Year |
Citation |
Score |
2024 |
Adams MC, Schiltz CJ, Sun J, Hosford CJ, Johnson VM, Pan H, Borbat PP, Freed JH, Thomason LC, Court C, Court DL, Chappie JS. The crystal structure of bacteriophage λ RexA provides novel insights into the DNA binding properties of Rex-like phage exclusion proteins. Nucleic Acids Research. PMID 38554102 DOI: 10.1093/nar/gkae212 |
0.78 |
|
2023 |
Dot EW, Thomason LC, Chappie JS. Everything OLD is new again: How structural, functional, and bioinformatic advances have redefined a neglected nuclease family. Molecular Microbiology. PMID 37254295 DOI: 10.1111/mmi.15074 |
0.731 |
|
2022 |
Schiltz CJ, Wilson JR, Hosford CJ, Adams MC, Preising SE, DeBlasio SL, MacLeod HJ, Van Eck J, Heck ML, Chappie JS. Polerovirus N-terminal readthrough domain structures reveal molecular strategies for mitigating virus transmission by aphids. Nature Communications. 13: 6368. PMID 36289207 DOI: 10.1038/s41467-022-33979-2 |
0.768 |
|
2021 |
Adams MC, Schiltz CJ, Heck ML, Chappie JS. Crystal structure of the potato leafroll virus coat protein and implications for viral assembly. Journal of Structural Biology. 214: 107811. PMID 34813955 DOI: 10.1016/j.jsb.2021.107811 |
0.778 |
|
2021 |
Chowdhury R, Pavinski Bitar PD, Adams MC, Chappie JS, Altier C. AraC-type regulators HilC and RtsA are directly controlled by an intestinal fatty acid to regulate Salmonella invasion Molecular Microbiology. PMID 34687258 DOI: 10.1111/mmi.14835 |
0.736 |
|
2021 |
Thomason LC, Schiltz CJ, Court C, Hosford CJ, Adams MC, Chappie JS, Court DL. Bacteriophage λ RexA and RexB Functions Assist the Transition from Lysogeny to Lytic Growth. Molecular Microbiology. PMID 34379857 DOI: 10.1111/mmi.14792 |
0.717 |
|
2020 |
Niu Y, Suzuki H, Hosford CJ, Walz T, Chappie JS. Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes. Nature Communications. 11: 5907. PMID 33219217 DOI: 10.1038/s41467-020-19735-4 |
0.808 |
|
2020 |
Bosire EM, Eade CR, Schiltz CJ, Reid AJ, Troutman A, Chappie JS, Altier C. Diffusible signal factors act through AraC-type transcriptional regulators as chemical cues to repress virulence of enteric pathogens Infection and Immunity. PMID 32690633 DOI: 10.1128/Iai.00226-20 |
0.757 |
|
2020 |
Hosford CJ, Adams MC, Niu Y, Chappie JS. The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins Journal of Structural Biology. PMID 32652237 DOI: 10.1016/J.Jsb.2020.107572 |
0.816 |
|
2020 |
Gray S, Santiago ER, Chappie JS, Cohen, PE. Cyclin N-Terminal Domain-Containing-1 Coordinates Meiotic Crossover Formation With Cell-Cycle Progression in a Cyclin-Independent Manner Cell Reports. 32: 107858. PMID 32640224 DOI: 10.1016/J.Celrep.2020.107858 |
0.512 |
|
2020 |
Jaimes JA, André NM, Chappie JS, Millet JK, Whittaker GR. Phylogenetic Analysis and Structural Modeling of SARS-CoV-2 Spike Protein Reveals an Evolutionary Distinct and Proteolytically Sensitive Activation Loop. Journal of Molecular Biology. PMID 32320687 DOI: 10.1016/J.Jmb.2020.04.009 |
0.479 |
|
2020 |
Schiltz CJ, Adams MC, Chappie JS. The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases. Nucleic Acids Research. 48: 2762-2776. PMID 32009148 DOI: 10.2210/Pdb6P74/Pdb |
0.805 |
|
2020 |
Schiltz CJ, Adams MC, Chappie JS. The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases. Nucleic Acids Research. PMID 32009148 DOI: 10.1093/nar/gkaa059 |
0.798 |
|
2020 |
Tornabene BA, Varlakhanova NV, Hosford CJ, Chappie JS, Ford MGJ. Structural and Functional Characterization of the Dominant Negative P-Loop Lysine Mutation in the Dynamin Superfamily Protein Vps1. Protein Science : a Publication of the Protein Society. PMID 31981262 DOI: 10.1002/Pro.3830 |
0.771 |
|
2020 |
Hosford CJ, Bui AQ, Chappie JS. The structure of the Thermococcus gammatolerans McrB N-terminal domain reveals a new mode of substrate recognition and specificity among McrB homologs. Journal of Biological Chemistry. 295: 743-756. PMID 31822563 DOI: 10.1074/jbc.RA119.010188 |
0.523 |
|
2019 |
Hosford CJ, Bui AQ, Chappie JS. The structure of the Thermococcus gammatolerans McrB N-terminal domain reveals a new mode of substrate recognition and specificity among McrB homologs. The Journal of Biological Chemistry. PMID 31822563 DOI: 10.1074/Jbc.Ra119.010188 |
0.814 |
|
2019 |
Partlow EA, Baker RW, Beacham GM, Chappie JS, Leschziner AE, Hollopeter G. A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex. Elife. 8. PMID 31464684 DOI: 10.7554/Elife.50003 |
0.496 |
|
2019 |
Schiltz CJ, Lee A, Partlow EA, Hosford CJ, Chappie JS.. tructural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage. Nucleic Acids Res.. 47: 9448-9463. PMID 31400118 DOI: 10.1093/nar/gkz703 |
0.548 |
|
2019 |
Schiltz CJ, Lee A, Partlow EA, Hosford CJ, Chappie JS. Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage. Nucleic Acids Research. 47: 9448-9463. PMID 31400118 DOI: 10.1093/nar/gkz703 |
0.552 |
|
2019 |
Schiltz CJ, Lee A, Partlow EA, Hosford CJ, Chappie JS. Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage. Nucleic Acids Research. PMID 31400118 DOI: 10.1093/Nar/Gkz703 |
0.822 |
|
2019 |
Ford MGJ, Chappie JS. The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family. Traffic. 20: 717-740. PMID 31298797 DOI: 10.1111/Tra.12676 |
0.774 |
|
2019 |
Murphy SG, Alvarez L, Adams MC, Liu S, Chappie JS, Cava F, Dörr T. Endopeptidase Regulation as a Novel Function of the Zur-Dependent Zinc Starvation Response. Mbio. 10. PMID 30782657 DOI: 10.1128/Mbio.02620-18 |
0.642 |
|
2018 |
Varlakhanova NV, Alvarez FJD, Brady TM, Tornabene BA, Hosford CJ, Chappie JS, Zhang P, Ford MGJ. Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture. The Journal of Cell Biology. PMID 30087125 DOI: 10.1083/Jcb.201712021 |
0.802 |
|
2018 |
Hosford CJ, Chappie JS. The crystal structure of the LlaJI.R1 N-terminal domain provides a model for site-specific DNA binding. The Journal of Biological Chemistry. 293: 11758-11771. PMID 29895618 DOI: 10.1074/Jbc.Ra118.001888 |
0.791 |
|
2015 |
Hinshaw JE, Sundborger AC, Fang S, Heymann JA, Ray P, Chappie JS. Dynamin at the Brink of Fission Biophysical Journal. 108: 489a. DOI: 10.1016/J.Bpj.2014.11.2673 |
0.525 |
|
2014 |
Sundborger AC, Fang S, Heymann JA, Ray P, Chappie JS, Hinshaw JE. A dynamin mutant defines a superconstricted prefission state. Cell Reports. 8: 734-42. PMID 25088425 DOI: 10.1016/J.Celrep.2014.06.054 |
0.455 |
|
2013 |
Chappie JS, Dyda F. Building a fission machine--structural insights into dynamin assembly and activation. Journal of Cell Science. 126: 2773-84. PMID 23781021 DOI: 10.1242/Jcs.108845 |
0.473 |
|
2013 |
Hinshaw JE, Sundborger A, Heymann JA, Fang S, Chappie JS. High-Resolution 3D Reconstruction of a Dynamin Mutant, K44A, in its Super-Constricted State Biophysical Journal. 104: 618a. DOI: 10.1016/J.Bpj.2012.11.3420 |
0.487 |
|
2012 |
Maggin JE, James JA, Chappie JS, Dyda F, Hickman AB. The amino acid linker between the endonuclease and helicase domains of adeno-associated virus type 5 Rep plays a critical role in DNA-dependent oligomerization. Journal of Virology. 86: 3337-46. PMID 22205752 DOI: 10.1128/Jvi.06775-11 |
0.572 |
|
2012 |
Hinshaw JE, Chappie JS, Mears JA, Fang S, Leonard M, Schmid SL, Milligan RA, Dyda F. Structural Analysis of Dynamin Reveals Power Stroke Biophysical Journal. 102: 321a. DOI: 10.1016/J.Bpj.2011.11.1764 |
0.731 |
|
2011 |
Chappie JS, Mears JA, Fang S, Leonard M, Schmid SL, Milligan RA, Hinshaw JE, Dyda F. A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke. Cell. 147: 209-22. PMID 21962517 DOI: 10.1016/J.Cell.2011.09.003 |
0.763 |
|
2011 |
Chappie JS, Mears JA, Fang S, Leonard M, Schmid SL, Milligan RA, Hinshaw JE, Dyda F. An Improved Model for Dynamin Assembly Revealed by Cryo-EM Biophysical Journal. 100: 324a. DOI: 10.1016/J.Bpj.2010.12.1969 |
0.758 |
|
2010 |
Wilson-Kubalek EM, Chappie JS, Arthur CP. Helical crystallization of soluble and membrane binding proteins. Methods in Enzymology. 481: 45-62. PMID 20887852 DOI: 10.1016/S0076-6879(10)81002-X |
0.722 |
|
2010 |
Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature. 465: 435-40. PMID 20428113 DOI: 10.1038/Nature09032 |
0.669 |
|
2009 |
Chappie JS, Acharya S, Liu YW, Leonard M, Pucadyil TJ, Schmid SL. An intramolecular signaling element that modulates dynamin function in vitro and in vivo. Molecular Biology of the Cell. 20: 3561-71. PMID 19515832 DOI: 10.1091/Mbc.E09-04-0318 |
0.66 |
|
2008 |
Littlefield KP, Ward AB, Chappie JS, Reedy MK, Bernstein SI, Milligan RA, Reedy MC. Similarities and differences between frozen-hydrated, rigor acto-S1 complexes of insect flight and chicken skeletal muscles. Journal of Molecular Biology. 381: 519-28. PMID 18588896 DOI: 10.1016/J.Jmb.2008.06.029 |
0.665 |
|
2007 |
Ramachandran R, Surka M, Chappie JS, Fowler DM, Foss TR, Song BD, Schmid SL. The dynamin middle domain is critical for tetramerization and higher-order self-assembly. The Embo Journal. 26: 559-66. PMID 17170701 DOI: 10.1038/Sj.Emboj.7601491 |
0.625 |
|
2006 |
Cheeseman IM, Chappie JS, Wilson-Kubalek EM, Desai A. The conserved KMN network constitutes the core microtubule-binding site of the kinetochore. Cell. 127: 983-97. PMID 17129783 DOI: 10.1016/J.Cell.2006.09.039 |
0.705 |
|
2005 |
Chappie JS, Cànaves JM, Han GW, Rife CL, Xu Q, Stevens RC. The structure of a eukaryotic nicotinic acid phosphoribosyltransferase reveals structural heterogeneity among type II PRTases. Structure (London, England : 1993). 13: 1385-96. PMID 16154095 DOI: 10.1016/J.Str.2005.05.016 |
0.523 |
|
2003 |
Nimigean CM, Chappie JS, Miller C. Electrostatic tuning of ion conductance in potassium channels. Biochemistry. 42: 9263-8. PMID 12899612 DOI: 10.1021/Bi0348720 |
0.442 |
|
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