3gpd › Citations

Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase.

Mercer WD, Winn SI, Watson HC
J Mol Biol 104 277-83 (1976)
Cited: 51 times
EuropePMC logo PMID: 957435

Articles - 3gpd mentioned but not cited (8)

  1. Conserved and host-specific features of influenza virion architecture. Hutchinson EC, Charles PD, Hester SS, Thomas B, Trudgian D, Martínez-Alonso M, Fodor E. Nat Commun 5 4816 (2014)
  2. Intron positions correlate with module boundaries in ancient proteins. de Souza SJ, Long M, Schoenbach L, Roy SW, Gilbert W. Proc Natl Acad Sci U S A 93 14632-14636 (1996)
  3. Exploring key orientations at protein-protein interfaces with small molecule probes. Ko E, Raghuraman A, Perez LM, Ioerger TR, Burgess K. J Am Chem Soc 135 167-173 (2013)
  4. Ionic strength dependence of F-actin and glycolytic enzyme associations: a Brownian dynamics simulations approach. Forlemu NY, Njabon EN, Carlson KL, Schmidt ES, Waingeh VF, Thomasson KA. Proteins 79 2813-2827 (2011)
  5. Combined Methylome and Transcriptome Analyses Reveals Potential Therapeutic Targets for EGFR Wild Type Lung Cancers with Low PD-L1 Expression. Hu W, Wang G, Yarmus LB, Wan Y. Cancers (Basel) 12 E2496 (2020)
  6. Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Ayres CA, Schormann N, Senkovich O, Fry A, Banerjee S, Ulett GC, Chattopadhyay D. Acta Crystallogr F Struct Biol Commun 70 1333-1339 (2014)
  7. Partial catalytic Cys oxidation of human GAPDH to Cys-sulfonic acid. Lia A, Dowle A, Taylor C, Santino A, Roversi P. Wellcome Open Res 5 114 (2020)
  8. Size of the protein-protein energy funnel in crowded environment. Jenkins NW, Kundrotas PJ, Vakser IA. Front Mol Biosci 9 1031225 (2022)


Reviews citing this publication (5)

  1. Molecular mechanisms and potential clinical significance of S-glutathionylation. Dalle-Donne I, Milzani A, Gagliano N, Colombo R, Giustarini D, Rossi R. Antioxid. Redox Signal. 10 445-473 (2008)
  2. Glycolysis as a target for the design of new anti-trypanosome drugs. Verlinde CL, Hannaert V, Blonski C, Willson M, Périé JJ, Fothergill-Gilmore LA, Opperdoes FR, Gelb MH, Hol WG, Michels PA. Drug Resist. Updat. 4 50-65 (2001)
  3. Application of the Hard and Soft, Acids and Bases (HSAB) theory to toxicant--target interactions. Lopachin RM, Gavin T, Decaprio A, Barber DS. Chem. Res. Toxicol. 25 239-251 (2012)
  4. Protein crystallography and infectious diseases. Verlinde CL, Merritt EA, Van den Akker F, Kim H, Feil I, Delboni LF, Mande SC, Sarfaty S, Petra PH, Hol WG. Protein Sci. 3 1670-1686 (1994)
  5. Combining structural genomics and enzymology: completing the picture in metabolic pathways and enzyme active sites. Erlandsen H, Abola EE, Stevens RC. Curr. Opin. Struct. Biol. 10 719-730 (2000)

Articles citing this publication (38)

  1. Improvements in protein secondary structure prediction by an enhanced neural network. Kneller DG, Cohen FE, Langridge R. J. Mol. Biol. 214 171-182 (1990)
  2. Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Kim JR, Yoon HW, Kwon KS, Lee SR, Rhee SG. Anal. Biochem. 283 214-221 (2000)
  3. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 A resolution. Skarzyński T, Moody PC, Wonacott AJ. J. Mol. Biol. 193 171-187 (1987)
  4. Structure-based design of submicromolar, biologically active inhibitors of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase. Aronov AM, Suresh S, Buckner FS, Van Voorhis WC, Verlinde CL, Opperdoes FR, Hol WG, Gelb MH. Proc. Natl. Acad. Sci. U.S.A. 96 4273-4278 (1999)
  5. Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Skarzyński T, Wonacott AJ. J. Mol. Biol. 203 1097-1118 (1988)
  6. Molecular distances from dipolar coupled spin-labels: the global analysis of multifrequency continuous wave electron paramagnetic resonance data. Hustedt EJ, Smirnov AI, Laub CF, Cobb CE, Beth AH. Biophys. J. 72 1861-1877 (1997)
  7. Adenosine analogues as selective inhibitors of glyceraldehyde-3-phosphate dehydrogenase of Trypanosomatidae via structure-based drug design. Bressi JC, Verlinde CL, Aronov AM, Shaw ML, Shin SS, Nguyen LN, Suresh S, Buckner FS, Van Voorhis WC, Kuntz ID, Hol WG, Gelb MH. J. Med. Chem. 44 2080-2093 (2001)
  8. Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data. Vellieux FM, Hajdu J, Verlinde CL, Groendijk H, Read RJ, Greenhough TJ, Campbell JW, Kalk KH, Littlechild JA, Watson HC. Proc. Natl. Acad. Sci. U.S.A. 90 2355-2359 (1993)
  9. Structure of lobster apo-D-glyceraldehyde-3-phosphate dehydrogenase at 3.0 A resolution. Murthy MR, Garavito RM, Johnson JE, Rossmann MG. J. Mol. Biol. 138 859-872 (1980)
  10. Glycolytic enzyme interactions with yeast and skeletal muscle F-actin. Waingeh VF, Gustafson CD, Kozliak EI, Lowe SL, Knull HR, Thomasson KA. Biophys. J. 90 1371-1384 (2006)
  11. Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus. Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, Littlechild JA. J. Mol. Biol. 291 651-660 (1999)
  12. Molecular mechanism of glyceraldehyde-3-phosphate dehydrogenase inactivation by α,β-unsaturated carbonyl derivatives. Martyniuk CJ, Fang B, Koomen JM, Gavin T, Zhang L, Barber DS, Lopachin RM. Chem. Res. Toxicol. 24 2302-2311 (2011)
  13. Conformational changes in Leishmania mexicana glyceraldehyde-3-phosphate dehydrogenase induced by designed inhibitors. Suresh S, Bressi JC, Kennedy KJ, Verlinde CL, Gelb MH, Hol WG. J. Mol. Biol. 309 423-435 (2001)
  14. A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+. Didierjean C, Rahuel-Clermont S, Vitoux B, Dideberg O, Branlant G, Aubry A. J. Mol. Biol. 268 739-759 (1997)
  15. Crystal structure of the non-regulatory A(4 )isoform of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase complexed with NADP. Fermani S, Ripamonti A, Sabatino P, Zanotti G, Scagliarini S, Sparla F, Trost P, Pupillo P. J. Mol. Biol. 314 527-542 (2001)
  16. Identification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase. Orru S, Ruoppolo M, Francese S, Vitagliano L, Marino G, Esposito C. Protein Sci. 11 137-146 (2002)
  17. A helix-turn-strand structural motif common in alpha-beta proteins. Rice PA, Goldman A, Steitz TA. Proteins 8 334-340 (1990)
  18. Polymorphism in crystallin elongation factor Tu-GDP from Escherichia coli. Leberman R, Wittinghofer A, Schulz GE. J. Mol. Biol. 106 951-961 (1976)
  19. The crystal structure of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP(+) at 2.1 A resolution. Charron C, Talfournier F, Isupov MN, Littlechild JA, Branlant G, Vitoux B, Aubry A. J. Mol. Biol. 297 481-500 (2000)
  20. Interactions of glyceraldehyde-3-phosphate dehydrogenase with G- and F-actin predicted by Brownian dynamics. Ouporov IV, Knull HR, Lowe SL, Thomasson KA. J. Mol. Recognit. 14 29-41 (2001)
  21. Structure-activity relationships of novel inhibitors of glyceraldehyde-3-phosphate dehydrogenase. Leitão A, Andricopulo AD, Oliva G, Pupo MT, de Marchi AA, Vieira PC, da Silva MF, Ferreira VF, de Souza MC, Sá MM, Moraes VR, Montanari CA. Bioorg. Med. Chem. Lett. 14 2199-2204 (2004)
  22. Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS. Chaikuad A, Shafqat N, Al-Mokhtar R, Cameron G, Clarke AR, Brady RL, Oppermann U, Frayne J, Yue WW. Biochem. J. 435 401-409 (2011)
  23. Ligand binding energy and enzyme efficiency from reductions in protein dynamics. Williams DH, Zhou M, Stephens E. J. Mol. Biol. 355 760-767 (2006)
  24. Interaction between mammalian glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase from heart and muscle. Svedruzić ZM, Spivey HO. Proteins 63 501-511 (2006)
  25. Molecular symmetry of glyceraldehyde-3-phosphate dehydrogenase from Bacillus coagulans. Griffith JP, Lee B, Murdock AL, Amelunxen RE. J. Mol. Biol. 169 963-974 (1983)
  26. Autonomous folding of the excised coenzyme-binding domain of D-glyceraldehyde 3-phosphate dehydrogenase from Thermotoga maritima. Jecht M, Tomschy A, Kirschner K, Jaenicke R. Protein Sci. 3 411-418 (1994)
  27. Investigation of glyceraldehyde-3-phosphate dehydrogenase from human sperms. Shchutskaya YY, Elkina YL, Kuravsky ML, Bragina EE, Schmalhausen EV. Biochemistry Mosc. 73 185-191 (2008)
  28. Sevoflurane modulates the activity of glyceraldehyde 3-phosphate dehydrogenase. Swearengin TA, Fibuch EE, Seidler NW. J Enzyme Inhib Med Chem 21 575-579 (2006)
  29. Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor. Shen YQ, Li J, Song SY, Lin ZJ. J. Struct. Biol. 130 1-9 (2000)
  30. Biosynthesis of the fungal glyceraldehyde-3-phosphate dehydrogenase inhibitor heptelidic acid and mechanism of self-resistance. Yan Y, Zang X, Jamieson CS, Lin HC, Houk KN, Zhou J, Tang Y. Chem Sci 11 9554-9562 (2020)
  31. Crystallographic data for sturgeon holo-D-glyceraldehyde-3-phosphate dehydrogenase: a holo-D-glyceraldehyde-3-phosphate dehydrogenase with crystallographic 2-fold symmetry. Holmes MA, Remington SJ, Schwendimann B, Christie GE, Matthews BW. J. Mol. Biol. 112 651-652 (1977)
  32. Lack of asymmetry in the active sites of tetrameric D-glyceraldehyde-3-phosphate dehydrogenase during alkylation in the crystalline state. Halász P, Polgár L. FEBS Lett. 143 93-95 (1982)
  33. Feed-forward neural networks for secondary structure prediction. Barlow TW. J Mol Graph 13 175-183 (1995)
  34. Preliminary crystallographic data for glyceraldehyde-3-phosphate dehydrogenase from the thermophile Bacillus coagulans. Lee B, Griffith JP, Park CH, Sheldon RI, McLinden J, Murdock AL, Amelunxen RE. J. Mol. Biol. 158 153-156 (1982)
  35. Preliminary crystallographic studies of lobster D-glyceraldehyde-3-phosphate dehydrogenase and the modified enzyme carrying the fluorescent derivative. Song SY, Gao YG, Zhou JM, Tsou CL. J. Mol. Biol. 171 225-228 (1983)
  36. 4-Chloroacetylpyridine adenine dinucleotide. A highly reactive and chromophoric affinity label of glyceraldehyde-3-phosphate dehydrogenase from sturgeon. Tritsch D, Eiler-Samama B, Svircevic J, Albrecht AM, Branlant G, Biellmann JF. Eur. J. Biochem. 181 215-222 (1989)
  37. Efficient tagging of endogenous proteins in human cell lines for structural studies by single-particle cryo-EM. Choi W, Wu H, Yserentant K, Huang B, Cheng Y. Proc Natl Acad Sci U S A 120 e2302471120 (2023)
  38. Novel Structures of Type 1 Glyceraldehyde-3-phosphate Dehydrogenase from Escherichia coli Provide New Insights into the Mechanism of Generation of 1,3-Bisphosphoglyceric Acid. Zhang L, Liu M, Bao L, Boström KI, Yao Y, Li J, Gu S, Ji C. Biomolecules 11 1565 (2021)


Related citations provided by authors (2)

  1. Low resolution structure of glyceraldehyde 3-phosphate dehydrogenase.. Watson HC, Duée E, Mercer WD Nat New Biol 240 130-3 (1972)
  2. The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase.. Nowak K, Wolny M, Banaś T FEBS Lett 134 143-6 (1981)

Quick links