Adrian Goldman - Publications

Affiliations: 
University of Leeds, Leeds, England, United Kingdom 
Area:
Structural Biology
Website:
https://biologicalsciences.leeds.ac.uk/school-biomedical-sciences/staff/72/adrian-goldman

76 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
2020 Harborne SPD, Strauss J, Boakes JC, Wright DL, Henderson JG, Boivineau J, Jaakola VP, Goldman A. IMPROvER: the Integral Membrane Protein Stability Selector. Scientific Reports. 10: 15165. PMID 32938971 DOI: 10.1038/s41598-020-71744-x  0.56
2020 Johansson NG, Turku A, Vidilaseris K, Dreano L, Khattab A, Ayuso Pérez D, Wilkinson A, Zhang Y, Tamminen M, Grazhdankin E, Kiriazis A, Fishwick CWG, Meri S, Yli-Kauhaluoma J, Goldman A, et al. Discovery of Membrane-Bound Pyrophosphatase Inhibitors Derived from an Isoxazole Fragment. Acs Medicinal Chemistry Letters. 11: 605-610. PMID 32292570 DOI: 10.1021/acsmedchemlett.9b00537  0.48
2019 Alfaro-Chávez AL, Liu JW, Stevenson BJ, Goldman A, Ollis DL. Evolving a lipase for hydrolysis of natural triglycerides along with enhanced tolerance towards a protease and surfactants. Protein Engineering, Design & Selection : Peds. PMID 31504920 DOI: 10.1093/protein/gzz023  0.6
2019 Alfaro-Chávez AL, Liu JW, Porter JL, Goldman A, Ollis DL. Improving on nature's shortcomings: evolving a lipase for increased lipolytic activity, expression and thermostability. Protein Engineering, Design & Selection : Peds. PMID 31403166 DOI: 10.1093/protein/gzz024  0.6
2019 Vidilaseris K, Kiriazis A, Turku A, Khattab A, Johansson NG, Leino TO, Kiuru PS, Boije Af Gennäs G, Meri S, Yli-Kauhaluoma J, Xhaard H, Goldman A. Asymmetry in catalysis by membrane-bound pyrophosphatase demonstrated by a nonphosphorus allosteric inhibitor. Science Advances. 5: eaav7574. PMID 31131322 DOI: 10.1126/sciadv.aav7574  0.48
2018 Liu Y, Kaljunen H, Pavić A, Saarenpää T, Himanen JP, Nikolov DB, Goldman A. Binding of EphrinA5 to RET receptor tyrosine kinase: An in vitro study. Plos One. 13: e0198291. PMID 29889908 DOI: 10.1371/journal.pone.0198291  0.56
2017 Kolodziejczyk R, Mikula KM, Kotila T, Postis VLG, Jokiranta TS, Goldman A, Meri T. Crystal structure of a tripartite complex between C3dg, C-terminal domains of factor H and OspE of Borrelia burgdorferi. Plos One. 12: e0188127. PMID 29190743 DOI: 10.1371/journal.pone.0188127  0.48
2017 Saarenpää T, Kogan K, Sidorova Y, Mahato AK, Tascón I, Kaljunen H, Yu L, Kallijärvi J, Jurvansuu J, Saarma M, Goldman A. Zebrafish GDNF and its co-receptor GFRα1 activate the human RET receptor and promote the survival of dopaminergic neurons in vitro. Plos One. 12: e0176166. PMID 28467503 DOI: 10.1371/journal.pone.0176166  0.56
2016 Li KM, Wilkinson C, Kellosalo J, Tsai JY, Kajander T, Jeuken LJ, Sun YJ, Goldman A. Membrane pyrophosphatases from Thermotoga maritima and Vigna radiata suggest a conserved coupling mechanism. Nature Communications. 7: 13596. PMID 27922000 DOI: 10.1038/ncomms13596  0.52
2016 Goldman A, Boije af Gennis G, Xhaard H, Meri S, Yli-Kauhaluoma J. [Pyrophosphate in medicine]. Duodecim; Laaketieteellinen Aikakauskirja. 132: 1111-7. PMID 27483627  0.48
2015 Rosti K, Goldman A, Kajander T. Solution structure and biophysical characterization of the multifaceted signalling effector protein growth arrest specific-1. Bmc Biochemistry. 16: 8. PMID 25888394 DOI: 10.1186/s12858-015-0037-6  0.52
2015 Saarenpää T, Jaakola VP, Goldman A. Baculovirus-mediated expression of GPCRs in insect cells. Methods in Enzymology. 556: 185-218. PMID 25857783 DOI: 10.1016/bs.mie.2014.12.033  0.56
2015 Bhattacharjee A, Reuter S, Trojnár E, Kolodziejczyk R, Seeberger H, Hyvärinen S, Uzonyi B, Szilágyi Á, Prohászka Z, Goldman A, Józsi M, Jokiranta TS. The major autoantibody epitope on factor H in atypical hemolytic uremic syndrome is structurally different from its homologous site in factor H-related protein 1, supporting a novel model for induction of autoimmunity in this disease. The Journal of Biological Chemistry. 290: 9500-10. PMID 25659429 DOI: 10.1074/jbc.M114.630871  0.56
2014 Repo H, Kuokkanen E, Oksanen E, Goldman A, Heikinheimo P. Is the bovine lysosomal phospholipase B-like protein an amidase? Proteins. 82: 300-11. PMID 23934913 DOI: 10.1002/prot.24388  0.4
2013 Happonen LJ, Oksanen E, Liljeroos L, Goldman A, Kajander T, Butcher SJ. The structure of the NTPase that powers DNA packaging into Sulfolobus turreted icosahedral virus 2. Journal of Virology. 87: 8388-98. PMID 23698307 DOI: 10.1128/JVI.00831-13  0.56
2013 Kajander T, Kellosalo J, Goldman A. Inorganic pyrophosphatases: one substrate, three mechanisms. Febs Letters. 587: 1863-9. PMID 23684653 DOI: 10.1016/j.febslet.2013.05.003  0.52
2013 Bhattacharjee A, Oeemig JS, Kolodziejczyk R, Meri T, Kajander T, Lehtinen MJ, Iwaï H, Jokiranta TS, Goldman A. Structural basis for complement evasion by Lyme disease pathogen Borrelia burgdorferi. The Journal of Biological Chemistry. 288: 18685-95. PMID 23658013 DOI: 10.1074/jbc.M113.459040  0.52
2013 Kellosalo J, Kajander T, Honkanen R, Goldman A. Crystallization and preliminary X-ray analysis of membrane-bound pyrophosphatases. Molecular Membrane Biology. 30: 64-74. PMID 22881431 DOI: 10.3109/09687688.2012.712162  0.52
2012 Kellosalo J, Kajander T, Kogan K, Pokharel K, Goldman A. The structure and catalytic cycle of a sodium-pumping pyrophosphatase. Science (New York, N.Y.). 337: 473-6. PMID 22837527 DOI: 10.1126/science.1222505  0.52
2011 Kajander T, Kuja-Panula J, Rauvala H, Goldman A. Crystal structure and role of glycans and dimerization in folding of neuronal leucine-rich repeat protein AMIGO-1. Journal of Molecular Biology. 413: 1001-15. PMID 21983541 DOI: 10.1016/j.jmb.2011.09.032  0.52
2011 Leo JC, Lyskowski A, Hattula K, Hartmann MD, Schwarz H, Butcher SJ, Linke D, Lupas AN, Goldman A. The structure of E. coli IgG-binding protein D suggests a general model for bending and binding in trimeric autotransporter adhesins. Structure (London, England : 1993). 19: 1021-30. PMID 21742268 DOI: 10.1016/j.str.2011.03.021  0.56
2011 Lyskowski A, Oeemig JS, Jaakkonen A, Rommi K, DiMaio F, Zhou D, Kajander T, Baker D, Wlodawer A, Goldman A, Iwaï H. Cloning, expression, purification, crystallization and preliminary X-ray diffraction data of the Pyrococcus horikoshii RadA intein. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 623-6. PMID 21543876 DOI: 10.1107/S1744309111008372  0.56
2011 Kajander T, Lehtinen MJ, Hyvärinen S, Bhattacharjee A, Leung E, Isenman DE, Meri S, Goldman A, Jokiranta TS. Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement. Proceedings of the National Academy of Sciences of the United States of America. 108: 2897-902. PMID 21285368 DOI: 10.1073/pnas.1017087108  0.52
2011 Kaila VRI, Oksanen E, Goldman A, Bloch DA, Verkhovsky MI, Sundholm D, Wikström M. A combined quantum chemical and crystallographic study on the oxidized binuclear center of cytochrome c oxidase Biochimica Et Biophysica Acta - Bioenergetics. 1807: 769-778. PMID 21211513 DOI: 10.1016/j.bbabio.2010.12.016  0.52
2010 Bhattacharjee A, Lehtinen MJ, Kajander T, Goldman A, Jokiranta TS. Both domain 19 and domain 20 of factor H are involved in binding to complement C3b and C3d. Molecular Immunology. 47: 1686-91. PMID 20378178 DOI: 10.1016/j.molimm.2010.03.007  0.52
2010 Ora A, Oksanen E, Kajander T, Goldman A, Butcher SJ. Crystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66: 357-60. PMID 20208180 DOI: 10.1107/S1744309110003684  0.56
2010 Leppänen VM, Prota AE, Jeltsch M, Anisimov A, Kalkkinen N, Strandin T, Lankinen H, Goldman A, Ballmer-Hofer K, Alitalo K. Structural determinants of growth factor binding and specificity by VEGF receptor 2 Proceedings of the National Academy of Sciences of the United States of America. 107: 2425-2430. PMID 20145116 DOI: 10.1073/pnas.0914318107  0.56
2010 Steitz TA, Goldman A, Engelman DM. Quantitative application of the helical hairpin hypothesis to membrane proteins. Biophysical Journal. 37: 124-5. PMID 19431438 DOI: 10.1016/S0006-3495(82)84633-X  0.6
2009 Kajander T, Sachs JN, Goldman A, Regan L. Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering. The Journal of Biological Chemistry. 284: 25364-74. PMID 19586912 DOI: 10.1074/jbc.M109.033894  0.56
2009 Parkash V, Lindholm P, Peränen J, Kalkkinen N, Oksanen E, Saarma M, Leppänen VM, Goldman A. The structure of the conserved neurotrophic factors MANF and CDNF explains why they are bifunctional. Protein Engineering, Design & Selection : Peds. 22: 233-41. PMID 19258449 DOI: 10.1093/protein/gzn080  0.36
2008 Parkash V, Leppänen VM, Virtanen H, Jurvansuu JM, Bespalov MM, Sidorova YA, Runeberg-Roos P, Saarma M, Goldman A. The structure of the glial cell line-derived neurotrophic factor-coreceptor complex: insights into RET signaling and heparin binding. The Journal of Biological Chemistry. 283: 35164-72. PMID 18845535 DOI: 10.1074/jbc.M802543200  0.36
2008 Xiong Y, Patana AS, Miley MJ, Zielinska AK, Bratton SM, Miller GP, Goldman A, Finel M, Redinbo MR, Radominska-Pandya A. The first aspartic acid of the DQxD motif for human UDP-glucuronosyltransferase 1A10 interacts with UDP-glucuronic acid during catalysis. Drug Metabolism and Disposition: the Biological Fate of Chemicals. 36: 517-22. PMID 18048489 DOI: 10.1124/dmd.107.016469  0.56
2007 Leppänen VM, Tossavainen H, Permi P, Lehtiö L, Rönnholm G, Goldman A, Kilpelaïnen I, Pihlajamaa T. Crystal structure of the N-terminal NC4 domain of collagen IX, a zinc binding member of the laminin-neurexin-sex hormone binding globulin (LNS) domain family. The Journal of Biological Chemistry. 282: 23219-30. PMID 17553797 DOI: 10.1074/jbc.M702514200  0.56
2007 Rantanen MK, Lehtiö L, Rajagopal L, Rubens CE, Goldman A. Structure of Streptococcus agalactiae serine/threonine phosphatase: The subdomain conformation is coupled to the binding of a third metal ion Febs Journal. 274: 3128-3137. PMID 17521332 DOI: 10.1111/j.1742-4658.2007.05845.x  0.52
2007 Rantanen MK, Lehtiö L, Rajagopal L, Rubens CE, Goldman A. Structure of the Streptococcus agalactiae family II inorganic pyrophosphatase at 2.80 Å resolution Acta Crystallographica Section D: Biological Crystallography. 63: 738-743. PMID 17505113 DOI: 10.1107/S0907444907019695  0.56
2007 Oksanen E, Ahonen AK, Tuominen H, Tuominen V, Lahti R, Goldman A, Heikinheimo P. A complete structural description of the catalytic cycle of yeast pyrophosphatase. Biochemistry. 46: 1228-39. PMID 17260952 DOI: 10.1021/bi0619977  0.4
2007 Fabrichniy IP, Lehtiö L, Tammenkoski M, Zyryanov AB, Oksanen E, Baykov AA, Lahti R, Goldman A. A trimetal site and substrate distortion in a family II inorganic pyrophosphatase. The Journal of Biological Chemistry. 282: 1422-31. PMID 17095506 DOI: 10.1074/jbc.M513161200  0.56
2006 Oksanen E, Jaakola VP, Tolonen T, Valkonen K, Akerström B, Kalkkinen N, Virtanen V, Goldman A. Reindeer beta-lactoglobulin crystal structure with pseudo-body-centred noncrystallographic symmetry. Acta Crystallographica. Section D, Biological Crystallography. 62: 1369-74. PMID 17057340 DOI: 10.1107/S0907444906031519  0.56
2006 Rantanen MK, Lehtiö L, Rajagopal L, Rubens CE, Goldman A. Crystallization and preliminary crystallographic analysis of two Streptococcus agalactiae proteins: The family II inorganic pyrophosphatase and the serine/threonine phosphatase Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 62: 891-894. PMID 16946472 DOI: 10.1107/S174430910602954X  0.56
2006 Jokiranta TS, Jaakola VP, Lehtinen MJ, Pärepalo M, Meri S, Goldman A. Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome. The Embo Journal. 25: 1784-94. PMID 16601698 DOI: 10.1038/sj.emboj.7601052  0.56
2006 Lehtiö L, Grossmann JG, Kokona B, Fairman R, Goldman A. Crystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus. Journal of Molecular Biology. 357: 221-35. PMID 16414072 DOI: 10.1016/j.jmb.2005.12.049  0.56
2005 Jaakola VP, Vainio M, Sen S, Rehn M, Heimo H, Scheinin M, Goldman A. Intracellularly truncated human alpha2B-adrenoceptors: stable and functional GPCRs for structural studies. Journal of Receptor and Signal Transduction Research. 25: 99-124. PMID 16149769 DOI: 10.1081/RRS-200068745  0.56
2005 Jaakola VP, Rehn M, Moeller M, Alexiev U, Goldman A, Turner GJ. G-protein-coupled receptor domain overexpression in Halobacterium salinarum: long-range transmembrane interactions in heptahelical membrane proteins. Proteins. 60: 412-23. PMID 15971205 DOI: 10.1002/prot.20498  0.56
2005 Sen S, Jaakola VP, Pirilä P, Finel M, Goldman A. Functional studies with membrane-bound and detergent-solubilized alpha2-adrenergic receptors expressed in Sf9 cells. Biochimica Et Biophysica Acta. 1712: 62-70. PMID 15893292 DOI: 10.1016/j.bbamem.2005.03.014  0.56
2005 Jaakola VP, Prilusky J, Sussman JL, Goldman A. G protein-coupled receptors show unusual patterns of intrinsic unfolding. Protein Engineering, Design & Selection : Peds. 18: 103-10. PMID 15790574 DOI: 10.1093/protein/gzi004  0.56
2005 Lehtiö L, Fabrichniy I, Hansen T, Schönheit P, Goldman A. Unusual twinning in an acetyl coenzyme A synthetase (ADP-forming) from Pyrococcus furiosus. Acta Crystallographica. Section D, Biological Crystallography. 61: 350-4. PMID 15735347 DOI: 10.1107/S0907444904034389  0.56
2005 Virtanen H, Yang J, Bespalov MM, Hiltunen JO, Leppänen VM, Kalkkinen N, Goldman A, Saarma M, Runeberg-Roos P. The first cysteine-rich domain of the receptor GFRalpha1 stabilizes the binding of GDNF. The Biochemical Journal. 387: 817-24. PMID 15610063 DOI: 10.1042/BJ20041257  0.36
2004 Fabrichniy IP, Lehtiö L, Salminen A, Zyryanov AB, Baykov AA, Lahti R, Goldman A. Structural studies of metal ions in family II pyrophosphatases: the requirement for a Janus ion. Biochemistry. 43: 14403-11. PMID 15533045 DOI: 10.1021/bi0484973  0.56
2004 Leppänen VM, Bespalov MM, Runeberg-Roos P, Puurand U, Merits A, Saarma M, Goldman A. The structure of GFRalpha1 domain 3 reveals new insights into GDNF binding and RET activation. The Embo Journal. 23: 1452-62. PMID 15044950 DOI: 10.1038/sj.emboj.7600174  0.36
2004 Tuominen VU, Myles DA, Dauvergne MT, Lahti R, Heikinheimo P, Goldman A. Production and preliminary analysis of perdeuterated yeast inorganic pyrophosphatase crystals suitable for neutron diffraction. Acta Crystallographica. Section D, Biological Crystallography. 60: 606-9. PMID 14993708 DOI: 10.1107/S0907444903029585  0.4
2003 Sen S, Jaakola VP, Heimo H, Engström M, Larjomaa P, Scheinin M, Lundstrom K, Goldman A. Functional expression and direct visualization of the human alpha 2B -adrenergic receptor and alpha 2B -AR-green fluorescent fusion protein in mammalian cell using Semliki Forest virus vectors. Protein Expression and Purification. 32: 265-75. PMID 14965773 DOI: 10.1016/j.pep.2003.08.006  0.56
2003 Kajander T, Lehtiö L, Schlömann M, Goldman A. The structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-evolution of structure and dynamics with the dehalogenation function. Protein Science : a Publication of the Protein Society. 12: 1855-64. PMID 12930985 DOI: 10.1110/ps.0388503  0.56
2003 Bartus CL, Jaakola VP, Reusch R, Valentine HH, Heikinheimo P, Levay A, Potter LT, Heimo H, Goldman A, Turner GJ. Downstream coding region determinants of bacterio-opsin, muscarinic acetylcholine receptor and adrenergic receptor expression in Halobacterium salinarum. Biochimica Et Biophysica Acta. 1610: 109-23. PMID 12586385 DOI: 10.1016/S0005-2736(02)00710-1  0.56
2002 Lehtiö L, Leppänen VM, Kozarich JW, Goldman A. Structure of Escherichia coli pyruvate formate-lyase with pyruvate. Acta Crystallographica. Section D, Biological Crystallography. 58: 2209-12. PMID 12454503  0.56
2002 Halonen P, Baykov AA, Goldman A, Lahti R, Cooperman BS. Single-turnover kinetics of Saccharomyces cerevisiae inorganic pyrophosphatase. Biochemistry. 41: 12025-31. PMID 12356302 DOI: 10.1021/bi026018z  0.56
2002 Merckel MC, Kajander T, Deacon AM, Thompson A, Grossmann JG, Kalkkinen N, Goldman A. 3-Carboxy-cis,cis-muconate lactonizing enzyme from Neurospora crassa: MAD phasing with 80 selenomethionines Acta Crystallographica Section D: Biological Crystallography. 58: 727-734. PMID 11976482 DOI: 10.1107/S0907444902002652  0.56
2002 Kajander T, Merckel MC, Thompson A, Deacon AM, Mazur P, Kozarich JW, Goldman A. The structure of Neurospora crassa 3-carboxy-cis,cis-muconate lactonizing enzyme, a beta propeller cycloisomerase. Structure (London, England : 1993). 10: 483-92. PMID 11937053 DOI: 10.1016/S0969-2126(02)00744-X  0.56
2001 Heikinheimo P, Tuominen V, Ahonen AK, Teplyakov A, Cooperman BS, Baykov AA, Lahti R, Goldman A. Toward a quantum-mechanical description of metal-assisted phosphoryl transfer in pyrophosphatase. Proceedings of the National Academy of Sciences of the United States of America. 98: 3121-6. PMID 11248042 DOI: 10.1073/pnas.061612498  0.4
2001 Kajander T, Kahn PC, Passila SH, Cohen DC, Lehtiö L, Adolfsen W, Warwicker J, Schell U, Goldman A. Buried charged surface in proteins. Structure (London, England : 1993). 8: 1203-14. PMID 11080642 DOI: 10.1016/S0969-2126(00)00520-7  0.52
2000 Kapat A, Jaakola VP, Heimo H, Liitti S, Heikinheimo P, Glumoff T, Goldman A. Production and purification of recombinant human alpha 2C2 adrenergic receptor using Saccharomyces cerevisiae. Bioseparation. 9: 167-72. PMID 11105246 DOI: 10.1023/A:1008150412294  0.56
1999 Leppänen VM, Nummelin H, Hansen T, Lahti R, Schäfer G, Goldman A. Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase. Protein Science : a Publication of the Protein Society. 8: 1218-31. PMID 10386872 DOI: 10.1110/ps.8.6.1218  0.44
1999 Schell U, Helin S, Kajander T, Schlömann M, Goldman A. Structural basis for the activity of two muconate cycloisomerase variants toward substituted muconates. Proteins. 34: 125-36. PMID 10336378 DOI: 10.1002/(SICI)1097-0134(19990101)34:1<125::AID-PROT10>3.0.CO;2-Y  0.36
1999 Hansen T, Urbanke C, Leppänen VM, Goldman A, Brandenburg K, Schäfer G. The extreme thermostable pyrophosphatase from Sulfolobus acidocaldarius: enzymatic and comparative biophysical characterization. Archives of Biochemistry and Biophysics. 363: 135-47. PMID 10049508 DOI: 10.1006/abbi.1998.1072  0.44
1998 Tuominen V, Heikinheimo P, Kajander T, Torkkel T, Hyytiä T, Käpylä J, Lahti R, Cooperman BS, Goldman A. The R78K and D117E active-site variants of Saccharomyces cerevisiae soluble inorganic pyrophosphatase: structural studies and mechanistic implications. Journal of Molecular Biology. 284: 1565-80. PMID 9878371 DOI: 10.1006/jmbi.1998.2266  0.52
1997 Fabrichniy IP, Kasho VN, Hyytiä T, Salminen T, Halonen P, Dudarenkov VY, Heikinheimo P, Chernyak VY, Goldman A, Lahti R, Cooperman BS, Baykov AA. Structural and functional consequences of substitutions at the tyrosine 55-lysine 104 hydrogen bond in Escherichia coli inorganic pyrophosphatase. Biochemistry. 36: 7746-53. PMID 9201916 DOI: 10.1021/bi9629844  0.4
1996 Heikinheimo P, Lehtonen J, Baykov A, Lahti R, Cooperman BS, Goldman A. The structural basis for pyrophosphatase catalysis. Structure (London, England : 1993). 4: 1491-508. PMID 8994974  0.4
1996 Heikinheimo P, Pohjanjoki P, Helminen A, Tasanen M, Cooperman BS, Goldman A, Baykov A, Lahti R. A site-directed mutagenesis study of Saccharomyces cerevisiae pyrophosphatase. Functional conservation of the active site of soluble inorganic pyrophosphatases European Journal of Biochemistry. 239: 138-143. PMID 8706698 DOI: 10.1111/j.1432-1033.1996.0138u.x  0.4
1996 Volk SE, Dudarenkov VY, Käpylä J, Kasho VN, Voloshina OA, Salminen T, Goldman A, Lahti R, Baykov AA, Cooperman BS. Effect of E20D substitution in the active site of Escherichia coli inorganic pyrophosphatase on its quaternary structure and catalytic properties. Biochemistry. 35: 4662-9. PMID 8664255 DOI: 10.1021/bi952636m  0.56
1996 Baykov AA, Hyytia T, Volk SE, Kasho VN, Vener AV, Goldman A, Lahti R, Cooperman BS. Catalysis by Escherichia coli inorganic pyrophosphatase: pH and Mg2+ dependence. Biochemistry. 35: 4655-61. PMID 8664254 DOI: 10.1021/bi952635u  0.56
1995 Velichko IS, Volk SE, Dudarenkov VYu, Magretova NN, Chernyak VYa, Goldman A, Cooperman BS, Lahti R, Baykov AA, Velichko IV. Cold lability of the mutant forms of Escherichia coli inorganic pyrophosphatase. Febs Letters. 359: 20-2. PMID 7851523 DOI: 10.1016/0014-5793(95)00003-R  0.56
1995 Heikinheimo P, Salminen T, Lahti R, Cooperman B, Goldman A. New crystal forms of Escherichia coli and Saccharomyces cerevisiae soluble inorganic pyrophosphatases Acta Crystallographica - Section D Biological Crystallography. 51: 399-401. DOI: 10.1107/S0907444994010784  0.4
1994 Kankare J, Neal GS, Salminen T, Glumoff T, Cooperman BS, Lahti R, Goldman A. The structure of E.coli soluble inorganic pyrophosphatase at 2.7 å resolution Protein Engineering, Design and Selection. 7: 1173. DOI: 10.1093/protein/7.9.1173  0.4
1993 Camacho NP, Smith DR, Goldman A, Schneider B, Green D, Young PR, Berman HM. Structure of an interleukin-1β mutant with reduced bioactivity shows multiple subtle changes in conformation that affect protein-protein recognition Biochemistry. 32: 8749-8757. PMID 8364024 DOI: 10.1021/BI00085A005  0.56
1990 Sanderson MR, Freemont PS, Rice PA, Goldman A, Hatfull GF, Grindley ND, Steitz TA. The crystal structure of the catalytic domain of the site-specific recombination enzyme gamma delta resolvase at 2.7 A resolution. Cell. 63: 1323-9. PMID 2175678 DOI: 10.1016/0092-8674(90)90427-G  0.56
1987 Goldman A, Ollis DL, Steitz TA. Crystal structure of muconate lactonizing enzyme at 3 A resolution. Journal of Molecular Biology. 194: 143-53. PMID 3612800 DOI: 10.1016/0022-2836(87)90723-6  0.6
1985 Goldman A, Ollis D, Ngai KL, Steitz TA. Crystal structure of muconate lactonizing enzyme at 6.5 A resolution. Journal of Molecular Biology. 182: 353-5. PMID 3999146 DOI: 10.1016/0022-2836(85)90352-3  0.6
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