| Year |
Citation |
Score |
| 2023 |
Wydorski PM, Osipiuk J, Lanham BT, Tesar C, Endres M, Engle E, Jedrzejczak R, Mullapudi V, Michalska K, Fidelis K, Fushman D, Joachimiak A, Joachimiak LA. Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin. Nature Communications. 14: 2366. PMID 37185902 DOI: 10.1038/s41467-023-38031-5 |
0.31 |
|
| 2022 |
Gama Lima Costa R, Fushman D. Reweighting methods for elucidation of conformation ensembles of proteins. Current Opinion in Structural Biology. 77: 102470. PMID 36183447 DOI: 10.1016/j.sbi.2022.102470 |
0.347 |
|
| 2021 |
Osipiuk J, Wydorski PM, Lanham BT, Tesar C, Endres M, Engle E, Jedrzejczak R, Mullapudi V, Michalska K, Fidelis K, Fushman D, Joachimiak A, Joachimiak LA. Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin. Biorxiv : the Preprint Server For Biology. PMID 35547846 DOI: 10.1101/2021.09.15.460543 |
0.302 |
|
| 2021 |
Boughton AJ, Zhang D, Singh RK, Fushman D. Polyubiquitin and ubiquitin-like signals share common recognition sites on proteasomal subunit Rpn1. The Journal of Biological Chemistry. 100450. PMID 33617881 DOI: 10.1016/j.jbc.2021.100450 |
0.309 |
|
| 2020 |
Liao TJ, Jang H, Fushman D, Nussinov R. SOS1 interacts with Grb2 through regions that induce closed nSH3 conformations. The Journal of Chemical Physics. 153: 045106. PMID 32752665 DOI: 10.1063/5.0013926 |
0.441 |
|
| 2020 |
Magnussen HM, Ahmed SF, Sibbet GJ, Hristova VA, Nomura K, Hock AK, Archibald LJ, Jamieson AG, Fushman D, Vousden KH, Weissman AM, Huang DT. Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain. Nature Communications. 11: 2094. PMID 32350255 DOI: 10.1038/S41467-020-15783-Y |
0.341 |
|
| 2020 |
Liao TJ, Jang H, Nussinov R, Fushman D. High-affinity Interactions of the nSH3/cSH3 Domains of Grb2 with the C-terminal Proline-rich Domain of SOS1. Journal of the American Chemical Society. PMID 31970984 DOI: 10.1021/Jacs.9B10710 |
0.396 |
|
| 2019 |
Wu X, Liu S, Sagum C, Chen J, Singh R, Chaturvedi A, Horton JR, Kashyap TR, Fushman D, Cheng X, Bedford MT, Wang B. Crosstalk between Lys63- and Lys11-polyubiquitin signaling at DNA damage sites is driven by Cezanne. Genes & Development. PMID 31699778 DOI: 10.1101/Gad.332395.119 |
0.312 |
|
| 2019 |
Boughton AJ, Krueger S, Fushman D. Branching via K11 and K48 Bestows Ubiquitin Chains with a Unique Interdomain Interface and Enhanced Affinity for Proteasomal Subunit Rpn1. Structure (London, England : 1993). PMID 31677892 DOI: 10.1016/J.Str.2019.10.008 |
0.331 |
|
| 2019 |
Nawatha M, Rogers JM, Bonn SM, Livneh I, Lemma B, Mali SM, Vamisetti GB, Sun H, Bercovich B, Huang Y, Ciechanover A, Fushman D, Suga H, Brik A. De novo macrocyclic peptides that specifically modulate Lys48-linked ubiquitin chains. Nature Chemistry. PMID 31182821 DOI: 10.1038/S41557-019-0278-X |
0.382 |
|
| 2019 |
Narayan A, Gopi S, Fushman D, Naganathan AN. A binding cooperativity switch driven by synergistic structural swelling of an osmo-regulatory protein pair. Nature Communications. 10: 1995. PMID 31040281 DOI: 10.1038/S41467-019-10002-9 |
0.387 |
|
| 2019 |
Braxton CN, Quartner E, Pawloski W, Fushman D, Cropp TA. Ubiquitin chains bearing genetically encoded photo-crosslinkers enable efficient covalent capture of (poly)ubiquitin-binding domains. Biochemistry. PMID 30668904 DOI: 10.1021/Acs.Biochem.8B01089 |
0.438 |
|
| 2019 |
Liao T, Jang H, Nussinov R, Fushman D. Abstract 5145: A new discovering motif on SOS1 PR domain clues Grb2-SOS1 association Cancer Research. 79: 5145-5145. DOI: 10.1158/1538-7445.Sabcs18-5145 |
0.431 |
|
| 2019 |
Liao T, Jang H, Nussinov R, Fushman D. Structure Based Search for Multiple Binding Sites of SOS1 PR Domain Recognizes an Uncovered Motif Favoring GRB2-SOS1 Association Biophysical Journal. 116: 169a. DOI: 10.1016/J.Bpj.2018.11.937 |
0.39 |
|
| 2018 |
Gomes F, Lemma B, Abeykoon D, Chen D, Wang Y, Fushman D, Fenselau C. Top-down Analysis of Novel Synthetic Branched Proteins. Journal of Mass Spectrometry : Jms. PMID 30347468 DOI: 10.1002/Jms.4303 |
0.316 |
|
| 2018 |
Liao TJ, Jang H, Fushman D, Nussinov R. Allosteric KRas4B Can Modulate SOS1 Fast and Slow Ras Activation Cycles. Biophysical Journal. PMID 30097175 DOI: 10.1016/J.Bpj.2018.07.016 |
0.327 |
|
| 2018 |
Chen D, Gomes F, Abeykoon D, Lemma B, Wang Y, Fushman D, Fenselau C. Top-Down Analysis of Branched Proteins Using Mass Spectrometry. Analytical Chemistry. PMID 29513006 DOI: 10.1021/Acs.Analchem.7B05234 |
0.377 |
|
| 2018 |
Kazansky Y, Lai MY, Singh RK, Fushman D. Impact of different ionization states of phosphorylated Serine-65 on ubiquitin structure and interactions. Scientific Reports. 8: 2651. PMID 29422536 DOI: 10.1038/S41598-018-20860-W |
0.433 |
|
| 2018 |
Liao T, Jang H, Fushman D, Nussinov R. Abstract 683: SOS1 allosterically linked conformational changes modulate KRas4B activation Cancer Research. 78: 683-683. DOI: 10.1158/1538-7445.Am2018-683 |
0.305 |
|
| 2017 |
Nakasone MA, Lewis TA, Walker O, Thakur A, Mansour W, Castañeda CA, Goeckeler-Fried JL, Parlati F, Chou TF, Hayat O, Zhang D, Camara CM, Bonn SM, Nowicka UK, Krueger S, ... ... Fushman D, et al. Structural Basis for the Inhibitory Effects of Ubistatins in the Ubiquitin-Proteasome Pathway. Structure (London, England : 1993). PMID 29153505 DOI: 10.1016/J.Str.2017.10.007 |
0.398 |
|
| 2017 |
Ceccon A, Tugarinov V, Boughton AJ, Fushman D, Clore GM. Probing the Binding Modes of a Multidomain Protein to Lipid-based Nanoparticles by Relaxation-based NMR. The Journal of Physical Chemistry Letters. 2535-2540. PMID 28530812 DOI: 10.1021/Acs.Jpclett.7B01019 |
0.408 |
|
| 2017 |
Chojnacki M, Mansour W, Hameed DS, Singh RK, El Oualid F, Rosenzweig R, Nakasone MA, Yu Z, Glaser F, Kay LE, Fushman D, Ovaa H, Glickman MH. Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit. Cell Chemical Biology. PMID 28330605 DOI: 10.1016/J.Chembiol.2017.02.013 |
0.418 |
|
| 2017 |
Munari F, Bortot A, Zanzoni S, D'Onofrio M, Fushman D, Assfalg M. Identification of primary and secondary UBA footprints on the surface of ubiquitin in cell-mimicking crowded solution. Febs Letters. PMID 28267209 DOI: 10.1002/1873-3468.12615 |
0.368 |
|
| 2017 |
Fushman D. Exploring Polyubiquitin as a Flexible Multiple-Ligand Binding Platform. Structure (London, England : 1993). 25: 1-3. PMID 28052234 DOI: 10.1016/J.Str.2016.12.010 |
0.349 |
|
| 2017 |
Liao T, Jang H, Tsai C, Fushman D, Nussinov R. Abstract 1367: The dynamic mechanism of SARAH domain in RASSF5 activation by K-Ras4B Cancer Research. 77: 1367-1367. DOI: 10.1158/1538-7445.Am2017-1367 |
0.318 |
|
| 2016 |
Lee AE, Geis-Asteggiante L, Dixon EK, Miller M, Wang Y, Fushman D, Fenselau C. Preparing to read the ubiquitin code: top-down analysis of unanchored ubiquitin tetramers. Journal of Mass Spectrometry : Jms. 51: 629-637. PMID 28239975 DOI: 10.1002/Jms.3787 |
0.398 |
|
| 2016 |
Narayan A, Campos LA, Bhatia S, Fushman D, Naganathan AN. Graded Structural Polymorphism in a Bacterial Thermosensor Protein. Journal of the American Chemical Society. PMID 27991780 DOI: 10.1021/Jacs.6B10608 |
0.401 |
|
| 2016 |
Chojnacki M, Zhang D, Talarowska M, Gałecki P, Szemraj J, Fushman D, Nakasone MA. Characterizing polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB(+1). Febs Letters. PMID 27861798 DOI: 10.1002/1873-3468.12484 |
0.307 |
|
| 2016 |
Lee AE, Geis-Asteggiante L, Dixon EK, Kim Y, Kashyap TR, Wang Y, Fushman D, Fenselau C. Preparing to read the ubiquitin code: characterization of ubiquitin trimers by top-down mass spectrometry. Journal of Mass Spectrometry : Jms. 51: 315-21. PMID 27041663 DOI: 10.1002/Jms.3759 |
0.374 |
|
| 2016 |
Castañeda CA, Dixon EK, Walker O, Chaturvedi A, Nakasone MA, Curtis JE, Reed MR, Krueger S, Cropp TA, Fushman D. Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins. Structure (London, England : 1993). PMID 26876099 DOI: 10.1016/J.Str.2016.01.007 |
0.321 |
|
| 2015 |
Castañeda CA, Chaturvedi A, Camara CM, Curtis JE, Krueger S, Fushman D. Linkage-specific conformational ensembles of non-canonical polyubiquitin chains. Physical Chemistry Chemical Physics : Pccp. PMID 26422168 DOI: 10.1039/C5Cp04601G |
0.379 |
|
| 2015 |
Burke MC, Wang Y, Lee AE, Dixon EK, Castaneda CA, Fushman D, Fenselau C. Unexpected trypsin cleavage at ubiquitinated lysines. Analytical Chemistry. PMID 26182167 DOI: 10.1021/Acs.Analchem.5B01960 |
0.326 |
|
| 2015 |
Andrałojć W, Berlin K, Fushman D, Luchinat C, Parigi G, Ravera E, Sgheri L. Information content of long-range NMR data for the characterization of conformational heterogeneity. Journal of Biomolecular Nmr. 62: 353-71. PMID 26044033 DOI: 10.1007/S10858-015-9951-6 |
0.605 |
|
| 2015 |
Schumann FH, Varadan R, Tayakuniyil PP, Grossman JH, Camarero JA, Fushman D. Changing the topology of protein backbone: the effect of backbone cyclization on the structure and dynamics of a SH3 domain. Frontiers in Chemistry. 3: 26. PMID 25905098 DOI: 10.3389/Fchem.2015.00026 |
0.807 |
|
| 2015 |
Zanzoni S, Ceccon A, Assfalg M, Singh RK, Fushman D, D'Onofrio M. Polyhydroxylated [60]fullerene binds specifically to functional recognition sites on a monomeric and a dimeric ubiquitin. Nanoscale. 7: 7197-205. PMID 25811293 DOI: 10.1039/C5Nr00539F |
0.393 |
|
| 2015 |
Nowicka U, Zhang D, Walker O, Krutauz D, Castañeda CA, Chaturvedi A, Chen TY, Reis N, Glickman MH, Fushman D. DNA-damage-inducible 1 protein (Ddi1) contains an uncharacteristic ubiquitin-like domain that binds ubiquitin. Structure (London, England : 1993). 23: 542-57. PMID 25703377 DOI: 10.1016/J.Str.2015.01.010 |
0.459 |
|
| 2015 |
Mansour W, Nakasone MA, von Delbrück M, Yu Z, Krutauz D, Reis N, Kleifeld O, Sommer T, Fushman D, Glickman MH. Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6. The Journal of Biological Chemistry. 290: 4688-704. PMID 25389291 DOI: 10.1074/Jbc.M114.568295 |
0.396 |
|
| 2015 |
Zhao H, Fushman D, Papoian GA. The Association Landscape of Ubiquitin Dimerization Biophysical Journal. 108: 519a. DOI: 10.1016/J.Bpj.2014.11.2848 |
0.454 |
|
| 2014 |
Lee AE, Castañeda CA, Wang Y, Fushman D, Fenselau C. Preparing to read the ubiquitin code: a middle-out strategy for characterization of all lysine-linked diubiquitins. Journal of Mass Spectrometry : Jms. 49: 1272-8. PMID 25476945 DOI: 10.1002/Jms.3458 |
0.324 |
|
| 2014 |
Krutauz D, Reis N, Nakasone MA, Siman P, Zhang D, Kirkpatrick DS, Gygi SP, Brik A, Fushman D, Glickman MH. Extended ubiquitin species are protein-based DUB inhibitors. Nature Chemical Biology. 10: 664-70. PMID 24997605 DOI: 10.1038/Nchembio.1574 |
0.337 |
|
| 2014 |
Singh RK, Sundar A, Fushman D. Nonenzymatic rubylation and ubiquitination of proteins for structural and functional studies. Angewandte Chemie (International Ed. in English). 53: 6120-5. PMID 24764216 DOI: 10.1002/Anie.201402642 |
0.386 |
|
| 2014 |
Berlin K, Gumerov NA, Fushman D, Duraiswami R. Hierarchical O(N) computation of small-angle scattering profiles and their associated derivatives. Journal of Applied Crystallography. 47: 755-761. PMID 24701198 DOI: 10.1107/S1600576714004671 |
0.538 |
|
| 2014 |
Lee SY, Pullen L, Virgil DJ, Castañeda CA, Abeykoon D, Bolon DNA, Fushman D. Alanine scan of core positions in ubiquitin reveals links between dynamics, stability, and function Journal of Molecular Biology. 426: 1377-1389. PMID 24361330 DOI: 10.1016/J.Jmb.2013.10.042 |
0.374 |
|
| 2013 |
Berlin K, Longhini A, Dayie TK, Fushman D. Deriving quantitative dynamics information for proteins and RNAs using ROTDIF with a graphical user interface. Journal of Biomolecular Nmr. 57: 333-52. PMID 24170368 DOI: 10.1007/S10858-013-9791-1 |
0.621 |
|
| 2013 |
Berlin K, Castañeda CA, Schneidman-Duhovny D, Sali A, Nava-Tudela A, Fushman D. Recovering a representative conformational ensemble from underdetermined macromolecular structural data. Journal of the American Chemical Society. 135: 16595-609. PMID 24093873 DOI: 10.1021/Ja4083717 |
0.65 |
|
| 2013 |
Haj-Yahya N, Haj-Yahya M, Castañeda CA, Spasser L, Hemantha HP, Jbara M, Penner M, Ciechanover A, Fushman D, Brik A. Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: organic chemistry applied to synthetic proteins. Angewandte Chemie (International Ed. in English). 52: 11149-53. PMID 24006204 DOI: 10.1002/Anie.201306118 |
0.426 |
|
| 2013 |
Castañeda CA, Kashyap TR, Nakasone MA, Krueger S, Fushman D. Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains. Structure (London, England : 1993). 21: 1168-81. PMID 23823328 DOI: 10.1016/J.Str.2013.04.029 |
0.364 |
|
| 2013 |
Nakasone MA, Livnat-Levanon N, Glickman MH, Cohen RE, Fushman D. Mixed-linkage ubiquitin chains send mixed messages. Structure (London, England : 1993). 21: 727-40. PMID 23562397 DOI: 10.1016/J.Str.2013.02.019 |
0.338 |
|
| 2013 |
Dixon EK, Castañeda CA, Kashyap TR, Wang Y, Fushman D. Nonenzymatic assembly of branched polyubiquitin chains for structural and biochemical studies. Bioorganic & Medicinal Chemistry. 21: 3421-9. PMID 23557636 DOI: 10.1016/J.Bmc.2013.02.052 |
0.431 |
|
| 2013 |
Roscoe BP, Thayer KM, Zeldovich KB, Fushman D, Bolon DNA. Analyses of the effects of all ubiquitin point mutants on yeast growth rate Journal of Molecular Biology. 425: 1363-1377. PMID 23376099 DOI: 10.1016/J.Jmb.2013.01.032 |
0.342 |
|
| 2013 |
Castaneda CA, Dixon E, Chaturvedi A, Krueger S, Cropp TA, Fushman D. Effect of Different Lysine Linkages on Polyubiquitin Chain Structure and Function Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.133 |
0.383 |
|
| 2012 |
Singh RK, Zerath S, Kleifeld O, Scheffner M, Glickman MH, Fushman D. Recognition and cleavage of related to ubiquitin 1 (Rub1) and Rub1-ubiquitin chains by components of the ubiquitin-proteasome system. Molecular & Cellular Proteomics : McP. 11: 1595-611. PMID 23105008 DOI: 10.1074/Mcp.M112.022467 |
0.417 |
|
| 2012 |
Cannon J, Nakasone M, Fushman D, Fenselau C. Proteomic identification and analysis of K63-linked ubiquitin conjugates. Analytical Chemistry. 84: 10121-8. PMID 23101881 DOI: 10.1021/Ac302675Y |
0.342 |
|
| 2012 |
D'Onofrio M, Gianolio E, Ceccon A, Arena F, Zanzoni S, Fushman D, Aime S, Molinari H, Assfalg M. High relaxivity supramolecular adducts between human-liver fatty-acid-binding protein and amphiphilic Gd(III) complexes: structural basis for the design of intracellular targeting MRI probes. Chemistry (Weinheim An Der Bergstrasse, Germany). 18: 9919-28. PMID 22763949 DOI: 10.1002/Chem.201103778 |
0.385 |
|
| 2012 |
Gumerov NA, Berlin K, Fushman D, Duraiswami R. A hierarchical algorithm for fast Debye summation with applications to small angle scattering. Journal of Computational Chemistry. 33: 1981-96. PMID 22707386 DOI: 10.1002/Jcc.23025 |
0.55 |
|
| 2012 |
Lai MY, Zhang D, Laronde-Leblanc N, Fushman D. Structural and biochemical studies of the open state of Lys48-linked diubiquitin. Biochimica Et Biophysica Acta. 1823: 2046-56. PMID 22542781 DOI: 10.1016/J.Bbamcr.2012.04.003 |
0.498 |
|
| 2012 |
Lange A, Castañeda C, Hoeller D, Lancelin JM, Fushman D, Walker O. Evidence for cooperative and domain-specific binding of the signal transducing adaptor molecule 2 (STAM2) to Lys63-linked diubiquitin. The Journal of Biological Chemistry. 287: 18687-99. PMID 22493438 DOI: 10.1074/Jbc.M111.324954 |
0.46 |
|
| 2012 |
Rosenzweig R, Bronner V, Zhang D, Fushman D, Glickman MH. Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. The Journal of Biological Chemistry. 287: 14659-71. PMID 22318722 DOI: 10.1074/Jbc.M111.316323 |
0.396 |
|
| 2012 |
Fushman D. Determining protein dynamics from ¹⁵N relaxation data by using DYNAMICS. Methods in Molecular Biology (Clifton, N.J.). 831: 485-511. PMID 22167688 DOI: 10.1007/978-1-61779-480-3_24 |
0.401 |
|
| 2011 |
Fushman D, Wilkinson KD. Structure and recognition of polyubiquitin chains of different lengths and linkage. F1000 Biology Reports. 3: 26. PMID 22162729 DOI: 10.3410/B3-26 |
0.412 |
|
| 2011 |
Castañeda C, Liu J, Chaturvedi A, Nowicka U, Cropp TA, Fushman D. Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme. Journal of the American Chemical Society. 133: 17855-68. PMID 21962295 DOI: 10.1021/Ja207220G |
0.42 |
|
| 2011 |
Castañeda CA, Spasser L, Bavikar SN, Brik A, Fushman D. Segmental isotopic labeling of ubiquitin chains to unravel monomer-specific molecular behavior. Angewandte Chemie (International Ed. in English). 50: 11210-4. PMID 21957015 DOI: 10.1002/Anie.201104649 |
0.431 |
|
| 2011 |
Bornet A, Ahuja P, Sarkar R, Fernandes L, Hadji S, Lee SY, Haririnia A, Fushman D, Bodenhausen G, Vasos PR. Long-lived states to monitor protein unfolding by proton NMR. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 12: 2729-34. PMID 21882334 DOI: 10.1002/Cphc.201100365 |
0.387 |
|
| 2011 |
Berlin K, O'Leary DP, Fushman D. Fast approximations of the rotational diffusion tensor and their application to structural assembly of molecular complexes. Proteins. 79: 2268-81. PMID 21604302 DOI: 10.1002/Prot.23053 |
0.612 |
|
| 2011 |
Cai L, Kosov DS, Fushman D. Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G. Journal of Biomolecular Nmr. 50: 19-33. PMID 21305337 DOI: 10.1007/S10858-011-9474-8 |
0.361 |
|
| 2011 |
Castañeda CA, Liu J, Kashyap TR, Singh RK, Fushman D, Cropp TA. Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups. Chemical Communications (Cambridge, England). 47: 2026-8. PMID 21212884 DOI: 10.1039/C0Cc04868B |
0.388 |
|
| 2011 |
Castaneda CA, Kashyap T, Fushman D. K11-linked Diubiquitin Exhibits Significant Interdomain Dynamics Biophysical Journal. 100: 3-5. DOI: 10.1016/J.Bpj.2010.12.2233 |
0.32 |
|
| 2011 |
Bornet A, Ahuja P, Sarkar R, Fernandes L, Hadji S, Lee SY, Haririnia A, Fushman D, Bodenhausen G, Vasos PR. Cover Picture: Long-Lived States to Monitor Protein Unfolding by Proton NMR (ChemPhysChem 15/2011) Chemphyschem. 12: 2677-2677. DOI: 10.1002/Cphc.201190075 |
0.332 |
|
| 2010 |
Caceres A, Shang F, Wawrousek E, Liu Q, Avidan O, Cvekl A, Yang Y, Haririnia A, Storaska A, Fushman D, Kuszak J, Dudek E, Smith D, Taylor A. Perturbing the ubiquitin pathway reveals how mitosis is hijacked to denucleate and regulate cell proliferation and differentiation in vivo. Plos One. 5: e13331. PMID 20975996 DOI: 10.1371/Journal.Pone.0013331 |
0.303 |
|
| 2010 |
Li Y, Yu X, Ho J, Fushman D, Allewell NM, Tuchman M, Shi D. Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry. 49: 6887-95. PMID 20695527 DOI: 10.1021/Bi1007386 |
0.362 |
|
| 2010 |
Berlin K, O'Leary DP, Fushman D. Structural assembly of molecular complexes based on residual dipolar couplings. Journal of the American Chemical Society. 132: 8961-72. PMID 20550109 DOI: 10.1021/Ja100447P |
0.641 |
|
| 2010 |
Fushman D, Walker O. Exploring the linkage dependence of polyubiquitin conformations using molecular modeling. Journal of Molecular Biology. 395: 803-14. PMID 19853612 DOI: 10.1016/J.Jmb.2009.10.039 |
0.348 |
|
| 2009 |
Zhang D, Chen T, Ziv I, Rosenzweig R, Matiuhin Y, Bronner V, Glickman MH, Fushman D. Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Molecular Cell. 36: 1018-33. PMID 20064467 DOI: 10.1016/J.Molcel.2009.11.012 |
0.393 |
|
| 2009 |
Berlin K, O'Leary DP, Fushman D. Improvement and analysis of computational methods for prediction of residual dipolar couplings. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 201: 25-33. PMID 19700353 DOI: 10.1016/J.Jmr.2009.07.028 |
0.573 |
|
| 2009 |
Zhang N, Wang Q, Ehlinger A, Randles L, Lary JW, Kang Y, Haririnia A, Storaska AJ, Cole JL, Fushman D, Walters KJ. Structure of the s5a:k48-linked diubiquitin complex and its interactions with rpn13. Molecular Cell. 35: 280-90. PMID 19683493 DOI: 10.1016/J.Molcel.2009.06.010 |
0.387 |
|
| 2009 |
Cai L, Fushman D, Kosov DS. Density functional calculations of chemical shielding of backbone 15N in helical residues of protein G. Journal of Biomolecular Nmr. 45: 245-53. PMID 19644655 DOI: 10.1007/S10858-009-9358-3 |
0.403 |
|
| 2009 |
Sims JJ, Haririnia A, Dickinson BC, Fushman D, Cohen RE. Avid interactions underlie the Lys63-linked polyubiquitin binding specificities observed for UBA domains. Nature Structural & Molecular Biology. 16: 883-9. PMID 19620964 DOI: 10.1038/Nsmb.1637 |
0.68 |
|
| 2009 |
Wang T, Yin L, Cooper EM, Lai MY, Dickey S, Pickart CM, Fushman D, Wilkinson KD, Cohen RE, Wolberger C. Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1. Journal of Molecular Biology. 386: 1011-23. PMID 19211026 DOI: 10.1016/J.Jmb.2008.12.085 |
0.321 |
|
| 2008 |
Chen T, Zhang D, Matiuhin Y, Glickman M, Fushman D. 1H, 13C, and 15N resonance assignment of the ubiquitin-like domain from Dsk2p. Biomolecular Nmr Assignments. 2: 147-9. PMID 19636891 DOI: 10.1007/S12104-008-9107-7 |
0.449 |
|
| 2008 |
Cai L, Fushman D, Kosov DS. Density functional calculations of 15N chemical shifts in solvated dipeptides. Journal of Biomolecular Nmr. 41: 77-88. PMID 18484179 DOI: 10.1007/S10858-008-9241-7 |
0.384 |
|
| 2008 |
Zhang D, Raasi S, Fushman D. Affinity makes the difference: nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains. Journal of Molecular Biology. 377: 162-80. PMID 18241885 DOI: 10.1016/J.Jmb.2007.12.029 |
0.507 |
|
| 2008 |
Haririnia A, Verma R, Purohit N, Twarog MZ, Deshaies RJ, Bolon D, Fushman D. Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins. Journal of Molecular Biology. 375: 979-96. PMID 18054791 DOI: 10.1016/J.Jmb.2007.11.016 |
0.444 |
|
| 2007 |
Ryabov Y, Fushman D. Structural assembly of multidomain proteins and protein complexes guided by the overall rotational diffusion tensor. Journal of the American Chemical Society. 129: 7894-902. PMID 17550252 DOI: 10.1021/Ja071185D |
0.48 |
|
| 2007 |
Haririnia A, D'Onofrio M, Fushman D. Mapping the interactions between Lys48 and Lys63-linked di-ubiquitins and a ubiquitin-interacting motif of S5a. Journal of Molecular Biology. 368: 753-66. PMID 17368669 DOI: 10.1016/J.Jmb.2007.02.037 |
0.471 |
|
| 2007 |
Ryabov YE, Fushman D. A model of interdomain mobility in a multidomain protein. Journal of the American Chemical Society. 129: 3315-27. PMID 17319663 DOI: 10.1021/Ja067667R |
0.457 |
|
| 2007 |
Dickinson BC, Varadan R, Fushman D. Effects of cyclization on conformational dynamics and binding properties of Lys48-linked di-ubiquitin Protein Science. 16: 369-378. PMID 17242378 DOI: 10.1110/Ps.062508007 |
0.807 |
|
| 2007 |
Eddins MJ, Varadan R, Fushman D, Pickart CM, Wolberger C. Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH. Journal of Molecular Biology. 367: 204-11. PMID 17240395 DOI: 10.1016/J.Jmb.2006.12.065 |
0.803 |
|
| 2007 |
Sadqi M, Fushman D, Muñoz V. Structural biology: Analysis of 'downhill' protein folding; analysis of protein-folding cooperativity (reply) Nature. 445: E17-E18. DOI: 10.1038/Nature05645 |
0.346 |
|
| 2006 |
Ryabov YE, Geraghty C, Varshney A, Fushman D. An efficient computational method for predicting rotational diffusion tensors of globular proteins using an ellipsoid representation. Journal of the American Chemical Society. 128: 15432-44. PMID 17132010 DOI: 10.1021/Ja062715T |
0.39 |
|
| 2006 |
Vasos PR, Hall JB, Kümmerle R, Fushman D. Measurement of 15N relaxation in deuterated amide groups in proteins using direct nitrogen detection. Journal of Biomolecular Nmr. 36: 27-36. PMID 16967194 DOI: 10.1007/S10858-006-9063-4 |
0.368 |
|
| 2006 |
Ryabov Y, Fushman D. Analysis of interdomain dynamics in a two-domain protein using residual dipolar couplings together with 15N relaxation data. Magnetic Resonance in Chemistry : Mrc. 44: S143-51. PMID 16823894 DOI: 10.1002/Mrc.1822 |
0.466 |
|
| 2006 |
Sadqi M, Fushman D, Muñoz V. Atom-by-atom analysis of global downhill protein folding. Nature. 442: 317-21. PMID 16799571 DOI: 10.1038/Nature04859 |
0.426 |
|
| 2006 |
Hall JB, Fushman D. Variability of the 15N chemical shielding tensors in the B3 domain of protein G from 15N relaxation measurements at several fields. Implications for backbone order parameters. Journal of the American Chemical Society. 128: 7855-70. PMID 16771499 DOI: 10.1021/Ja060406X |
0.369 |
|
| 2006 |
Ryabov Y, Fushman D. Interdomain mobility in di-ubiquitin revealed by NMR. Proteins. 63: 787-96. PMID 16609980 DOI: 10.1002/Prot.20917 |
0.516 |
|
| 2005 |
Ranjani Varadan, Assfalg M, Fushman D. Using NMR spectroscopy to monitor ubiquitin chain conformation and interactions with ubiquitin-binding domains. Methods in Enzymology. 399: 177-92. PMID 16338356 DOI: 10.1016/S0076-6879(05)99012-5 |
0.487 |
|
| 2005 |
Raasi S, Varadan R, Fushman D, Pickart CM. Diverse polyubiquitin interaction properties of ubiquitin-associated domains Nature Structural and Molecular Biology. 12: 708-714. PMID 16007098 DOI: 10.1038/Nsmb962 |
0.789 |
|
| 2005 |
Varadan R, Assfalg M, Raasi S, Pickart C, Fushman D. Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain. Molecular Cell. 18: 687-98. PMID 15949443 DOI: 10.1016/J.Molcel.2005.05.013 |
0.808 |
|
| 2005 |
van Dijk AD, Fushman D, Bonvin AM. Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data. Proteins. 60: 367-81. PMID 15937902 DOI: 10.1002/Prot.20476 |
0.418 |
|
| 2005 |
Vasos PR, Hall JB, Fushman D. Spin-state selection for increased confidence in cross-correlation rates measurements. Journal of Biomolecular Nmr. 31: 149-54. PMID 15772754 DOI: 10.1007/S10858-004-7562-8 |
0.331 |
|
| 2004 |
Pickart CM, Fushman D. Polyubiquitin chains: Polymeric protein signals Current Opinion in Chemical Biology. 8: 610-616. PMID 15556404 DOI: 10.1016/J.Cbpa.2004.09.009 |
0.433 |
|
| 2004 |
Verma R, Peters NR, D'Onofrio M, Tochtrop GP, Sakamoto KM, Varadan R, Zhang M, Coffino P, Fushman D, Deshaies RJ, King RW. Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain. Science (New York, N.Y.). 306: 117-20. PMID 15459393 DOI: 10.1126/Science.1100946 |
0.778 |
|
| 2004 |
Blake-Hall J, Walker O, Fushman D. Characterization of the overall rotational diffusion of a protein from 15N relaxation measurements and hydrodynamic calculations. Methods in Molecular Biology (Clifton, N.J.). 278: 139-60. PMID 15317996 DOI: 10.1385/1-59259-809-9:139 |
0.387 |
|
| 2004 |
Walker O, Varadan R, Fushman D. Efficient and accurate determination of the overall rotational diffusion tensor of a molecule from (15)N relaxation data using computer program ROTDIF. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 168: 336-45. PMID 15140445 DOI: 10.1016/J.Jmr.2004.03.019 |
0.767 |
|
| 2004 |
Varadan R, Assfalg M, Haririnia A, Raasi S, Pickart C, Fushman D. Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. The Journal of Biological Chemistry. 279: 7055-63. PMID 14645257 DOI: 10.1074/Jbc.M309184200 |
0.809 |
|
| 2004 |
Fushman D, Varadan R, Assfalg M, Walker O. Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements Progress in Nuclear Magnetic Resonance Spectroscopy. 44: 189-214. DOI: 10.1016/J.Pnmrs.2004.02.001 |
0.786 |
|
| 2003 |
Hall JB, Fushman D. Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G. Journal of Biomolecular Nmr. 27: 261-75. PMID 12975584 DOI: 10.1023/A:1025467918856 |
0.431 |
|
| 2003 |
Hall JB, Dayie KT, Fushman D. Direct measurement of the 15N CSA/dipolar relaxation interference from coupled HSQC spectra. Journal of Biomolecular Nmr. 26: 181-6. PMID 12766413 DOI: 10.1023/A:1023546107553 |
0.35 |
|
| 2003 |
Hall JB, Fushman D. Direct measurement of the transverse and longitudinal 15N chemical shift anisotropy-dipolar cross-correlation rate constants using 1H-coupled HSQC spectra Magnetic Resonance in Chemistry. 41: 837-842. DOI: 10.1002/Mrc.1253 |
0.353 |
|
| 2002 |
Varadan R, Walker O, Pickart C, Fushman D. Structural properties of polyubiquitin chains in solution. Journal of Molecular Biology. 324: 637-47. PMID 12460567 DOI: 10.1016/S0022-2836(02)01198-1 |
0.809 |
|
| 2001 |
Camarero JA, Fushman D, Cowburn D, Muir TW. Peptide chemical ligation inside living cells: in vivo generation of a circular protein domain. Bioorganic & Medicinal Chemistry. 9: 2479-84. PMID 11553489 DOI: 10.1016/S0968-0896(01)00217-6 |
0.705 |
|
| 2001 |
Fushman D, Cowburn D. Nuclear magnetic resonance relaxation in determination of residue-specific 15N chemical shift tensors in proteins in solution: protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy. Methods in Enzymology. 339: 109-26. PMID 11462809 DOI: 10.1016/S0076-6879(01)39312-6 |
0.716 |
|
| 2001 |
Pfeiffer S, Fushman D, Cowburn D. Simulated and NMR-derived backbone dynamics of a protein with significant flexibility: a comparison of spectral densities for the betaARK1 PH domain. Journal of the American Chemical Society. 123: 3021-36. PMID 11457013 DOI: 10.1021/Ja0031117 |
0.689 |
|
| 2001 |
Camarero JA, Fushman D, Sato S, Giriat I, Cowburn D, Raleigh DP, Muir TW. Rescuing a destabilized protein fold through backbone cyclization. Journal of Molecular Biology. 308: 1045-62. PMID 11352590 DOI: 10.1006/Jmbi.2001.4631 |
0.73 |
|
| 2001 |
Ghose R, Fushman D, Cowburn D. Determination of the rotational diffusion tensor of macromolecules in solution from nmr relaxation data with a combination of exact and approximate methods--application to the determination of interdomain orientation in multidomain proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 149: 204-17. PMID 11318619 DOI: 10.1006/Jmre.2001.2295 |
0.742 |
|
| 2000 |
Nicholas P, Fushman D, Ruchinsky V, Cowburn D. The virtual NMR spectrometer: a computer program for efficient simulation of NMR experiments involving pulsed field gradients. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 145: 262-75. PMID 10910695 DOI: 10.1006/Jmre.2000.2108 |
0.649 |
|
| 2000 |
Fushman D, Ghose R, Cowburn D. The effect of finite sampling on the determination of orientational properties: A theoretical treatment with application to interatomic vectors in proteins Journal of the American Chemical Society. 122: 10640-10649. DOI: 10.1021/Ja001128J |
0.728 |
|
| 1999 |
Fushman D, Xu R, Cowburn D. Direct determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32). Biochemistry. 38: 10225-30. PMID 10441115 DOI: 10.1021/Bi990897G |
0.747 |
|
| 1999 |
Lücke C, Fushman D, Ludwig C, Hamilton JA, Sacchettini JC, Rüterjans H. A comparative study of the backbone dynamics of two closely related lipid binding proteins: bovine heart fatty acid binding protein and porcine ileal lipid binding protein. Molecular and Cellular Biochemistry. 192: 109-21. PMID 10331665 DOI: 10.1023/A:1006834708786 |
0.412 |
|
| 1999 |
Pfeiffer S, Fushman D, Cowburn D. Impact of Cl- and Na+ ions on simulated structure and dynamics of betaARK1 PH domain. Proteins. 35: 206-17. PMID 10223293 DOI: 10.1002/(Sici)1097-0134(19990501)35:2<206::Aid-Prot7>3.0.Co;2-A |
0.672 |
|
| 1999 |
McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D. Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. Cell. 96: 625-34. PMID 10089878 DOI: 10.1016/S0092-8674(00)80573-5 |
0.683 |
|
| 1999 |
Fushman D, Cowburn D. The effect of noncollinearity of 15N-1H dipolar and 15N CSA tensors and rotational anisotropy on 15N relaxation, CSA/dipolar cross correlation, and TROSY. Journal of Biomolecular Nmr. 13: 139-47. PMID 10070755 DOI: 10.1023/A:1008349331773 |
0.689 |
|
| 1999 |
Fushman D, Tjandra N, Cowburn D. An approach to direct determination of protein dynamics from 15N NMR relaxation at multiple fields, independent of variable 15N chemical shift anisotropy and chemical exchange contributions Journal of the American Chemical Society. 121: 8577-8582. DOI: 10.1021/Ja9904991 |
0.7 |
|
| 1998 |
McDonnell JM, Fushman D, Cahill SM, Zhou W, Wolven A, Wilson CB, Nelle TD, Resh MD, Wills J, Cowburn D. Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus. Journal of Molecular Biology. 279: 921-8. PMID 9642071 DOI: 10.1006/Jmbi.1998.1788 |
0.693 |
|
| 1998 |
Fushman D, Najmabadi-Haske T, Cahill S, Zheng J, LeVine H, Cowburn D. The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits. The Journal of Biological Chemistry. 273: 2835-43. PMID 9446593 DOI: 10.1074/Jbc.273.5.2835 |
0.717 |
|
| 1998 |
Fushman D, Tjandra N, Cowburn D. Direct measurement of 15N chemical shift anisotropy in solution Journal of the American Chemical Society. 120: 10947-10952. DOI: 10.1021/Ja981686M |
0.687 |
|
| 1998 |
Fushman D, Cowburn D. Model-independent analysis of 15N chemical shift anisotropy from NMR relaxation data. Ubiquitin as a test example [5] Journal of the American Chemical Society. 120: 7109-7110. DOI: 10.1021/Ja980565J |
0.677 |
|
| 1998 |
Xn R, Fushman D, Cahill S, Xu Q, Cowburn D. study of possible interdomain interactions in an Abl SH32 dual domain construct by solution NMR technique Faseb Journal. 12: A1448. |
0.326 |
|
| 1997 |
Fushman D, Cahill S, Cowburn D. The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration. Journal of Molecular Biology. 266: 173-94. PMID 9054979 DOI: 10.1006/Jmbi.1996.0771 |
0.721 |
|
| 1997 |
McDonnell JM, Fushman D, Cahill SM, Sutton BJ, Cowburn D. Solution structures of FcεRI α-chain mimics: A β-hairpin peptide and its retroenantiomer Journal of the American Chemical Society. 119: 5321-5328. DOI: 10.1021/Ja963884O |
0.691 |
|
| 1996 |
Zheng J, Cahill SM, Lemmon MA, Fushman D, Schlessinger J, Cowburn D. Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity. Journal of Molecular Biology. 255: 14-21. PMID 8568861 DOI: 10.1006/Jmbi.1996.0002 |
0.696 |
|
| 1996 |
Fushman D, Weisemann R, Thüring H, Ohlenschläger O, Rüterjans H. Backbone dynamics of proteins studied by two‐dimensional heteronuclear NMR spectroscopy and molecular dynamics simulations International Journal of Quantum Chemistry. 59: 291-300. DOI: 10.1002/(Sici)1097-461X(1996)59:4<291::Aid-Qua4>3.0.Co;2-T |
0.338 |
|
| 1995 |
Fushman D, Cahill S, Lemmon MA, Schlessinger J, Cowburn D. Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 92: 816-20. PMID 7846058 DOI: 10.1073/Pnas.92.3.816 |
0.734 |
|
| 1994 |
Fushman D, Weisemann R, Thüring H, Rüterjans H. Backbone dynamics of ribonuclease T1 and its complex with 2'GMP studied by two-dimensional heteronuclear NMR spectroscopy. Journal of Biomolecular Nmr. 4: 61-78. PMID 22911159 DOI: 10.1007/Bf00178336 |
0.352 |
|
| 1994 |
Fushman D, Ohlenschläger O, Rüterjans H. Determination of the backbone mobility of ribonuclease T1 and its 2'GMP complex using molecular dynamics simulations and NMR relaxation data. Journal of Biomolecular Structure & Dynamics. 11: 1377-402. PMID 7946080 DOI: 10.1080/07391102.1994.10508074 |
0.365 |
|
| 1990 |
Fushman D. Surface fractality of proteins from theory and NMR data. Journal of Biomolecular Structure & Dynamics. 7: 1333-44. PMID 2363849 DOI: 10.1080/07391102.1990.10508569 |
0.334 |
|
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