| Year |
Citation |
Score |
| 2014 |
Preiss J. Glycogen: Biosynthesis and Regulation. Ecosal Plus. 6. PMID 26442935 DOI: 10.1128/ecosalplus.ESP-0015-2014 |
0.409 |
|
| 2014 |
Preiss J. Glycogen Biosynthesis Reference Module in Biomedical Research. DOI: 10.1016/B978-0-12-801238-3.02439-9 |
0.31 |
|
| 2010 |
Petreikov M, Eisenstein M, Yeselson Y, Preiss J, Schaffer AA. Characterization of the AGPase large subunit isoforms from tomato indicates that the recombinant L3 subunit is active as a monomer. The Biochemical Journal. 428: 201-12. PMID 20236089 DOI: 10.1042/Bj20091777 |
0.452 |
|
| 2010 |
Iglesias AA, Kakefuda G, Preiss J. Regulatory and Structural Properties of the Cyanobacterial ADPglucose Pyrophosphorylases. Plant Physiology. 97: 1187-95. PMID 16668507 DOI: 10.1104/Pp.97.3.1187 |
0.551 |
|
| 2010 |
Kim WT, Franceschi VR, Okita TW, Robinson NL, Morell M, Preiss J. Immunocytochemical Localization of ADPglucose Pyrophosphorylase in Developing Potato Tuber Cells. Plant Physiology. 91: 217-20. PMID 16666999 DOI: 10.1104/Pp.91.1.217 |
0.608 |
|
| 2010 |
Lin TP, Preiss J. Characterization of d-Enzyme (4-alpha-Glucanotransferase) in Arabidopsis Leaf. Plant Physiology. 86: 260-5. PMID 16665877 DOI: 10.1104/Pp.86.1.260 |
0.503 |
|
| 2010 |
Morell MK, Bloom M, Knowles V, Preiss J. Subunit Structure of Spinach Leaf ADPglucose Pyrophosphorylase. Plant Physiology. 85: 182-7. PMID 16665654 DOI: 10.1104/Pp.85.1.182 |
0.469 |
|
| 2010 |
Plaxton WC, Preiss J. Purification and Properties of Nonproteolytic Degraded ADPglucose Pyrophosphorylase from Maize Endosperm. Plant Physiology. 83: 105-12. PMID 16665182 DOI: 10.1104/Pp.83.1.105 |
0.72 |
|
| 2010 |
Okita TW, Preiss J. Starch Degradation in Spinach Leaves: ISOLATION AND CHARACTERIZATION OF THE AMYLASES AND R-ENZYME OF SPINACH LEAVES. Plant Physiology. 66: 870-6. PMID 16661544 DOI: 10.1104/Pp.66.5.870 |
0.682 |
|
| 2010 |
Preiss J, Okita TW, Greenberg E. Characterization of the spinach leaf phosphorylases. Plant Physiology. 66: 864-9. PMID 16661543 DOI: 10.1104/Pp.66.5.864 |
0.653 |
|
| 2010 |
Okita TW, Greenberg E, Kuhn DN, Preiss J. Subcellular localization of the starch degradative and biosynthetic enzymes of spinach leaves. Plant Physiology. 64: 187-92. PMID 16660929 DOI: 10.1104/Pp.64.2.187 |
0.715 |
|
| 2009 |
Preiss J. Glycogen: Biosynthesis and Regulation. Ecosal Plus. 3. PMID 26443753 DOI: 10.1128/ecosalplus.4.7.4 |
0.428 |
|
| 2009 |
Sheng F, Yep A, Feng L, Preiss J, Geiger JH. Oligosaccharide binding in Escherichia coli glycogen synthase. Biochemistry. 48: 10089-97. PMID 19761218 DOI: 10.1021/Bi900916T |
0.506 |
|
| 2009 |
Sheng F, Jia X, Yep A, Preiss J, Geiger JH. The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase. The Journal of Biological Chemistry. 284: 17796-807. PMID 19244233 DOI: 10.1074/Jbc.M809804200 |
0.515 |
|
| 2008 |
Ventriglia T, Kuhn ML, Ruiz MT, Ribeiro-Pedro M, Valverde F, Ballicora MA, Preiss J, Romero JM. Two Arabidopsis ADP-glucose pyrophosphorylase large subunits (APL1 and APL2) are catalytic. Plant Physiology. 148: 65-76. PMID 18614708 DOI: 10.1104/Pp.108.122846 |
0.826 |
|
| 2007 |
Ballicora MA, Erben ED, Yazaki T, Bertolo AL, Demonte AM, Schmidt JR, Aleanzi M, Bejar CM, Figueroa CM, Fusari CM, Iglesias AA, Preiss J. Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis. Journal of Bacteriology. 189: 5325-33. PMID 17496097 DOI: 10.1128/Jb.00481-07 |
0.847 |
|
| 2007 |
Ventriglia T, Ballicora MA, Crevillén P, Preiss J, Romero JM. Regulatory properties of potato-Arabidopsis hybrid ADP-glucose pyrophosphorylase. Plant & Cell Physiology. 48: 875-80. PMID 17452341 DOI: 10.1093/Pcp/Pcm047 |
0.729 |
|
| 2006 |
Bejar CM, Jin X, Ballicora MA, Preiss J. Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases. The Journal of Biological Chemistry. 281: 40473-84. PMID 17079236 DOI: 10.1074/Jbc.M607088200 |
0.822 |
|
| 2006 |
Yep A, Ballicora MA, Preiss J. The ADP-glucose binding site of the Escherichia coli glycogen synthase. Archives of Biochemistry and Biophysics. 453: 188-96. PMID 16919233 DOI: 10.1016/J.Abb.2006.07.003 |
0.761 |
|
| 2006 |
Bejar CM, Ballicora MA, Iglesias AA, Preiss J. ADPglucose pyrophosphorylase's N-terminus: structural role in allosteric regulation. Biochemical and Biophysical Research Communications. 343: 216-21. PMID 16530732 DOI: 10.1016/J.Bbrc.2006.02.123 |
0.808 |
|
| 2006 |
Iglesias AA, Ballicora MA, Sesma JI, Preiss J. Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase. Plant & Cell Physiology. 47: 523-30. PMID 16501256 DOI: 10.1093/Pcp/Pcj021 |
0.778 |
|
| 2005 |
Jin X, Ballicora MA, Preiss J, Geiger JH. Crystal structure of potato tuber ADP-glucose pyrophosphorylase. The Embo Journal. 24: 694-704. PMID 15692569 DOI: 10.1038/Sj.Emboj.7600551 |
0.764 |
|
| 2005 |
Ballicora MA, Dubay JR, Devillers CH, Preiss J. Resurrecting the ancestral enzymatic role of a modulatory subunit. The Journal of Biological Chemistry. 280: 10189-95. PMID 15632142 DOI: 10.1074/Jbc.M413540200 |
0.746 |
|
| 2004 |
Ballicora MA, Iglesias AA, Preiss J. ADP-Glucose Pyrophosphorylase: A Regulatory Enzyme for Plant Starch Synthesis. Photosynthesis Research. 79: 1-24. PMID 16228397 DOI: 10.1023/B:Pres.0000011916.67519.58 |
0.773 |
|
| 2004 |
Bejar CM, Ballicora MA, Gómez-Casati DF, Iglesias AA, Preiss J. The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains. Febs Letters. 573: 99-104. PMID 15327982 DOI: 10.1016/J.Febslet.2004.07.060 |
0.815 |
|
| 2004 |
Yep A, Ballicora MA, Preiss J. The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases. Biochemical and Biophysical Research Communications. 316: 960-6. PMID 15033495 DOI: 10.1016/J.Bbrc.2004.02.136 |
0.707 |
|
| 2004 |
Yep A, Ballicora MA, Sivak MN, Preiss J. Identification and characterization of a critical region in the glycogen synthase from Escherichia coli. The Journal of Biological Chemistry. 279: 8359-67. PMID 14665620 DOI: 10.1074/Jbc.M312686200 |
0.762 |
|
| 2004 |
Yep A, Bejar CM, Ballicora MA, Dubay JR, Iglesias AA, Preiss J. An assay for adenosine 5'-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase. Analytical Biochemistry. 324: 52-9. PMID 14654045 DOI: 10.1016/J.Ab.2003.09.024 |
0.801 |
|
| 2004 |
Sakulsingharoj C, Choi SB, Hwang SK, Edwards GE, Bork J, Meyer CR, Preiss J, Okita TW. Engineering starch biosynthesis for increasing rice seed weight: The role of the cytoplasmic ADP-glucose pyrophosphorylase Plant Science. 167: 1323-1333. DOI: 10.1016/J.Plantsci.2004.06.028 |
0.815 |
|
| 2004 |
Devillers CH, Piper ME, Ballicora MA, Preiss J. Erratum to “Characterization of the branching patterns of glycogen branching enzyme truncated on the N-terminus” [Arch. Biochem. Biophys. 418 (2003) 34–38] Archives of Biochemistry and Biophysics. 421: 290. DOI: 10.1016/J.Abb.2003.10.015 |
0.703 |
|
| 2003 |
Devillers CH, Piper ME, Ballicora MA, Preiss J. Characterization of the branching patterns of glycogen branching enzyme truncated on the N-terminus. Archives of Biochemistry and Biophysics. 418: 34-8. PMID 13679080 DOI: 10.1016/S0003-9861(03)00341-2 |
0.702 |
|
| 2003 |
Ballicora MA, Iglesias AA, Preiss J. ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis. Microbiology and Molecular Biology Reviews : Mmbr. 67: 213-25, table of con. PMID 12794190 DOI: 10.1128/Mmbr.67.2.213-225.2003 |
0.751 |
|
| 2003 |
Crevillén P, Ballicora MA, Mérida A, Preiss J, Romero JM. The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme. The Journal of Biological Chemistry. 278: 28508-15. PMID 12748181 DOI: 10.1074/Jbc.M304280200 |
0.758 |
|
| 2003 |
Frueauf JB, Ballicora MA, Preiss J. ADP-glucose pyrophosphorylase from potato tuber: site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits. The Plant Journal : For Cell and Molecular Biology. 33: 503-11. PMID 12581308 DOI: 10.1046/J.1365-313X.2003.01643.X |
0.774 |
|
| 2002 |
Abad MC, Binderup K, Rios-Steiner J, Arni RK, Preiss J, Geiger JH. The X-ray crystallographic structure of Escherichia coli branching enzyme. The Journal of Biological Chemistry. 277: 42164-70. PMID 12196524 DOI: 10.1074/Jbc.M205746200 |
0.845 |
|
| 2002 |
Ballicora MA, Sesma JI, Iglesias AA, Preiss J. Characterization of chimeric ADPglucose pyrophosphorylases of Escherichia coli and Agrobacterium tumefaciens. Importance of the C-terminus on the selectivity for allosteric regulators. Biochemistry. 41: 9431-7. PMID 12135365 DOI: 10.1021/Bi025793B |
0.785 |
|
| 2002 |
Frueauf JB, Ballicora MA, Preiss J. Alteration of inhibitor selectivity by site-directed mutagenesis of Arg(294) in the ADP-glucose pyrophosphorylase from Anabaena PCC 7120. Archives of Biochemistry and Biophysics. 400: 208-14. PMID 12054431 DOI: 10.1016/S0003-9861(02)00015-2 |
0.709 |
|
| 2002 |
Abad MC, Binderup K, Preiss J, Geiger JH. Crystallization and preliminary X-ray diffraction studies of Escherichia coli branching enzyme. Acta Crystallographica. Section D, Biological Crystallography. 58: 359-61. PMID 11807277 DOI: 10.1107/S090744490102073X |
0.81 |
|
| 2002 |
Binderup K, Mikkelsen R, Preiss J. Truncation of the amino terminus of branching enzyme changes its chain transfer pattern. Archives of Biochemistry and Biophysics. 397: 279-85. PMID 11795883 DOI: 10.1006/Abbi.2001.2544 |
0.836 |
|
| 2002 |
Preiss J. Glycogen Synthesis and its Regulation in Bacteria Biopolymers Online. DOI: 10.1002/3527600035.Bpol5002 |
0.457 |
|
| 2001 |
Frueauf JB, Ballicora MA, Preiss J. Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli. The Journal of Biological Chemistry. 276: 46319-25. PMID 11567027 DOI: 10.1074/Jbc.M107408200 |
0.744 |
|
| 2001 |
Mikkelsen R, Binderup K, Preiss J. Tyrosine residue 300 is important for activity and stability of branching enzyme from Escherichia coli. Archives of Biochemistry and Biophysics. 385: 372-7. PMID 11368019 DOI: 10.1006/Abbi.2000.2164 |
0.848 |
|
| 2001 |
Hong S, Mikkelsen R, Preiss J. Analysis of the amino terminus of maize branching enzyme II by polymerase chain reaction random mutagenesis. Archives of Biochemistry and Biophysics. 386: 62-8. PMID 11361001 DOI: 10.1006/Abbi.2000.2179 |
0.564 |
|
| 2001 |
Wu MX, Preiss J. Truncated forms of the recombinant Escherichia coli ADP-glucose pyrophosphorylase: the importance of the N-terminal region for allosteric activation and inhibition. Archives of Biochemistry and Biophysics. 389: 159-65. PMID 11339804 DOI: 10.1006/Abbi.2001.2327 |
0.591 |
|
| 2001 |
Zabawinski C, Van Den Koornhuyse N, D'Hulst C, Schlichting R, Giersch C, Delrue B, Lacroix JM, Preiss J, Ball S. Starchless mutants of Chlamydomonas reinhardtii lack the small subunit of a heterotetrameric ADP-glucose pyrophosphorylase. Journal of Bacteriology. 183: 1069-77. PMID 11208806 DOI: 10.1128/Jb.183.3.1069-1077.2001 |
0.57 |
|
| 2000 |
Gómez-Casati DF, Preiss J, Iglesias AA. Studies on the effect of temperature on the activity and stability of cyanobacterial ADP-glucose pyrophosphorylase. Archives of Biochemistry and Biophysics. 384: 319-26. PMID 11368319 DOI: 10.1006/Abbi.2000.2101 |
0.453 |
|
| 2000 |
Hong S, Preiss J. Localization of C-terminal domains required for the maximal activity or for determination of substrate preference of maize branching enzymes. Archives of Biochemistry and Biophysics. 378: 349-55. PMID 10860552 DOI: 10.1006/Abbi.2000.1845 |
0.508 |
|
| 2000 |
Binderup K, Mikkelsen R, Preiss J. Limited proteolysis of branching enzyme from Escherichia coli. Archives of Biochemistry and Biophysics. 377: 366-71. PMID 10845715 DOI: 10.1006/Abbi.2000.1815 |
0.853 |
|
| 2000 |
Binderup K, Watanabe L, Polikarpov I, Preiss J, Arni RK. Crystallization and preliminary X-ray diffraction analysis of the catalytic subunit of ADP-glucose pyrophosphorylase from potato tuber. Acta Crystallographica. Section D, Biological Crystallography. 56: 192-4. PMID 10666602 DOI: 10.1107/S0907444999015012 |
0.816 |
|
| 2000 |
Binderup K, Libessart N, Preiss J. Slow-binding inhibition of branching enzyme by the pseudooligosaccharide BAY e4609. Archives of Biochemistry and Biophysics. 374: 73-8. PMID 10640398 DOI: 10.1006/Abbi.1999.1580 |
0.826 |
|
| 2000 |
Ballicora MA, Frueauf JB, Fu Y, Schürmann P, Preiss J. Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin Journal of Biological Chemistry. 275: 1315-1320. PMID 10625679 DOI: 10.1074/Jbc.275.2.1315 |
0.742 |
|
| 1999 |
Ballicora MA, Fu Y, Frueauf JB, Preiss J. Heat stability of the potato tuber ADP-glucose pyrophosphorylase: Role of Cys residue 12 in the small subunit Biochemical and Biophysical Research Communications. 257: 782-786. PMID 10208860 DOI: 10.1006/Bbrc.1999.0469 |
0.751 |
|
| 1999 |
Cao H, Preiss J. Site-directed mutagenesis evidence for arginine-384 residue at the active site of maize branching enzyme ii Protein Journal. 18: 379-386. DOI: 10.1023/A:1021003915810 |
0.444 |
|
| 1998 |
Funane K, Libessart N, Stewart D, Michishita T, Preiss J. Analysis of essential histidine residues of maize branching enzymes by chemical modification and site-directed mutagenesis Journal of Protein Chemistry. 17: 579-590. PMID 9853672 DOI: 10.1007/Bf02780959 |
0.58 |
|
| 1998 |
Libessart N, Preiss J. Arginine residue 384 at the catalytic center is important for branching enzyme II from maize endosperm Archives of Biochemistry and Biophysics. 360: 135-141. PMID 9826438 DOI: 10.1006/Abbi.1998.0960 |
0.544 |
|
| 1998 |
Barth H, Preiss JC, Hofmann F, Aktories K. Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis. The Journal of Biological Chemistry. 273: 29506-11. PMID 9792657 DOI: 10.1074/jbc.273.45.29506 |
0.327 |
|
| 1998 |
Libessart N, Preiss J. High-level expression of branching enzyme II from maize endosperm in Escherichia coli Protein Expression and Purification. 14: 1-7. PMID 9758744 DOI: 10.1006/Prep.1998.0950 |
0.476 |
|
| 1998 |
Wu MX, Preiss J. The N-terminal region is important for the allosteric activation and inhibition of the Escherichia coli ADP-glucose pyrophosphorylase Archives of Biochemistry and Biophysics. 358: 182-188. PMID 9750179 DOI: 10.1006/Abbi.1998.0846 |
0.591 |
|
| 1998 |
Fu Y, Ballicora MA, Leykam JF, Preiss J. Mechanism of reductive activation of potato tuber ADP-glucose pyrophosphorylase Journal of Biological Chemistry. 273: 25045-25052. PMID 9737961 DOI: 10.1074/Jbc.273.39.25045 |
0.77 |
|
| 1998 |
Ballicora MA, Fu Y, Nesbitt NM, Preiss J. ADP-Glucose pyrophosphorylase from potato tubers. Site-directed mutagenesis studies of the regulatory sites. Plant Physiology. 118: 265-74. PMID 9733546 DOI: 10.1104/Pp.118.1.265 |
0.743 |
|
| 1998 |
Uttaro AD, Ugalde RA, Preiss J, Iglesias AA. Cloning and expression of the glgC gene from Agrobacterium tumefaciens: Purification and characterization of the ADPglucose synthetase Archives of Biochemistry and Biophysics. 357: 13-21. PMID 9721178 DOI: 10.1006/Abbi.1998.0786 |
0.575 |
|
| 1998 |
Preiss J, Sivak MN. Biochemistry, molecular biology and regulation of starch synthesis Genetic Engineering. 20: 177-223. PMID 9666561 DOI: 10.1007/978-1-4899-1739-3_10 |
0.351 |
|
| 1998 |
Fu Y, Ballicora MA, Preiss J. Mutagenesis of the Glucose-1-Phosphate-Binding Site of Potato Tuber ADP-Glucose Pyrophosphorylase Plant Physiology. 117: 989-996. PMID 9662541 DOI: 10.1104/Pp.117.3.989 |
0.76 |
|
| 1998 |
Binderup K, Preiss J. Glutamate-459 is important for Escherichia coli branching enzyme activity. Biochemistry. 37: 9033-7. PMID 9636047 DOI: 10.1021/Bi980199G |
0.857 |
|
| 1998 |
Meyer CR, Yirsa J, Gott B, Preiss J. A kinetic study of site-directed mutants of Escherichia coli ADP- glucose pyrophosphorylase: The role of residue 295 in allosteric regulation Archives of Biochemistry and Biophysics. 352: 247-254. PMID 9587413 DOI: 10.1006/Abbi.1998.0593 |
0.583 |
|
| 1998 |
Meyer CR, Bork JA, Nadler S, Yirsa J, Preiss J. Site-directed mutagenesis of a regulatory site of Escherichia coli ADP- glucose pyrophosphorylase: The role of residue 336 in allosteric behavior Archives of Biochemistry and Biophysics. 353: 152-159. PMID 9578610 DOI: 10.1006/Abbi.1998.0648 |
0.572 |
|
| 1998 |
Hill MA, Preiss J. Functional analysis of conserved histidines in ADP-glucose pyrophosphorylase from Escherichia coli Biochemical and Biophysical Research Communications. 244: 573-577. PMID 9514953 DOI: 10.1006/Bbrc.1998.8301 |
0.588 |
|
| 1998 |
Ballicora MA, Fu Y, Nesbitt NM, Preiss J. Regulation of the ADP-Glucose pyrophosphorylase from potato tuber. site-directed mutagenesis study Faseb Journal. 12: A1443. |
0.656 |
|
| 1998 |
Fu Y, Ballicora MA, Preiss J. Mutagenesis of the glucose-1-phosphate-binding site of potato tuber ADP-glucose pyrophosphorylase Plant Physiology. 117: 989-996. |
0.659 |
|
| 1997 |
Kuriki T, Stewart DC, Preiss J. Construction of chimetic enzymes out of maize endosperm branching enzymes I and II: Activity and properties Journal of Biological Chemistry. 272: 28999-29004. PMID 9360973 DOI: 10.1074/Jbc.272.46.28999 |
0.458 |
|
| 1997 |
Sheng J, Preiss J. Arginine294 is essential for the inhibition of Anabaena PCC 7120 ADP- glucose pyrophosphorylase by phosphate Biochemistry. 36: 13077-13084. PMID 9335570 DOI: 10.1021/Bi9713355 |
0.579 |
|
| 1997 |
Guan H, Li P, Imparl-Radosevich J, Preiss J, Keeling P. Comparing the properties of Escherichia coli branching enzyme and maize branching enzyme Archives of Biochemistry and Biophysics. 342: 92-98. PMID 9185617 DOI: 10.1006/Abbi.1997.0115 |
0.367 |
|
| 1997 |
Preiss J, Kuriki T, Stewart DC. Chimeric enzymes of maize branching enzymes I and II Faseb Journal. 11: A1146. |
0.397 |
|
| 1996 |
PREISS J, SHEN L, PARTRIDGE M. THE ACTIVATION OF ESCHERICHIA COLI ADP-GLUCOSE PYROPHOSPHORYLASE. Biochemical and Biophysical Research Communications. 18: 180-5. PMID 14282015 DOI: 10.1016/0006-291X(65)90737-0 |
0.448 |
|
| 1996 |
SHEN L, GHOSH HP, GREENBERG E, PREISS J. ADENOSINE DIPHOSPHATE GLUCOSE-GLYCOGEN TRANSGLUCOSYLASE IN ARTHROBACTER SP. NRRL B 1973. Biochimica Et Biophysica Acta. 89: 370-2. PMID 14205498 DOI: 10.1016/0926-6569(64)90232-9 |
0.333 |
|
| 1996 |
Preiss J. ADPglucose Pyrophosphorylase: Basic Science and Applications in Biotechnology Biotechnology Annual Review. 2: 259-279. PMID 9704099 DOI: 10.1016/S1387-2656(08)70013-9 |
0.408 |
|
| 1996 |
Ball S, Guan HP, James M, Myers A, Keeling P, Mouille G, Buléon A, Colonna P, Preiss J. From glycogen to amylopectin: A model for the biogenesis of the plant starch granule Cell. 86: 349-352. PMID 8756717 DOI: 10.1016/S0092-8674(00)80107-5 |
0.31 |
|
| 1996 |
Van den Koornhuyse N, Libessart N, Delrue B, Zabawinski C, Decq A, Iglesias A, Carton A, Preiss J, Ball S. Control of starch composition and structure through substrate supply in the monocellular alga Chlamydomonas reinhardtii Journal of Biological Chemistry. 271: 16281-16287. PMID 8663144 DOI: 10.1074/Jbc.271.27.16281 |
0.52 |
|
| 1996 |
Greene TW, Chantler SE, Kahn ML, Barry GF, Preiss J, Okita TW. Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation Proceedings of the National Academy of Sciences of the United States of America. 93: 1509-1513. PMID 8643662 DOI: 10.1073/Pnas.93.4.1509 |
0.714 |
|
| 1996 |
Sheng J, Charng YY, Preiss J. Site-directed mutagenesis of lysine382, the activator-binding site, of ADP-glucose pyrophosphorylase from Anabaena PCC 7120 Biochemistry. 35: 3115-3121. PMID 8608152 DOI: 10.1021/Bi952359J |
0.565 |
|
| 1996 |
Kuriki T, Guan H, Sivak M, Preiss J. Analysis of the active center of branching enzyme II from maize endosperm Protein Journal. 15: 305-313. DOI: 10.1007/Bf01887119 |
0.54 |
|
| 1996 |
Sheng J, Preiss J. Evidence for arginine residues involved in the allosteric site of cyanobacterial ADP-glucose pyrophosphorylase Faseb Journal. 10: A1101. |
0.326 |
|
| 1996 |
Fu Y, Ballicora MA, Preiss J. Site-directed mutagenesis study on the glucose 1-phosphate binding site of potato tuber adpglucose pyrophosphorylase Faseb Journal. 10: A1384. |
0.641 |
|
| 1996 |
Cao H, Preiss J. Evidence for essential arginine residues at the active sites of maize branching enzymes Protein Journal. 15: 291-304. |
0.427 |
|
| 1995 |
Guan H, Kuriki T, Sivak M, Preiss J. Maize branching enzyme catalyzes synthesis of glycogen-like polysaccharide in glgB-deficient Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 92: 964-967. PMID 7862674 DOI: 10.1073/Pnas.92.4.964 |
0.407 |
|
| 1995 |
Roberts MW, Preiss J, Okita TW. A Capillary Zone Electrophoresis Assay for the Nucleoside Transfer Enzyme Adenosine Diphosphate-Glucose Pyrophosphorylase Analytical Biochemistry. 225: 121-126. PMID 7778762 DOI: 10.1006/Abio.1995.1117 |
0.714 |
|
| 1995 |
Charng YY, Sheng J, Preiss J. Mutagenesis of an amino acid residue in the activator-binding site of cyanobacterial ADP-glucose pyrophosphorylase causes alteration in activator specificity Archives of Biochemistry and Biophysics. 318: 476-480. PMID 7733679 DOI: 10.1006/Abbi.1995.1256 |
0.578 |
|
| 1995 |
Ballicora MA, Laughlin MJ, Fu Y, Okita TW, Barry GF, Preiss J. Adenosine 5′-diphosphate-glucose pyrophosphorylase from potato tuber: Significance of the N terminus of the small subunit for catalytic properties and heat stability Plant Physiology. 109: 245-251. PMID 7480324 DOI: 10.1104/Pp.109.1.245 |
0.821 |
|
| 1995 |
Rahman S, Kosar-Hashemi B, Samuel MS, Hill A, Abbott DC, Skerritt JH, Preiss J, Appels R, Morell MK. The major proteins of wheat endosperm starch granules Australian Journal of Plant Physiology. 22: 793-803. DOI: 10.1071/Pp9950793 |
0.336 |
|
| 1995 |
Sivak MN, Preiss J. Progress in the genetic manipulation of crops aimed at changing starch structure and increasing starch accumulation Journal of Environmental Polymer Degradation. 3: 145-152. DOI: 10.1007/Bf02068465 |
0.439 |
|
| 1994 |
Guan HP, Baba T, Preiss J. Expression of branching enzyme I of maize endosperm in Escherichia coli Plant Physiology. 104: 1449-1453. PMID 8016271 DOI: 10.1104/Pp.104.4.1449 |
0.504 |
|
| 1994 |
Iglesias AA, Charng YY, Ball S, Preiss J. Characterization of the kinetic, regulatory, and structural properties of ADP-glucose pyrophosphorylase from Chlamydomonas reinhardtii Plant Physiology. 104: 1287-1294. PMID 8016263 DOI: 10.1104/Pp.104.4.1287 |
0.566 |
|
| 1994 |
Ball K, Preiss J. Allosteric sites of the large subunit of the spinach leaf ADPglucose pyrophosphorylase Journal of Biological Chemistry. 269: 24706-24711. PMID 7929144 |
0.393 |
|
| 1994 |
Charng YY, Iglesias AA, Preiss J. Structure-function relationships of cyanobacterial ADP-glucose pyrophosphorylase. Site-directed mutagenesis and chemical modification of the activator-binding sites of ADP-glucose pyrophosphorylase from Anabaena PCC 7120 Journal of Biological Chemistry. 269: 24107-24113. PMID 7929064 |
0.491 |
|
| 1994 |
Alonso MD, Lomako J, Lomako WM, Whelan WJ, Preiss J. Properties of carbohydrate-free recombinant glycogenin expressed in an Escherichia coli mutant lacking UDP-glucose pyrophosphorylase activity Febs Letters. 352: 222-226. PMID 7925977 DOI: 10.1016/0014-5793(94)00962-7 |
0.486 |
|
| 1994 |
Guan HP, Baba T, Preiss J. Expression of branching enzyme II of maize endosperm in Escherichia coli Cellular and Molecular Biology. 40: 981-988. PMID 7849565 |
0.379 |
|
| 1994 |
Kuriki T, Guan H, Preiss J. Structure and Function of Starch Branching Enzyme. Journal of the Agricultural Chemical Society of Japan. 68: 1581-1584. DOI: 10.1271/Nogeikagaku1924.68.1581 |
0.471 |
|
| 1994 |
Preiss J, Romeo T. Molecular Biology and Regulatory Aspects of Glycogen Biosynthesis in Bacteria Progress in Nucleic Acid Research and Molecular Biology. 47: 299-329. DOI: 10.1016/S0079-6603(08)60255-X |
0.5 |
|
| 1994 |
Smith-White B, Preiss J. Suggested mnemonics for cloned DNA corresponding to enzymes involved in starch metabolism Plant Molecular Biology Reporter. 12: S67-S71. DOI: 10.1007/Bf02671575 |
0.406 |
|
| 1993 |
Russell DA, Deboer DL, Stark DM, Preiss J, Fromm ME. Plastid targeting of E. coli β-glucuronidase and ADP-glucose pyrophosphorylase in maize (Zea mays L.) cells. Plant Cell Reports. 13: 24-7. PMID 24196177 DOI: 10.1007/Bf00232309 |
0.635 |
|
| 1993 |
Meyer CR, Ghosh P, Nadler S, Preiss J. Cloning, Expression, and Sequence of an Allosteric Mutant ADPglucose Pyrophosphorylase from Escherichia coli B Archives of Biochemistry and Biophysics. 302: 64-71. PMID 8385906 DOI: 10.1006/Abbi.1993.1181 |
0.475 |
|
| 1993 |
Kleczkowski LA, Villand P, Lüthi E, Olsen OA, Preiss J. Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation Plant Physiology. 101: 179-186. PMID 8278493 DOI: 10.1104/Pp.101.1.179 |
0.555 |
|
| 1993 |
Preiss J. Biosynthesis of Starch : ADPglucose Pyrophosphorylase, the Regulatory Enzyme of Starch Synthesis Structure-Function Relationships Journal of the Japanese Society of Starch Science. 40: 117-131. DOI: 10.5458/Jag1972.40.117 |
0.495 |
|
| 1993 |
Sivak MN, Wagner M, Preiss J. Biochemical evidence for the role of the waxy protein from pea (Pisum sativum L.) as a granule-bound starch synthase Plant Physiology. 103: 1355-1359. DOI: 10.1104/Pp.103.4.1355 |
0.327 |
|
| 1993 |
Guan HP, Preiss J. Differentiation of the properties of the branching isozymes from maize (Zea mays) Plant Physiology. 102: 1269-1273. DOI: 10.1104/Pp.102.4.1269 |
0.417 |
|
| 1993 |
Takeda Y, Guan HP, Preiss J. Branching of amylose by the branching isoenzymes of maize endosperm Carbohydrate Research. 240: 253-263. DOI: 10.1016/0008-6215(93)84188-C |
0.442 |
|
| 1992 |
Stark DM, Timmerman KP, Barry GF, Preiss J, Kishore GM. Regulation of the Amount of Starch in Plant Tissues by ADP Glucose Pyrophosphorylase. Science (New York, N.Y.). 258: 287-92. PMID 17835129 DOI: 10.1126/Science.258.5080.287 |
0.492 |
|
| 1992 |
Kakefuda G, Charng YY, Iglesias AA, McIntosh L, Preiss J. Molecular Cloning and Sequencing of ADP-Glucose Pyrophosphorylase from Synechocystis PCC 6803. Plant Physiology. 99: 359-61. PMID 16668879 DOI: 10.1104/Pp.99.1.359 |
0.49 |
|
| 1992 |
Ghosh P, Meyer C, Remy E, Peterson D, Preiss J. Cloning, expression, and nucleotide sequence of glgC gene from an allosteric mutant of Escherichia coli B. Archives of Biochemistry and Biophysics. 296: 122-8. PMID 1339262 DOI: 10.1016/0003-9861(92)90553-9 |
0.475 |
|
| 1992 |
Ball KL, Preiss J. Evidence for an arginine residue at the allosteric sites of spinach leaf ADPglucose pyrophosphorylase. Journal of Protein Chemistry. 11: 231-8. PMID 1326986 DOI: 10.1007/Bf01024861 |
0.55 |
|
| 1992 |
Iglesias AA, Kakefuda G, Preiss J. Involvement of arginine residues in the allosteric activation and inhibition of Synechocystis PCC 6803 ADPglucose pyrophosphorylase. Journal of Protein Chemistry. 11: 119-28. PMID 1326983 DOI: 10.1007/Bf01025217 |
0.52 |
|
| 1992 |
Charng YY, Kakefuda G, Iglesias AA, Buikema WJ, Preiss J. Molecular cloning and expression of the gene encoding ADP-glucose pyrophosphorylase from the cyanobacterium Anabaena sp. strain PCC 7120. Plant Molecular Biology. 20: 37-47. PMID 1325205 DOI: 10.1007/Bf00029147 |
0.531 |
|
| 1992 |
Meyer CR, Ghosh P, Remy E, Preiss J. Cloning, expression, and nucleotide sequence of a mutant glgC gene from Escherichia coli B. Journal of Bacteriology. 174: 4509-12. PMID 1320612 DOI: 10.1128/Jb.174.13.4509-4512.1992 |
0.378 |
|
| 1992 |
Smith-White BJ, Preiss J. Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources. Journal of Molecular Evolution. 34: 449-464. PMID 1318389 DOI: 10.1007/Bf00162999 |
0.432 |
|
| 1992 |
Li L, Preiss J. Characterization of ADPglucose pyrophosphorylase from a starch-deficient mutant of Arabidopsis thaliana (L.) Carbohydrate Research. 227: 227-239. DOI: 10.1016/0008-6215(92)85074-A |
0.531 |
|
| 1991 |
Caspar T, Lin T, Kakefuda G, Benbow L, Preiss J, Somerville C. Mutants of Arabidopsis with Altered Regulation of Starch Degradation Plant Physiology. 95: 1181-1188. PMID 16668109 DOI: 10.1104/Pp.95.4.1181 |
0.441 |
|
| 1991 |
Andersen JM, Larsen R, Laudencia D, Kim WT, Morrow D, Okita TW, Preiss J. Molecular characterization of the gene encoding a rice endosperm-specific ADPglucose pyrophosphorylase subunit and its developmental pattern of transcription Gene. 97: 199-205. PMID 1847888 DOI: 10.1016/0378-1119(91)90052-D |
0.573 |
|
| 1991 |
Nakata PA, Greene TW, Anderson JM, Smith-White BJ, Okita TW, Preiss J. Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits Plant Molecular Biology. 17: 1089-1093. PMID 1657244 DOI: 10.1007/Bf00037149 |
0.662 |
|
| 1991 |
Preiss J, Ball K, Hutney J, Smith-White B, Li L, Okita TW. Regulatory mechanisms involved in the biosynthesis of starch Pure and Applied Chemistry. 63: 535-544. DOI: 10.1351/Pac199163040535 |
0.73 |
|
| 1990 |
Monroe JD, Preiss J. Purification of a beta-Amylase that Accumulates in Arabidopsis thaliana Mutants Defective in Starch Metabolism. Plant Physiology. 94: 1033-9. PMID 16667793 DOI: 10.1104/Pp.94.3.1033 |
0.461 |
|
| 1990 |
Okita TW, Nakata PA, Anderson JM, Sowokinos J, Morell M, Preiss J. The Subunit Structure of Potato Tuber ADPglucose Pyrophosphorylase. Plant Physiology. 93: 785-790. PMID 16667537 DOI: 10.1104/Pp.93.2.785 |
0.691 |
|
| 1990 |
Preiss J, Danner S, Summers PS, Morell M, Barton CR, Yang L, Nieder M. Molecular Characterization of the Brittle-2 Gene Effect on Maize Endosperm ADPglucose Pyrophosphorylase Subunits. Plant Physiology. 92: 881-885. PMID 16667400 DOI: 10.1104/Pp.92.4.881 |
0.416 |
|
| 1990 |
Gardiol A, Preiss J. Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzyme. Archives of Biochemistry and Biophysics. 280: 175-80. PMID 2162151 DOI: 10.1016/0003-9861(90)90533-5 |
0.568 |
|
| 1990 |
Preiss J, Romeo T. Physiology, Biochemistry and Genetics of Bacterial Glycogen Synthesis Advances in Microbial Physiology. 30: 183-238. DOI: 10.1016/S0065-2911(08)60113-7 |
0.407 |
|
| 1990 |
Romeo T, Black J, Preiss J. Genetic regulation of glycogen biosynthesis in Escherichia coli: In vivo effects of the catabolite repression and stringent response systems in glg gene expression Current Microbiology. 21: 131-137. DOI: 10.1007/Bf02091831 |
0.44 |
|
| 1989 |
Caspar T, Lin T, Monroe J, Bernhard W, Spilatro S, Preiss J, Somerville C. Altered regulation of β-amylase activity in mutants of Arabidopsis with lesions in starch metabolism Proceedings of the National Academy of Sciences of the United States of America. 86: 5830-5833. PMID 16594057 DOI: 10.1073/Pnas.86.15.5830 |
0.424 |
|
| 1989 |
Romeo T, Preiss J. Genetic regulation of glycogen biosynthesis in Escherichia coli: in vitro effects of cyclic AMP and guanosine 5'-diphosphate 3'-diphosphate and analysis of in vivo transcripts Journal of Bacteriology. 171: 2773-2782. PMID 2468650 DOI: 10.1128/Jb.171.5.2773-2782.1989 |
0.437 |
|
| 1988 |
Lin TP, Caspar T, Somerville CR, Preiss J. A Starch Deficient Mutant of Arabidopsis thaliana with Low ADPglucose Pyrophosphorylase Activity Lacks One of the Two Subunits of the Enzyme. Plant Physiology. 88: 1175-81. PMID 16666440 DOI: 10.1104/Pp.88.4.1175 |
0.438 |
|
| 1988 |
Lin T, Caspar T, Somerville C, Preiss J. Isolation and characterization of a starchless mutant of Arabidopsis thaliana (L. ) Heynh lacking ADPglucose pyrophosphorylase activity Plant Physiology. 86: 1131-1135. PMID 16666044 DOI: 10.1104/Pp.86.4.1131 |
0.352 |
|
| 1988 |
Lin T, Spilatro SR, Preiss J. Subcellular localization and characterization of amylases in Arabidopsis leaf. Plant Physiology. 86: 251-259. PMID 16665876 DOI: 10.1104/Pp.86.1.251 |
0.353 |
|
| 1988 |
Romeo T, Kumar A, Preiss J. Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes Gene. 70: 363-376. PMID 2975249 DOI: 10.1016/0378-1119(88)90208-9 |
0.46 |
|
| 1988 |
Lee YM, Kumar A, Preiss J. Amino acid sequence of an Escherichia coli ADPglucose synthetase allosteric mutant as deduced from the DNA sequence of the glg C gene. Nucleic Acids Research. 15: 10603. PMID 2827128 DOI: 10.1093/Nar/15.24.10603 |
0.335 |
|
| 1987 |
Robinson NL, Preiss J. Localization of Carbohydrate Metabolizing Enzymes in Guard Cells of Commelina communis Plant Physiology. 85: 360-364. PMID 16665702 DOI: 10.1104/Pp.85.2.360 |
0.539 |
|
| 1987 |
Spilatro SR, Preiss J. Regulation of Starch Synthesis in the Bundle Sheath and Mesophyll of Zea mays L. : Intercellular Compartmentalization of Enzymes of Starch Metabolism and the Properties of the ADPglucose Pyrophosphorylases Plant Physiology. 83: 621-627. PMID 16665298 DOI: 10.1104/Pp.83.3.621 |
0.56 |
|
| 1987 |
Leung PS, Preiss J. Biosynthesis of bacterial glycogen: primary structure of Salmonella typhimurium ADPglucose synthetase as deduced from the nucleotide sequence of the glgC gene. Journal of Bacteriology. 169: 4355-60. PMID 3040691 DOI: 10.1128/Jb.169.9.4355-4360.1987 |
0.379 |
|
| 1987 |
Preiss J, Bloom M, Morell M, Knowles VL, Plaxton WC, Okita TW, Larsen R, Harmon AC, Putnam-Evans C. Regulation of starch synthesis: enzymological and genetic studies Basic Life Sciences. 41: 133-152. PMID 3036058 DOI: 10.1007/978-1-4684-5329-4_12 |
0.701 |
|
| 1986 |
Larsen CE, Preiss J. Covalent modification of the inhibitor binding site(s) of Escherichia coli ADP-glucose synthetase: specific incorporation of the photoaffinity analogue 8-azidoadenosine 5'-monophosphate. Biochemistry. 25: 4371-6. PMID 3019387 DOI: 10.1021/Bi00363A029 |
0.513 |
|
| 1986 |
Leung P, Lee YM, Greenberg E, Esch K, Boylan S, Preiss J. Cloning and expression of the Escherichia coli glgC gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties. Journal of Bacteriology. 167: 82-8. PMID 3013841 DOI: 10.1128/Jb.167.1.82-88.1986 |
0.469 |
|
| 1986 |
Lee YM, Mukherjee S, Preiss J. Covalent modification of Escherichia coli ADPglucose synthetase with 8-azido substrate analogs. Archives of Biochemistry and Biophysics. 244: 585-95. PMID 3004345 DOI: 10.1016/0003-9861(86)90627-2 |
0.507 |
|
| 1986 |
Macdonald FD, Preiss J. The subcellular location and characteristics of pyrophosphate-fructose-6-phosphate 1-phosphotransferase from suspension-cultured cells of soybean Planta. 167: 240-245. DOI: 10.1007/BF00391421 |
0.429 |
|
| 1985 |
Singh BK, Preiss J. Starch Branching Enzymes from Maize : Immunological Characterization using Polyclonal and Monoclonal Antibodies. Plant Physiology. 79: 34-40. PMID 16664399 DOI: 10.1104/Pp.79.1.34 |
0.526 |
|
| 1985 |
Macdonald FD, Preiss J. Partial purification and characterization of granule-bound starch synthases from normal and waxy maize. Plant Physiology. 78: 849-852. PMID 16664339 DOI: 10.1104/Pp.78.4.849 |
0.464 |
|
| 1984 |
Singh BK, Greenberg E, Preiss J. ADPglucose Pyrophosphorylase from the CAM Plants Hoya carnosa and Xerosicyos danguyi. Plant Physiology. 74: 711-6. PMID 16663486 DOI: 10.1104/Pp.74.3.711 |
0.494 |
|
| 1984 |
Yung SG, Paule M, Beggs R, Greenberg E, Preiss J. Biosynthesis of bacterial glycogen: characterization of adenosine diphosphate glucose synthetases from Enterobacter hafniae and Aeromonas hydrophila. Archives of Microbiology. 138: 1-8. PMID 6331331 DOI: 10.1007/Bf00425398 |
0.791 |
|
| 1984 |
Preiss J, Yung SG, Baecker PA. Regulation of bacterial glycogen synthesis. Molecular and Cellular Biochemistry. 57: 61-80. PMID 6316123 DOI: 10.1007/Bf00223525 |
0.545 |
|
| 1984 |
Preiss J. Bacterial glycogen synthesis and its regulation Annual Review of Microbiology. 38: 419-458. PMID 6093684 DOI: 10.1146/Annurev.Mi.38.100184.002223 |
0.481 |
|
| 1984 |
Preiss J. Starch, sucrose biosynthesis and partition of carbon in plants are regulated by orthophosphate and triose-phosphates Trends in Biochemical Sciences. 9: 24-27. DOI: 10.1016/0968-0004(84)90043-4 |
0.496 |
|
| 1983 |
Hammond JBW, Preiss J. ATP-Dependent Proteolytic Activity from Spinach Leaves Plant Physiology. 73: 902-905. PMID 16663340 DOI: 10.1104/Pp.73.4.902 |
0.369 |
|
| 1983 |
Robinson NL, Zeiger E, Preiss J. Regulation of ADPGlucose Synthesis in Guard Cells of Commelina communis Plant Physiology. 73: 862-864. PMID 16663316 DOI: 10.1104/Pp.73.3.862 |
0.384 |
|
| 1983 |
Hammond JBW, Preiss J. Spinach Leaf Intra and Extra Chloroplast Phosphorylase Activities during Growth. Plant Physiology. 73: 709-712. PMID 16663287 DOI: 10.1104/Pp.73.3.709 |
0.454 |
|
| 1983 |
Macdonald FD, Preiss J. Solubilization of the starch-granule-bound starch synthase of normal maize kernels. Plant Physiology. 73: 175-178. PMID 16663170 DOI: 10.1104/Pp.73.1.175 |
0.48 |
|
| 1983 |
Preiss J, Greenberg E. Pyrophosphate may be involved in regulation of bacterial glycogen synthesis Biochemical and Biophysical Research Communications. 115: 820-826. PMID 6312996 DOI: 10.1016/S0006-291X(83)80008-4 |
0.493 |
|
| 1983 |
Greenberg E, Preiss JE, Boldrick MV, Preiss J. Biosynthesis of bacterial glycogen: activator specificity of the ADPglucose pyrophosphorylase of Rhodopseudomonads. Archives of Biochemistry and Biophysics. 220: 594-604. PMID 6297405 DOI: 10.1016/0003-9861(83)90452-6 |
0.483 |
|
| 1982 |
Sowokinos JR, Preiss J. Pyrophosphorylases in Solanum tuberosum: III. PURIFICATION, PHYSICAL, AND CATALYTIC PROPERTIES OF ADPGLUCOSE PYROPHOSPHORYLASE IN POTATOES. Plant Physiology. 69: 1459-1466. PMID 16662422 DOI: 10.1104/Pp.69.6.1459 |
0.52 |
|
| 1982 |
Amir J, Preiss J. Kinetic characterization of spinach leaf sucrose-phosphate synthase. Plant Physiology. 69: 1027-1030. PMID 16662338 DOI: 10.1104/Pp.69.5.1027 |
0.51 |
|
| 1982 |
Holmes E, Preiss J. Detection of two essential sulfhydryl residues in Escherichia coli B glycogen synthase. Archives of Biochemistry and Biophysics. 216: 736-40. PMID 6810761 DOI: 10.1016/0003-9861(82)90264-8 |
0.416 |
|
| 1982 |
Okita TW, Rodriguez RL, Preiss J. [49] Isolation of Escherichia coli structural genes coding for the glycogen biosynthetic enzymes Methods in Enzymology. 83: 549-556. PMID 6285138 DOI: 10.1016/0076-6879(82)83051-6 |
0.579 |
|
| 1982 |
Carlson CA, Preiss J. Involvement of arginine residues in the allosteric activation of Escherichia coli ADP-glucose synthetase. Biochemistry. 21: 1929-34. PMID 6282325 DOI: 10.1021/Bi00537A036 |
0.587 |
|
| 1982 |
Holmes E, Boyer C, Preiss J. Immunological characterization of Escherichia coli B glycogen synthase and branching enzyme and comparison with enzymes from other bacteria. Journal of Bacteriology. 151: 1444-1453. PMID 6179926 DOI: 10.1128/Jb.151.3.1444-1453.1982 |
0.555 |
|
| 1982 |
Yung SG, Preiss J. Biosynthesis of bacterial glycogen: purification and structural and immunological properties of Rhodopseudomonas sphaeroides ADPglucose synthetase. Journal of Bacteriology. 151: 742-9. PMID 6178721 DOI: 10.1128/JB.151.2.742-749.1982 |
0.449 |
|
| 1982 |
Preiss J. Regulation of the Biosynthesis and Degradation of Starch Annual Review of Plant Biology. 33: 431-454. DOI: 10.1146/Annurev.Pp.33.060182.002243 |
0.422 |
|
| 1982 |
Preiss J, Huebner J, Greenberg E. Purification and structural properties ofRhodospirillum rubrum ADPglucose pyrophosphorylase Current Microbiology. 7: 257-262. DOI: 10.1007/Bf01568809 |
0.517 |
|
| 1982 |
Preiss J, Mazelis M, Greenberg E. Cloning of the aspartate-β-semialdehyde dehydrogenase structural gene fromEscherichia coli K12 Current Microbiology. 7: 263-267. DOI: 10.1007/Bf01566860 |
0.478 |
|
| 1981 |
Copeland L, Preiss J. Purification of Spinach Leaf ADPglucose Pyrophosphorylase Plant Physiology. 68: 996-1001. PMID 16662079 DOI: 10.1104/Pp.68.5.996 |
0.468 |
|
| 1981 |
Boyer CD, Preiss J. Evidence for Independent Genetic Control of the Multiple Forms of Maize Endosperm Branching Enzymes and Starch Synthases Plant Physiology. 67: 1141-1145. PMID 16661824 DOI: 10.1104/Pp.67.6.1141 |
0.539 |
|
| 1981 |
Pollock C, Preiss J. The citrate-stimulated starch synthase of starchy maize kernels: purification and properties. Archives of Biochemistry and Biophysics. 204: 578-88. PMID 6449907 DOI: 10.1016/0003-9861(80)90070-3 |
0.49 |
|
| 1981 |
Carlson CA, Preiss J. Modification of the allosteric activator site of Escherichia coli ADP-glucose synthetase by trinitrobenzenesulfonate. Biochemistry. 20: 7519-28. PMID 6275883 DOI: 10.1021/Bi00529A029 |
0.61 |
|
| 1981 |
Kappel WK, Preiss J. Biosynthesis of bacterial glycogen: purification and characterization of ADPglucose pyrophosphorylase with modified regulatory properties from Escherichia coli B mutant CL1136-504. Archives of Biochemistry and Biophysics. 209: 15-28. PMID 6269493 DOI: 10.1016/0003-9861(81)90252-6 |
0.494 |
|
| 1981 |
Preiss J, Greenberg E. Biosynthesis of bacterial glycogen: Activator specificity of the adenosine diphosphate glucose pyrophosphorylases from the genus Rhodospirillum Journal of Bacteriology. 147: 711-719. PMID 6268603 DOI: 10.1128/JB.147.3.711-719.1981 |
0.333 |
|
| 1981 |
Yung SG, Preiss J. Biosynthesis of bacterial glycogen: purification and structural properties of Rhodospirillum tenue adenosine diphosphate glucose synthetase. Journal of Bacteriology. 147: 101-9. PMID 6263861 DOI: 10.1128/JB.147.1.101-109.1981 |
0.502 |
|
| 1980 |
Lehmann M, Preiss J. Biosynthesis of bacterial glycogen: purification and properties of Salmonella typhimurium LT-2 adenosine diphosphate glucose pyrophosphorylase. Journal of Bacteriology. 143: 120-127. PMID 6156933 DOI: 10.1128/Jb.143.1.120-127.1980 |
0.582 |
|
| 1979 |
Boyer CD, Preiss J. Properties of Citrate-stimulated Starch Synthesis Catalyzed by Starch Synthase I of Developing Maize Kernels. Plant Physiology. 64: 1039-1042. PMID 16661088 DOI: 10.1104/Pp.64.6.1039 |
0.487 |
|
| 1979 |
Holmes E, Preiss J. Characterization of Escherichia coli B glycogen synthase enzymatic reactions and products Archives of Biochemistry and Biophysics. 196: 436-448. DOI: 10.1016/0003-9861(79)90295-9 |
0.448 |
|
| 1978 |
Su J, Preiss J. Purification and properties of sucrose synthase from maize kernels. Plant Physiology. 61: 389-393. PMID 16660299 DOI: 10.1104/Pp.61.3.389 |
0.521 |
|
| 1978 |
Levi C, Preiss J. Amylopectin degradation in pea chloroplast extracts. Plant Physiology. 61: 218-220. PMID 16660263 DOI: 10.1104/Pp.61.2.218 |
0.487 |
|
| 1978 |
Boyer CD, Preiss J. Multiple forms of starch branching enzyme of maize: Evidence for independent genetic control Biochemical and Biophysical Research Communications. 80: 169-175. PMID 623651 DOI: 10.1016/0006-291X(78)91119-1 |
0.543 |
|
| 1978 |
Kawaguchi K, Fox J, Holmes E, Boyer C, Preiss J. De novo synthesis of Escherichia coli glycogen is due to primer associated with glycogen synthase and activation by branching enzyme. Archives of Biochemistry and Biophysics. 190: 385-397. PMID 102249 DOI: 10.1016/0003-9861(78)90291-6 |
0.497 |
|
| 1978 |
Boyer CD, Preiss J. Multiple forms of (1 → 4)-α-d-glucan, (1 → 4)-α-d-glucan-6- glycosyl transferase from developing zea mays L. Kernels Carbohydrate Research. 61: 321-334. DOI: 10.1016/S0008-6215(00)84492-4 |
0.509 |
|
| 1977 |
Boyer C, Preiss J. Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B α-1,4-glucan:α-1,4-glucan 6-glycosyltransferase Biochemistry. 16: 3693-3699. PMID 407932 DOI: 10.1021/Bi00635A029 |
0.521 |
|
| 1977 |
Steiner KE, Preiss J. Biosynthesis of bacterial glycogen: genetic and allosteric regulation of glycogen biosynthesis in Salmonella typhimurium LT-2. Journal of Bacteriology. 129: 246-253. PMID 401493 DOI: 10.1128/Jb.129.1.246-253.1977 |
0.473 |
|
| 1976 |
Levi C, Preiss J. Regulatory Properties of the ADP-Glucose Pyrophosphorylase of the Blue-Green Bacterium Synechococcus 6301 Plant Physiology. 58: 753-756. PMID 16659760 DOI: 10.1104/Pp.58.6.753 |
0.533 |
|
| 1976 |
Preiss J, Lammel C, Greenberg E. Biosynthesis of bacterial glycogen: Kinetic studies of a glucose-1-P adenylyltransferase (EC 2.7.7.27) from a glycogen-excess mutant of Escherichia coli B Archives of Biochemistry and Biophysics. 174: 105-119. PMID 779654 DOI: 10.1016/0003-9861(76)90329-5 |
0.514 |
|
| 1976 |
Haugen T, Ishaque A, Preiss J. ADPGlucose pyrophosphorylase: evidence for a lysine residue at the activator site of the Escherichia coli B enzyme. Biochemical and Biophysical Research Communications. 69: 346-53. PMID 773375 DOI: 10.1016/0006-291X(76)90528-3 |
0.555 |
|
| 1976 |
Preiss J, Crawford K, Downey J, Lammel C, Greenberg E. Kinetic properties of Serratia marcescens adenosine 5'-diphosphate glucose pyrophosphorylase. Journal of Bacteriology. 127: 193-203. PMID 6432 DOI: 10.1128/Jb.127.1.193-203.1976 |
0.559 |
|
| 1976 |
Fox J, Kawaguchi K, Greenberg E, Preiss J. Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B ADPglucose:1,4-alpha-D-glucan 4-alpha-glucosyltransferase. Biochemistry. 15: 849-57. PMID 2288 DOI: 10.1021/Bi00649A019 |
0.521 |
|
| 1974 |
Haugen T, Ishaque A, Chatterjee AK, Preiss J. Purification of Escherichia coli ADPglucose pyrophosphorylase by affinity chromatography. Febs Letters. 42: 205-8. PMID 4369095 DOI: 10.1016/0014-5793(74)80786-6 |
0.367 |
|
| 1974 |
Hawker JS, Ozbun JL, Ozaki H, Greenberg E, Preiss J. Interaction of spinach leaf adenosine diphosphate glucose α-1, 4-glucan α-4-glucosyl transferase and α-1, 4-glucan α-1, 4-glucan-6-glycosyl transferase in synthesis of branched α-glucan Archives of Biochemistry and Biophysics. 160: 530-551. PMID 4208773 DOI: 10.1016/0003-9861(74)90430-5 |
0.442 |
|
| 1973 |
Ozbun JL, Hawker JS, Greenberg E, Lammel C, Preiss J, Lee EYC. Starch Synthetase, Phosphorylase, ADPglucose Pyrophosphorylase, and UDPglucose Pyrophosphorylase in Developing Maize Kernels. Plant Physiology. 51: 1-5. PMID 16658267 DOI: 10.1104/Pp.51.1.1 |
0.378 |
|
| 1973 |
Preiss J, Ozbun JL, Hawker JS, Greenberg E, Lammel C. ADPG SYNTHETASE AND ADPG‐α‐GLUCAN 4‐GLUCOSYL TRANSFERASE: ENZYMES INVOLVED IN BACTERIAL GLYCOGEN AND PLANT STARCH SYNTHESIS* Annals of the New York Academy of Sciences. 210: 265-278. PMID 4633325 DOI: 10.1111/J.1749-6632.1973.Tb47578.X |
0.475 |
|
| 1972 |
Ozbun JL, Hawker JS, Preiss J. Soluble adenosine diphosphate glucose–α-1,4-glucan α-4-glucosyltransferases from spinach leaves Biochemical Journal. 126: 953-963. PMID 5073245 DOI: 10.1042/Bj1260953 |
0.338 |
|
| 1972 |
Hawker JS, Ozbun JL, Preiss J. Unprimed starch synthesis by soluble ADPglucose—starch glucosyltransferase from potato tubers Phytochemistry. 11: 1287-1293. DOI: 10.1016/S0031-9422(00)90076-1 |
0.494 |
|
| 1972 |
Ozbun JL, Hawker JS, Preiss J. [75] Starch synthetase from spinach leaves Methods in Enzymology. 28: 545-550. DOI: 10.1016/0076-6879(72)28078-8 |
0.397 |
|
| 1972 |
Fox J, Govons S, Preiss J. [74] Glycogen synthetase from Escherichia coli B Methods in Enzymology. 28: 539-544. DOI: 10.1016/0076-6879(72)28077-6 |
0.32 |
|
| 1972 |
Ozaki H, Preiss J. [50] ADP-glucose pyrophosphorylase from Escherichia coli B Methods in Enzymology. 28: 406-413. DOI: 10.1016/0076-6879(72)28053-3 |
0.393 |
|
| 1972 |
Preiss J, Greenberg E. [27] ADP-[14C]Glucose Methods in Enzymology. 28: 279-281. DOI: 10.1016/0076-6879(72)28029-6 |
0.357 |
|
| 1971 |
Ozbun JL, Hawker JS, Preiss J. Adenosine Diphosphoglucose-Starch Glucosyltransferases from Developing Kernels of Waxy Maize Plant Physiology. 48: 765-769. PMID 16657876 DOI: 10.1104/Pp.48.6.765 |
0.341 |
|
| 1971 |
Preiss J, Lammel C, Sabraw A. A unique adenosine diphosphoglucose pyrophosphorylase associated with maize embryo tissue. Plant Physiology. 47: 104-108. PMID 16657563 DOI: 10.1104/Pp.47.1.104 |
0.525 |
|
| 1971 |
Ozbun JL, Hawker JS, Preiss J. Multiple forms of α-1,4 glucan synthetase from spinach leaves Biochemical and Biophysical Research Communications. 43: 631-636. PMID 4998187 DOI: 10.1016/0006-291X(71)90661-9 |
0.344 |
|
| 1971 |
Ribéreau-Gayon G, Sabraw A, Lammel C, Preiss J. Biosynthesis of bacterial glycogen IX: Regulatory properties of the adenosine diphosphate glucose pyrophosphorylases of the Enterobocteriaceae Archives of Biochemistry and Biophysics. 142: 675-692. PMID 4396287 DOI: 10.1016/0003-9861(71)90534-0 |
0.556 |
|
| 1971 |
Preiss J, Sabraw A, Greenberg E. An ADP-glucsoe pyrophosphorylase with lower apparent affinities for substract and effector molecules in an Escherichia coli B mutant deficient in glycogen synthesis. Biochemical and Biophysical Research Communications. 42: 180-6. PMID 4395969 DOI: 10.1016/0006-291X(71)90085-4 |
0.547 |
|
| 1971 |
Preiss J, Greenberg E. [68] Spinach leaf d-fructose 1,6-diphosphate 1-phosphohydrolase (FDPase) EC 3.1.3.11 Methods in Enzymology. 23: 691-696. DOI: 10.1016/S0076-6879(71)23144-X |
0.45 |
|
| 1971 |
Ribéreau-Gayon G, Preiss J. [59] ADP-glucose pyrophosphorylase from spinach leaf Methods in Enzymology. 23: 618-624. DOI: 10.1016/S0076-6879(71)23135-9 |
0.434 |
|
| 1970 |
Eidels L, Edelmann PL, Preiss J. Biosynthesis of bacterial glycogen. 8. Activation and inhibition of the adenosine diphosphoglucose pyrophosphorylase of Rhodopseudomonas capsulata and of Agrobacterium tumefaciens. Archives of Biochemistry and Biophysics. 140: 60-74. PMID 5460185 DOI: 10.1016/0003-9861(70)90010-X |
0.477 |
|
| 1970 |
Eidels L, Preiss J. Carbohydrate metabolism in Rhodopseudomonas capsulata: enzyme titers, glucose metabolism, and polyglucose polymer synthesis. Archives of Biochemistry and Biophysics. 140: 75-89. PMID 4248272 DOI: 10.1016/0003-9861(70)90011-1 |
0.441 |
|
| 1969 |
Dickinson DB, Preiss J. Presence of ADP-Glucose Pyrophosphorylase in Shrunken-2 and Brittle-2 Mutants of Maize Endosperm. Plant Physiology. 44: 1058-1062. PMID 16657157 DOI: 10.1104/Pp.44.7.1058 |
0.532 |
|
| 1969 |
Preiss J, Greenberg E. Allosteric regulation of uridine diphosphoglucose: D-fructose-6-phosphate-2-glucosyl transferase (E.C.2.4.1.14) Biochemical and Biophysical Research Communications. 36: 289-295. PMID 5799647 DOI: 10.1016/0006-291X(69)90328-3 |
0.502 |
|
| 1969 |
Dickinson DB, Preiss J. ADP glucose pyrophosphorylase from maize endosperm. Archives of Biochemistry and Biophysics. 130: 119-128. PMID 5778634 DOI: 10.1016/0003-9861(69)90017-4 |
0.542 |
|
| 1969 |
Govons S, Vinopal R, Ingraham J, Preiss J. Isolation of mutants of Escherichia coli B altered in their ability to synthesize glycogen. Journal of Bacteriology. 97: 970-2. PMID 4886303 DOI: 10.1128/Jb.97.2.970-972.1969 |
0.335 |
|
| 1969 |
Gentner N, Greenberg E, Preiss J. TPNH and pyridoxal-5'-phosphate: activators of ADP-glucose pyrophosphorylase of Escherichia coli B1. Biochemical and Biophysical Research Communications. 36: 373-80. PMID 4390399 DOI: 10.1016/0006-291X(69)90574-9 |
0.494 |
|
| 1969 |
Sanwal GG, Preiss J. Sugar nucleotides and nucleotide-peptide complexes of Chlorella pyrenoidosa: Isolation and characterization Phytochemistry. 8: 707-723. DOI: 10.1016/S0031-9422(00)85842-2 |
0.388 |
|
| 1969 |
Preiss J. The Regulation of the Biosynthesis of α-1,4 Glucans in Bacteria and Plants Current Topics in Cellular Regulation. 1: 125-160. DOI: 10.1016/B978-0-12-152801-0.50011-0 |
0.453 |
|
| 1968 |
Sanwal GG, Greenberg E, Hardie J, Cameron EC, Preiss J. Regulation of starch biosynthesis in plant leaves: activation and inhibition of ADPglucose pyrophosphorylase. Plant Physiology. 43: 417-27. PMID 5644247 DOI: 10.1104/Pp.43.3.417 |
0.441 |
|
| 1967 |
Preiss J, Greenberg E. Biosynthesis of starch in Chlorella pyrenoidosa. I. Purification and properties of the adenosine diphosphoglucose: α-1, 4-glucan, α-4-glucosyl transferase from Chlorella Archives of Biochemistry and Biophysics. 118: 702-708. PMID 6057640 DOI: 10.1016/0003-9861(67)90407-9 |
0.418 |
|
| 1967 |
Sanwal GG, Preiss J. Biosynthesis of starch in Chlorella pyrenoidosa: II. Regulation of ATP: α-d-Glucose 1-phosphate adenyl transferase (ADP-Glucose pyrophosphorylase) by inorganic phosphate and 3-phosphoglycerate Archives of Biochemistry and Biophysics. 119: 454-469. PMID 6052439 DOI: 10.1016/0003-9861(67)90477-8 |
0.527 |
|
| 1967 |
Shen L, Preiss J. Biosynthesis of bacterial glycogen. V. The activation and inhibition of the adenosine diphosphate glucose pyrophosphorylase of Arthrobacter viscosus NRRL BI973. Archives of Biochemistry and Biophysics. 116: 375-90. PMID 5961843 DOI: 10.1016/0003-9861(66)90044-0 |
0.44 |
|
| 1967 |
Gentner N, Preiss J. Activator-inhibitor interactions in the adenosine diphosphate glucose pyrophosphorylase of Escherichia coli B. Biochemical and Biophysical Research Communications. 27: 417-23. PMID 4291967 DOI: 10.1016/S0006-291X(67)80116-5 |
0.421 |
|
| 1967 |
Dahmen W, Webb B, Preiss J. The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide pyrophosphorylases of Escherichia coli and yeast. Archives of Biochemistry and Biophysics. 120: 440-50. PMID 4291828 DOI: 10.1016/0003-9861(67)90262-7 |
0.501 |
|
| 1967 |
Preiss J, Greenberg E. Enzymic synthesis of GDP-mannose-14C from mannose-14C Analytical Biochemistry. 18: 464-471. DOI: 10.1016/0003-2697(67)90105-4 |
0.35 |
|
| 1966 |
Preiss J, Shen L, Greenberg E, Gentner N. Biosynthesis of Bacterial Glycogen. IV. Activation and Inhibition of the Adenosine Diphosphate Glucose Pyrophosphorylase of Escherichia coli B* Biochemistry. 5: 1833-1845. DOI: 10.1021/Bi00870A008 |
0.441 |
|
| 1966 |
Preiss J. [107] 4-Deoxy-l-threo-5-hexosulose uronic acid isomerase Methods in Enzymology. 9: 602-604. DOI: 10.1016/0076-6879(66)09121-3 |
0.34 |
|
| 1966 |
Preiss J. [42] 4-Deoxy-l-erythro-5-hexosulose uronic acid reductase Methods in Enzymology. 9: 206-209. DOI: 10.1016/0076-6879(66)09049-9 |
0.446 |
|
| 1966 |
Preiss J. [41] 3-Deoxy-d-glycero-2,5-hexodiulosonic acid reductase☆ Methods in Enzymology. 9: 203-206. DOI: 10.1016/0076-6879(66)09048-7 |
0.397 |
|
| 1966 |
Preiss J. [110] Bacterial alginate lyase Methods in Enzymology. 8: 641-644. DOI: 10.1016/0076-6879(66)08116-3 |
0.345 |
|
| 1966 |
Preiss J. [65] ADP-glucose: α-1,4-glucan glucosyltransferase (glycogen synthetase) of Arthrobacter Methods in Enzymology. 8: 384-387. DOI: 10.1016/0076-6879(66)08069-8 |
0.539 |
|
| 1966 |
Preiss J. [49] GDP-mannose dehydrogenase from Arthrobacter Methods in Enzymology. 8: 285-287. DOI: 10.1016/0076-6879(66)08053-4 |
0.507 |
|
| 1966 |
Preiss J. [45] GDP-mannose pyrophosphorylase from Arthrobacter Methods in Enzymology. 8: 271-275. DOI: 10.1016/0076-6879(66)08049-2 |
0.454 |
|
| 1966 |
Shen L, Preiss J. [42] ADP-glucose pyrophosphorylase from Arthrobacter Methods in Enzymology. 8: 262-266. DOI: 10.1016/0076-6879(66)08046-7 |
0.521 |
|
| 1965 |
Ghosh HP, Preiss J. Biosynthesis of starch in spinach chloroplasts Biochemistry. 4: 1354-1361. PMID 5856636 DOI: 10.1021/Bi00883A020 |
0.477 |
|
| 1965 |
Preiss J, Greenberg E. Biosynthesis of bacterial glycogen. III. The adenosine diphosphate-glucose:α-4-glucosyl transferase of Escherichia coli B Biochemistry. 4: 2328-2334. PMID 5326687 DOI: 10.1021/Bi00887A010 |
0.515 |
|
| 1964 |
Shen L, Preiss J. The activation and inhibition of bacterial adenosine-diphosphoglucose pyrophosphorylase☆ Biochemical and Biophysical Research Communications. 17: 424-429. DOI: 10.1016/0006-291X(64)90023-3 |
0.324 |
|
| 1963 |
Imsande J, Preiss J, Handler P. [44] Synthesis of diphosphopyridine nucleotide from nicotinic acid Methods in Enzymology. 6: 345-352. DOI: 10.1016/0076-6879(63)06184-X |
0.544 |
|
| 1961 |
PREISS J, DIECKMANN M, BERG P. The enzymic synthesis of amino acyl derivatives of ribonucleic acid. IV. The formation of the 3'-hydroxyl terminal trinucleotide sequence of amino acid-acceptor ribonucleic acid. The Journal of Biological Chemistry. 236: 1748-57. PMID 13737830 |
0.476 |
|
| 1959 |
Preiss J, Berg P, Ofengand EJ, Bergmann FH, Dieckmann M. THE CHEMICAL NATURE OF THE RNA-AMINO ACID COMPOUND FORMED BY AMINO ACID-ACTIVATING ENZYMES. Proceedings of the National Academy of Sciences of the United States of America. 45: 319-28. PMID 16590384 DOI: 10.1073/Pnas.45.3.319 |
0.776 |
|
| 1958 |
PREISS J, HANDLER P. Biosynthesis of diphosphopyridine nucleotide. II. Enzymatic aspects. The Journal of Biological Chemistry. 233: 493-500. PMID 13563527 |
0.445 |
|
| 1958 |
PREISS J, HANDLER P. Biosynthesis of diphosphopyridine nucleotide. I. Identification of intermediates. The Journal of Biological Chemistry. 233: 488-92. PMID 13563526 |
0.495 |
|
| 1957 |
PREISS J, HANDLER P. Enzymatic synthesis of nicotinamide mononucleotide. The Journal of Biological Chemistry. 225: 759-70. PMID 13416279 |
0.476 |
|
| 1957 |
Preiss J, Handler P. INTERMEDIATES IN THE SYNTHESIS OF DIPHOSPHOPYRIDINE NUCLEOTIDE FROM NICOTINIC ACID1 Journal of the American Chemical Society. 79: 4246-4247. DOI: 10.1021/Ja01572A079 |
0.443 |
|
| 1957 |
Preiss J, Handler P. Synthesis of diphosphopyridine nucleotide from nicotinic acid by human erythrocytes in vitro [10] Journal of the American Chemical Society. 79: 1514-1515. DOI: 10.1021/Ja01563A073 |
0.497 |
|
| Show low-probability matches. |
