| Year |
Citation |
Score |
| 2022 |
McCallum M, Czudnochowski N, Rosen LE, Zepeda SK, Bowen JE, Walls AC, Hauser K, Joshi A, Stewart C, Dillen JR, Powell AE, Croll TI, Nix J, Virgin HW, Corti D, ... ... Veesler D, et al. Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement. Science (New York, N.Y.). eabn8652. PMID 35076256 DOI: 10.1126/science.abn8652 |
0.307 |
|
| 2020 |
Piccoli L, Park YJ, Tortorici MA, Czudnochowski N, Walls AC, Beltramello M, Silacci-Fregni C, Pinto D, Rosen LE, Bowen JE, Acton OJ, Jaconi S, Guarino B, Minola A, Zatta F, ... ... Veesler D, et al. Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology. Cell. PMID 32991844 DOI: 10.1016/J.Cell.2020.09.037 |
0.386 |
|
| 2020 |
Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls AC, Park YJ, Strauch EM, Stewart L, Diamond MS, Veesler D, Baker D. De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. Science (New York, N.Y.). PMID 32907861 DOI: 10.1126/Science.Abd9909 |
0.366 |
|
| 2020 |
Starr TN, Greaney AJ, Hilton SK, Ellis D, Crawford KHD, Dingens AS, Navarro MJ, Bowen JE, Tortorici MA, Walls AC, King NP, Veesler D, Bloom JD. Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding. Cell. PMID 32841599 DOI: 10.1016/J.Cell.2020.08.012 |
0.34 |
|
| 2020 |
McCallum M, Walls AC, Bowen JE, Corti D, Veesler D. Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation. Nature Structural & Molecular Biology. PMID 32753755 DOI: 10.1038/S41594-020-0483-8 |
0.405 |
|
| 2020 |
Ueda G, Antanasijevic A, Fallas JA, Sheffler W, Copps J, Ellis D, Hutchinson GB, Moyer A, Yasmeen A, Tsybovsky Y, Park YJ, Bick MJ, Sankaran B, Gillespie RA, Brouwer PJ, ... ... Veesler D, et al. Tailored design of protein nanoparticle scaffolds for multivalent presentation of viral glycoprotein antigens. Elife. 9. PMID 32748788 DOI: 10.7554/Elife.57659 |
0.356 |
|
| 2020 |
Pinto D, Park YJ, Beltramello M, Walls AC, Tortorici MA, Bianchi S, Jaconi S, Culap K, Zatta F, De Marco A, Peter A, Guarino B, Spreafico R, Cameroni E, Case JB, ... ... Veesler D, et al. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature. PMID 32422645 DOI: 10.1038/S41586-020-2349-Y |
0.363 |
|
| 2020 |
Crawford KHD, Eguia R, Dingens AS, Loes AN, Malone KD, Wolf CR, Chu HY, Tortorici MA, Veesler D, Murphy M, Pettie D, King NP, Balazs AB, Bloom JD. Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays. Viruses. 12. PMID 32384820 DOI: 10.3390/V12050513 |
0.364 |
|
| 2020 |
Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell. PMID 32155444 DOI: 10.1016/J.Cell.2020.02.058 |
0.36 |
|
| 2020 |
Ueda G, Antanasijevic A, Fallas JA, Sheffler W, Copps J, Ellis D, Hutchinson GB, Moyer A, Yasmeen A, Tsybovsky Y, Park Y, Bick MJ, Sankaran B, Gillespie RA, Brouwer PJ, ... ... Veesler D, et al. Author response: Tailored design of protein nanoparticle scaffolds for multivalent presentation of viral glycoprotein antigens Elife. DOI: 10.7554/Elife.57659.Sa2 |
0.305 |
|
| 2020 |
Khmelinskaia A, Borst AJ, Hsia Y, Dowling Q, Veesler D, King NP. Breaking the Symmetry of Protein Assemblies: Structural Flexibility as a De Novo Design Principle Biophysical Journal. 118: 516a-517a. DOI: 10.1016/J.Bpj.2019.11.2844 |
0.375 |
|
| 2019 |
Parks KR, MacCamy AJ, Trichka J, Gray M, Weidle C, Borst AJ, Khechaduri A, Takushi B, Agrawal P, Guenaga J, Wyatt RT, Coler R, Seaman M, LaBranche C, Montefiori DC, ... Veesler D, et al. Overcoming Steric Restrictions of VRC01 HIV-1 Neutralizing Antibodies through Immunization. Cell Reports. 29: 3060-3072.e7. PMID 31801073 DOI: 10.1016/J.Celrep.2019.10.071 |
0.326 |
|
| 2019 |
Park YJ, Walls AC, Wang Z, Sauer MM, Li W, Tortorici MA, Bosch BJ, DiMaio F, Veesler D. Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors. Nature Structural & Molecular Biology. PMID 31792450 DOI: 10.1038/S41594-019-0334-7 |
0.365 |
|
| 2019 |
Mire CE, Chan YP, Borisevich V, Cross RW, Yan L, Agans KN, Dang HV, Veesler D, Fenton KA, Geisbert TW, Broder CC. A Cross-Reactive Humanized Monoclonal Antibody Targeting Fusion Glycoprotein Function Protects Ferrets Against Lethal Nipah Virus and Hendra Virus Infection. The Journal of Infectious Diseases. PMID 31686101 DOI: 10.1093/Infdis/Jiz515 |
0.351 |
|
| 2019 |
Dang HV, Chan YP, Park YJ, Snijder J, Da Silva SC, Vu B, Yan L, Feng YR, Rockx B, Geisbert TW, Mire CE, Broder CC, Veesler D. An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections. Nature Structural & Molecular Biology. PMID 31570878 DOI: 10.1038/S41594-019-0308-9 |
0.358 |
|
| 2019 |
Tortorici MA, Veesler D. Structural insights into coronavirus entry. Advances in Virus Research. 105: 93-116. PMID 31522710 DOI: 10.1016/Bs.Aivir.2019.08.002 |
0.322 |
|
| 2019 |
Alejandra Tortorici M, Walls AC, Lang Y, Wang C, Li Z, Koerhuis D, Boons GJ, Bosch BJ, Rey FA, de Groot RJ, Veesler D. Structural basis for human coronavirus attachment to sialic acid receptors. Nature Structural & Molecular Biology. PMID 31160783 DOI: 10.1038/S41594-019-0233-Y |
0.414 |
|
| 2019 |
Walls AC, Xiong X, Park YJ, Tortorici MA, Snijder J, Quispe J, Cameroni E, Gopal R, Dai M, Lanzavecchia A, Zambon M, Rey FA, Corti D, Veesler D. Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion. Cell. PMID 30712865 DOI: 10.1016/J.Cell.2018.12.028 |
0.389 |
|
| 2019 |
Park YJ, Walls AC, Wang Z, Sauer M, Li W, Tortorici MA, Bosch BJ, DiMaio FD, Veesler D. MERS-CoV spike glycoprotein structures in complex with sialoside attachment receptors Nature Structural & Molecular Biology. DOI: 10.2210/Pdb6Q06/Pdb |
0.34 |
|
| 2019 |
Dang HV, Chan Y, Park Y, Broder CC, Veesler D. Cryo-EM Structure of Nipah Virus Fusion Glycoprotein in Complex with a Monoclonal Antibody Reveals Mechanism of Neutralization Microscopy and Microanalysis. 25: 1328-1329. DOI: 10.1017/S1431927619007372 |
0.371 |
|
| 2019 |
Walls AC, Tortorici MA, Xiong X, Snijder J, Frenz B, Bosch B, DiMaio F, Corti D, Rey FA, Veesler D. Structural Studies of Coronavirus Fusion Proteins Microscopy and Microanalysis. 25: 1300-1301. DOI: 10.1017/S1431927619007232 |
0.399 |
|
| 2018 |
Park YJ, Lacourse KD, Cambillau C, DiMaio F, Mougous JD, Veesler D. Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy. Nature Communications. 9: 5385. PMID 30568167 DOI: 10.2210/Pdb6N38/Pdb |
0.584 |
|
| 2018 |
Borst AJ, Weidle CE, Gray MD, Frenz B, Snijder J, Joyce MG, Georgiev IS, Stewart-Jones GB, Kwong PD, McGuire AT, DiMaio F, Stamatatos L, Pancera M, Veesler D. Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer and a glycosylated HIV-1 gp120 core. Elife. 7. PMID 30403372 DOI: 10.2210/Pdb6Mft/Pdb |
0.35 |
|
| 2018 |
Frenz B, Rämisch S, Borst AJ, Walls AC, Adolf-Bryfogle J, Schief WR, Veesler D, DiMaio F. Automatically Fixing Errors in Glycoprotein Structures with Rosetta. Structure (London, England : 1993). PMID 30344107 DOI: 10.1016/J.Str.2018.09.006 |
0.391 |
|
| 2018 |
Ting SY, Bosch DE, Mangiameli SM, Radey MC, Huang S, Park YJ, Kelly KA, Filip SK, Goo YA, Eng JK, Allaire M, Veesler D, Wiggins PA, Peterson SB, Mougous JD. Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins. Cell. PMID 30343895 DOI: 10.1016/J.Cell.2018.09.037 |
0.376 |
|
| 2018 |
Snijder J, Ortego MS, Weidle C, Stuart AB, Gray MD, McElrath MJ, Pancera M, Veesler D, McGuire AT. An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus. Immunity. 48: 799-811.e9. PMID 29669253 DOI: 10.1016/J.Immuni.2018.03.026 |
0.414 |
|
| 2018 |
Xu N, Veesler D, Doerschuk PC, Johnson JE. Allosteric effects in bacteriophage HK97 procapsids revealed directly from covariance analysis of cryo EM data. Journal of Structural Biology. PMID 29331608 DOI: 10.1016/J.Jsb.2017.12.013 |
0.309 |
|
| 2017 |
Xiong X, Tortorici MA, Snijder J, Yoshioka C, Walls AC, Li W, McGuire AT, Rey FA, Bosch BJ, Veesler D. Glycan shield and fusion activation of a deltacoronavirus spike glycoprotein fine-tuned for enteric infections. Journal of Virology. PMID 29093093 DOI: 10.1128/Jvi.01628-17 |
0.453 |
|
| 2017 |
Walls AC, Tortorici MA, Snijder J, Xiong X, Bosch BJ, Rey FA, Veesler D. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proceedings of the National Academy of Sciences of the United States of America. 114: 11157-11162. PMID 29073020 DOI: 10.1073/Pnas.1708727114 |
0.407 |
|
| 2017 |
Borst AJ, James ZM, Zagotta WN, Ginsberg M, Rey FA, DiMaio F, Backovic M, Veesler D. The Therapeutic Antibody LM609 Selectively Inhibits Ligand Binding to Human αVβ3 Integrin via Steric Hindrance. Structure (London, England : 1993). PMID 29033288 DOI: 10.1016/J.Str.2017.09.007 |
0.369 |
|
| 2017 |
Nygren PJ, Mehta S, Schweppe DK, Langeberg LK, Whiting JL, Weisbrod CR, Bruce JE, Zhang J, Veesler D, Scott JD. Intrinsic disorder within AKAP79 fine-tunes anchored phosphatase activity toward substrates and drug sensitivity. Elife. 6. PMID 28967377 DOI: 10.7554/Elife.30872 |
0.327 |
|
| 2017 |
Smith FD, Esseltine JL, Nygren PJ, Veesler D, Byrne DP, Vonderach M, Strashnov I, Eyers CE, Eyers PA, Langeberg LK, Scott JD. Local protein kinase A action proceeds through intact holoenzymes. Science (New York, N.Y.). 356: 1288-1293. PMID 28642438 DOI: 10.1126/Science.Aaj1669 |
0.313 |
|
| 2017 |
Frenz B, Walls AC, Egelman EH, Veesler D, DiMaio F. RosettaES: a sampling strategy enabling automated interpretation of difficult cryo-EM maps. Nature Methods. PMID 28628127 DOI: 10.1038/Nmeth.4340 |
0.334 |
|
| 2017 |
Yu X, Veesler D, Campbell MG, Barry ME, Asturias FJ, Barry MA, Reddy VS. Cryo-EM structure of human adenovirus D26 reveals the conservation of structural organization among human adenoviruses. Science Advances. 3: e1602670. PMID 28508067 DOI: 10.1126/Sciadv.1602670 |
0.377 |
|
| 2016 |
Eshraghi A, Kim J, Walls AC, Ledvina HE, Miller CN, Ramsey KM, Whitney JC, Radey MC, Peterson SB, Ruhland BR, Tran BQ, Goo YA, Goodlett DR, Dove SL, Celli J, ... Veesler D, et al. Secreted Effectors Encoded within and outside of the Francisella Pathogenicity Island Promote Intramacrophage Growth. Cell Host & Microbe. 20: 573-583. PMID 27832588 DOI: 10.1016/J.Chom.2016.10.008 |
0.383 |
|
| 2016 |
Walls A, Tortorici MA, Bosch BJ, Frenz B, Rottier PJ, DiMaio F, Rey F, Veesler D. Crucial steps in the structure determination of a coronavirus spike glycoprotein using cryo-electron microscopy. Protein Science : a Publication of the Protein Society. PMID 27667334 DOI: 10.1002/Pro.3048 |
0.423 |
|
| 2016 |
Walls AC, Tortorici MA, Frenz B, Snijder J, Li W, Rey FA, DiMaio F, Bosch BJ, Veesler D. Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy. Nature Structural & Molecular Biology. PMID 27617430 DOI: 10.1038/Nsmb.3293 |
0.487 |
|
| 2016 |
Yap ML, Klose T, Arisaka F, Speir JA, Veesler D, Fokine A, Rossmann MG. Role of bacteriophage T4 baseplate in regulating assembly and infection. Proceedings of the National Academy of Sciences of the United States of America. PMID 26929357 DOI: 10.1073/Pnas.1601654113 |
0.373 |
|
| 2016 |
Walls AC, Tortorici MA, Bosch BJ, Frenz B, Rottier PJ, DiMaio F, Rey FA, Veesler D. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer. Nature. 531: 114-7. PMID 26855426 DOI: 10.1038/Nature16988 |
0.47 |
|
| 2016 |
Veesler D, Kearney BM, Johnson JE. Integration of X-ray crystallography and electron cryo-microscopy in the analysis of virus structure and function Crystallography Reviews. 22: 102-127. DOI: 10.1080/0889311X.2015.1038530 |
0.406 |
|
| 2015 |
Gong Y, Veesler D, Doerschuk PC, Johnson JE. Effect of the viral protease on the dynamics of bacteriophage HK97 maturation intermediates characterized by variance analysis of cryo EM particle ensembles. Journal of Structural Biology. PMID 26724602 DOI: 10.1016/J.Jsb.2015.12.012 |
0.366 |
|
| 2014 |
Campbell MG, Kearney BM, Cheng A, Potter CS, Johnson JE, Carragher B, Veesler D. Near-atomic resolution reconstructions using a mid-range electron microscope operated at 200 kV. Journal of Structural Biology. 188: 183-7. PMID 25278130 DOI: 10.1016/J.Jsb.2014.09.008 |
0.357 |
|
| 2014 |
Veesler D, Cupelli K, Burger M, Gräber P, Stehle T, Johnson JE. Single-particle EM reveals plasticity of interactions between the adenovirus penton base and integrin αVβ3. Proceedings of the National Academy of Sciences of the United States of America. 111: 8815-9. PMID 24889614 DOI: 10.1073/Pnas.1404575111 |
0.408 |
|
| 2014 |
Spinelli S, Veesler D, Bebeacua C, Cambillau C. Structures and host-adhesion mechanisms of lactococcal siphophages. Frontiers in Microbiology. 5: 3. PMID 24474948 DOI: 10.3389/Fmicb.2014.00003 |
0.599 |
|
| 2014 |
Veesler D, Khayat R, Krishnamurthy S, Snijder J, Huang RK, Heck AJ, Anand GS, Johnson JE. Architecture of a dsDNA viral capsid in complex with its maturation protease. Structure (London, England : 1993). 22: 230-7. PMID 24361271 DOI: 10.1016/J.Str.2013.11.007 |
0.359 |
|
| 2013 |
Veesler D, Campbell MG, Cheng A, Fu CY, Murez Z, Johnson JE, Potter CS, Carragher B. Maximizing the potential of electron cryomicroscopy data collected using direct detectors. Journal of Structural Biology. 184: 193-202. PMID 24036281 DOI: 10.1016/J.Jsb.2013.09.003 |
0.303 |
|
| 2013 |
Bebeacua C, Tremblay D, Farenc C, Chapot-Chartier MP, Sadovskaya I, van Heel M, Veesler D, Moineau S, Cambillau C. Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2 Journal of Virology. 87: 12302-12312. PMID 24027307 DOI: 10.1128/Jvi.02033-13 |
0.602 |
|
| 2013 |
Veesler D, Johnson JE. Cystovirus maturation at atomic resolution. Structure (London, England : 1993). 21: 1266-8. PMID 23931138 DOI: 10.1016/J.Str.2013.07.009 |
0.441 |
|
| 2013 |
Collins B, Bebeacua C, Mahony J, Blangy S, Douillard FP, Veesler D, Cambillau C, van Sinderen D. Structure and functional analysis of the host recognition device of lactococcal phage tuc2009. Journal of Virology. 87: 8429-40. PMID 23698314 DOI: 10.1128/Jvi.00907-13 |
0.601 |
|
| 2013 |
Desmyter A, Farenc C, Mahony J, Spinelli S, Bebeacua C, Blangy S, Veesler D, Van Sinderen D, Cambillau C. Viral infection modulation and neutralization by camelid nanobodies Proceedings of the National Academy of Sciences of the United States of America. 110. PMID 23530214 DOI: 10.1073/Pnas.1301336110 |
0.593 |
|
| 2013 |
Veesler D, Ng TS, Sendamarai AK, Eilers BJ, Lawrence CM, Lok SM, Young MJ, Johnson JE, Fu CY. Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography. Proceedings of the National Academy of Sciences of the United States of America. 110: 5504-9. PMID 23520050 DOI: 10.1073/Pnas.1300601110 |
0.453 |
|
| 2013 |
Snijder J, Rose RJ, Veesler D, Johnson JE, Heck AJ. Studying 18 MDa virus assemblies with native mass spectrometry. Angewandte Chemie (International Ed. in English). 52: 4020-3. PMID 23450509 DOI: 10.1002/Anie.201210197 |
0.317 |
|
| 2013 |
Bebeacua C, Lai L, Vegge CS, Brøndsted L, van Heel M, Veesler D, Cambillau C. Visualizing a complete Siphoviridae member by single-particle electron microscopy: The structure of lactococcal phage TP901-1 Journal of Virology. 87: 1061-1068. PMID 23135714 DOI: 10.1128/Jvi.02836-12 |
0.602 |
|
| 2012 |
Veesler D, Quispe J, Grigorieff N, Potter CS, Carragher B, Johnson JE. Maturation in action: CryoEM study of a viral capsid caught during expansion. Structure (London, England : 1993). 20: 1384-90. PMID 22748764 DOI: 10.1016/J.Str.2012.05.011 |
0.351 |
|
| 2012 |
Veesler D, Spinelli S, Mahony J, Lichière J, Blangy S, Bricogne G, Legrand P, Ortiz-Lombardia M, Campanacci V, van Sinderen D, Cambillau C. Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism. Proceedings of the National Academy of Sciences of the United States of America. 109: 8954-8. PMID 22611190 DOI: 10.1073/Pnas.1200966109 |
0.582 |
|
| 2011 |
Veesler D, Cambillau C. A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries. Microbiology and Molecular Biology Reviews : Mmbr. 75: 423-33, first page o. PMID 21885679 DOI: 10.1128/Mmbr.00014-11 |
0.584 |
|
| 2011 |
Shepherd DA, Veesler D, Lichière J, Ashcroft AE, Cambillau C. Unraveling lactococcal phage baseplate assembly by mass spectrometry. Molecular & Cellular Proteomics : McP. 10: M111.009787. PMID 21646642 DOI: 10.1074/Mcp.M111.009787 |
0.578 |
|
| 2011 |
Goulet A, Lai-Kee-Him J, Veesler D, Auzat I, Robin G, Shepherd DA, Ashcroft AE, Richard E, Lichière J, Tavares P, Cambillau C, Bron P. The opening of the SPP1 bacteriophage tail, a prevalent mechanism in Gram-positive-infecting siphophages. The Journal of Biological Chemistry. 286: 25397-405. PMID 21622577 DOI: 10.1074/Jbc.M111.243360 |
0.732 |
|
| 2010 |
Bebeacua C, Bron P, Lai L, Vegge CS, Brøndsted L, Spinelli S, Campanacci V, Veesler D, Van Heel M, Cambillau C. Structure and molecular assignment of lactococcal phage TP901-1 baseplate Journal of Biological Chemistry. 285: 39079-39086. PMID 20937834 DOI: 10.1074/Jbc.M110.175646 |
0.613 |
|
| 2010 |
Veesler D, Robin G, Lichière J, Auzat I, Tavares P, Bron P, Campanacci V, Cambillau C. Crystal structure of bacteriophage SPP1 distal tail protein (gp19.1): a baseplate hub paradigm in gram-positive infecting phages. The Journal of Biological Chemistry. 285: 36666-73. PMID 20843802 DOI: 10.1074/Jbc.M110.157529 |
0.632 |
|
| 2010 |
Veesler D, Blangy S, Lichière J, Ortiz-Lombardía M, Tavares P, Campanacci V, Cambillau C. Crystal structure of Bacillus subtilis SPP1 phage gp23.1, a putative chaperone. Protein Science : a Publication of the Protein Society. 19: 1812-6. PMID 20665904 DOI: 10.1002/Pro.464 |
0.599 |
|
| 2010 |
Veesler D, Blangy S, Spinelli S, Tavares P, Campanacci V, Cambillau C. Crystal structure of Bacillus subtilis SPP1 phage gp22 shares fold similarity with a domain of lactococcal phage p2 RBP. Protein Science : a Publication of the Protein Society. 19: 1439-43. PMID 20506290 DOI: 10.1002/Pro.416 |
0.579 |
|
| 2010 |
Campanacci V, Veesler D, Lichière J, Blangy S, Sciara G, Moineau S, van Sinderen D, Bron P, Cambillau C. Solution and electron microscopy characterization of lactococcal phage baseplates expressed in Escherichia coli. Journal of Structural Biology. 172: 75-84. PMID 20153432 DOI: 10.1016/J.Jsb.2010.02.007 |
0.599 |
|
| 2009 |
Veesler D, Dreier B, Blangy S, Lichière J, Tremblay D, Moineau S, Spinelli S, Tegoni M, Plückthun A, Campanacci V, Cambillau C. Crystal structure and function of a DARPin neutralizing inhibitor of lactococcal phage TP901-1: comparison of DARPin and camelid VHH binding mode. The Journal of Biological Chemistry. 284: 30718-26. PMID 19740746 DOI: 10.1074/Jbc.M109.037812 |
0.595 |
|
| 2009 |
Veesler D, Blangy S, Siponen M, Vincentelli R, Cambillau C, Sciara G. Production and biophysical characterization of the CorA transporter from Methanosarcina mazei. Analytical Biochemistry. 388: 115-21. PMID 19233118 DOI: 10.1016/J.Ab.2009.02.018 |
0.519 |
|
| 2008 |
Veesler D, Blangy S, Cambillau C, Sciara G. There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 64: 880-5. PMID 18931428 DOI: 10.1107/S1744309108028248 |
0.539 |
|
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