMID 12497595 DOI: 10.1002/Jcc.10101 |
0.574 |
|
2002 |
Massi F, Klimov D, Thirumalai D, Straub JE. Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant. Protein Science : a Publication of the Protein Society. 11: 1639-47. PMID 12070316 DOI: 10.1110/Ps.3150102 |
0.573 |
|
2001 |
Massi F, Straub JE. Probing the origins of increased activity of the E22Q "Dutch" mutant Alzheimer's beta-amyloid peptide. Biophysical Journal. 81: 697-709. PMID 11463618 DOI: 10.1016/S0006-3495(01)75734-7 |
0.583 |
|
2001 |
Massi F, Peng JW, Lee JP, Straub JE. Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution. Biophysical Journal. 80: 31-44. PMID 11159381 DOI: 10.1016/S0006-3495(01)75993-0 |
0.584 |
|
2001 |
Massi F, Straub JE. Energy landscape theory for Alzheimer's amyloid beta-peptide fibril elongation. Proteins. 42: 217-29. PMID 11119646 DOI: 10.1002/1097-0134(20010201)42:2<217::Aid-Prot90>3.0.Co;2-N |
0.547 |
|
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