Robert M. Immormino, Ph.D. - Publications

Affiliations: 
2007 Duke University, Durham, NC 
Area:
Biochemistry

13 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Huck JD, Que NLS, Immormino RM, Shrestha L, Taldone T, Chiosis G, Gewirth DT. NECA derivatives exploit the paralog-specific properties of the Site 3 side pocket of Grp94, the ER Hsp90. The Journal of Biological Chemistry. PMID 31501246 DOI: 10.1074/Jbc.Ra119.009960  0.763
2015 Immormino RM, Starbird CA, Silversmith RE, Bourret RB. Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases. Biochemistry. 54: 3514-27. PMID 25928369 DOI: 10.1021/acs.biochem.5b00286  0.311
2012 Chen VB, Arendall WB, Headd JJ, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC. Chapter 21.6 MolProbity: all-atom structure validation for macromolecular crystallography International Tables For Crystallography. DOI: 10.1107/97809553602060000884  0.358
2010 Chen VB, Arendall WB, Headd JJ, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallographica. Section D, Biological Crystallography. 66: 12-21. PMID 20057044 DOI: 10.1107/S0907444909042073  0.38
2009 Immormino RM, Metzger LE, Reardon PN, Dollins DE, Blagg BS, Gewirth DT. Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. Journal of Molecular Biology. 388: 1033-42. PMID 19361515 DOI: 10.1016/J.Jmb.2009.03.071  0.724
2009 Headd JJ, Immormino RM, Keedy DA, Emsley P, Richardson DC, Richardson JS. Autofix for backward-fit sidechains: using MolProbity and real-space refinement to put misfits in their place. Journal of Structural and Functional Genomics. 10: 83-93. PMID 19002604 DOI: 10.1007/S10969-008-9045-8  0.35
2008 Richardson JS, Schneider B, Murray LW, Kapral GJ, Immormino RM, Headd JJ, Richardson DC, Ham D, Hershkovits E, Williams LD, Keating KS, Pyle AM, Micallef D, Westbrook J, Berman HM, et al. RNA backbone: consensus all-angle conformers and modular string nomenclature (an RNA Ontology Consortium contribution). Rna (New York, N.Y.). 14: 465-81. PMID 18192612 DOI: 10.1261/Rna.657708  0.316
2007 Dollins DE, Warren JJ, Immormino RM, Gewirth DT. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Molecular Cell. 28: 41-56. PMID 17936703 DOI: 10.1016/J.Molcel.2007.08.024  0.753
2006 Immormino RM, Kang Y, Chiosis G, Gewirth DT. Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors. Journal of Medicinal Chemistry. 49: 4953-60. PMID 16884307 DOI: 10.1021/Jm060297X  0.757
2006 Williams AH, Immormino RM, Gewirth DT, Raetz CR. Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide. Proceedings of the National Academy of Sciences of the United States of America. 103: 10877-82. PMID 16835299 DOI: 10.1073/Pnas.0604465103  0.668
2006 He H, Zatorska D, Kim J, Aguirre J, Llauger L, She Y, Wu N, Immormino RM, Gewirth DT, Chiosis G. Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90. Journal of Medicinal Chemistry. 49: 381-90. PMID 16392823 DOI: 10.1021/Jm0508078  0.704
2005 Dollins DE, Immormino RM, Gewirth DT. Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change. The Journal of Biological Chemistry. 280: 30438-47. PMID 15951571 DOI: 10.1074/Jbc.M503761200  0.748
2004 Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. The Journal of Biological Chemistry. 279: 46162-71. PMID 15292259 DOI: 10.1074/Jbc.M405253200  0.693
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