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Carl Frieden - Publications

Affiliations: 
Biochemistry and Molecular Biophysics Washington University, Saint Louis, St. Louis, MO 
Area:
protein folding, protein structure/function relationships, protein-protein interactions and the mechanisms of enzymatic reactions
Website:
http://bmbweb.wustl.edu/faculty/faculty/carl-frieden

193 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 Kober DL, Stuchell-Brereton MD, Kluender CE, Dean HB, Strickland MR, Steinberg DF, Nelson SS, Baban B, Holtzman DM, Frieden C, Alexander-Brett J, Roberson ED, Song Y, Brett TJ. Functional insights from biophysical study of TREM2 interactions with apoE and Aβ. Alzheimer's & Dementia : the Journal of the Alzheimer's Association. PMID 33090700 DOI: 10.1002/alz.12194  0.4
2016 Shu Q, Krezel AM, Cusumano ZT, Pinkner JS, Klein R, Hultgren SJ, Frieden C. Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation. Proceedings of the National Academy of Sciences of the United States of America. PMID 27298344 DOI: 10.1073/Pnas.1607222113  1
2016 Mondal T, Wang H, DeKoster GT, Baban B, Gross ML, Frieden C. ApoE: In vitro studies of a small molecule effector. Biochemistry. PMID 27065061 DOI: 10.1021/Acs.Biochem.6B00324  1
2015 Wang H, Shu Q, Rempel DL, Frieden C, Gross ML. Continuous and Pulsed Hydrogen-Deuterium Exchange and Mass Spectrometry Characterize CsgE Oligomerization. Biochemistry. 54: 6475-81. PMID 26418947 DOI: 10.1021/Acs.Biochem.5B00871  1
2015 Frieden C. ApoE: The role of conserved residues in defining function Protein Science. 24: 138-144. DOI: 10.1002/pro.2597  1
2014 Garai K, Verghese PB, Baban B, Holtzman DM, Frieden C. The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation. Biochemistry. 53: 6323-31. PMID 25207746 DOI: 10.1021/Bi5008172  1
2013 Crick SL, Ruff KM, Garai K, Frieden C, Pappu RV. Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation. Proceedings of the National Academy of Sciences of the United States of America. 110: 20075-80. PMID 24282292 DOI: 10.1073/Pnas.1320626110  0.64
2013 Frieden C, Garai K. Concerning the structure of apoE Protein Science. 22: 1820-1825. PMID 24115173 DOI: 10.1002/Pro.2379  1
2013 Verghese PB, Castellano JM, Garai K, Wang Y, Jiang H, Shah A, Bu G, Frieden C, Holtzman DM. ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions. Proceedings of the National Academy of Sciences of the United States of America. 110: E1807-16. PMID 23620513 DOI: 10.1073/Pnas.1220484110  1
2013 Garai K, Frieden C. Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ Proceedings of the National Academy of Sciences of the United States of America. 110: 3321-3326. PMID 23401512 DOI: 10.1073/Pnas.1222478110  1
2013 Crick SL, Ruff KM, Garai K, Frieden C, Pappu RV. Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation Proceedings of the National Academy of Sciences of the United States of America. 110: 20075-20080. DOI: 10.1073/pnas.1320626110  1
2012 Frieden C, Garai K. Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease. Proceedings of the National Academy of Sciences of the United States of America. 109: 8913-8. PMID 22615372 DOI: 10.1073/Pnas.1207022109  1
2012 Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. Proceedings of the National Academy of Sciences of the United States of America. 109: 6502-7. PMID 22493266 DOI: 10.1073/Pnas.1204161109  1
2012 Frieden C, Garai K. Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease (Proceedings of the National Academy of Sciences of the United States of America (2012) 109, (8913-8918) DOI: 10.1073/pnas.1207022109) Proceedings of the National Academy of Sciences of the United States of America. 109: 13130. DOI: 10.1073/pnas.1209739109  1
2011 Huang RY, Garai K, Frieden C, Gross ML. Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization. Biochemistry. 50: 9273-82. PMID 21899263 DOI: 10.1021/Bi2010027  1
2011 Gau B, Garai K, Frieden C, Gross ML. Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4. Biochemistry. 50: 8117-26. PMID 21848287 DOI: 10.1021/Bi200911C  1
2011 Garai K, Baban B, Frieden C. Self-association and stability of the ApoE isoforms at low pH: Implications for ApoE-lipid interactions Biochemistry. 50: 6356-6364. PMID 21699199 DOI: 10.1021/Bi2006702  1
2011 Garai K, Baban B, Frieden C. Dissociation of apolipoprotein e oligomers to monomer is required for high-affinity binding to phospholipid vesicles Biochemistry. 50: 2550-2558. PMID 21322570 DOI: 10.1021/Bi1020106  1
2010 Garai K, Frieden C. The association-dissociation behavior of the ApoE proteins: Kinetic and equilibrium studies Biochemistry. 49: 9533-9541. PMID 20923231 DOI: 10.1021/Bi101407M  1
2010 Niu W, Shu Q, Chen Z, Mathews S, Di Cera E, Frieden C. The role of Zn2+ on the structure and stability of murine adenosine deaminase Journal of Physical Chemistry B. 114: 16156-16165. PMID 20815357 DOI: 10.1021/Jp106041V  1
2010 Baldwin RL, Frieden C, Rose GD. Dry molten globule intermediates and the mechanism of protein unfolding. Proteins. 78: 2725-37. PMID 20635344 DOI: 10.1002/Prot.22803  1
2010 Mustafi SM, Garai K, Crick SL, Baban B, Frieden C. Substoichiometric inhibition of Aβ1-40 aggregation by a tandem Aβ40-1-Gly8-1-40 peptide Biochemical and Biophysical Research Communications. 397: 509-512. PMID 20515649 DOI: 10.1016/J.Bbrc.2010.05.144  1
2010 Garai K, Mustafi SM, Baban B, Frieden C. Structural differences between apolipoprotein E3 and E4 as measured by 19F NMR Protein Science. 19: 66-74. PMID 19904741 DOI: 10.1002/Pro.283  1
2009 Hu X, Crick SL, Bu G, Frieden C, Pappu RV, Lee JM. Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide Proceedings of the National Academy of Sciences of the United States of America. 106: 20324-20329. PMID 19910533 DOI: 10.1073/Pnas.0911281106  1
2009 Zhang R, Hu X, Khant H, Ludtke SJ, Chiu W, Schmid MF, Frieden C, Lee JM. Interprotofilament interactions between alzheimer's aβ 1-42 peptides in amyloid fibrils revealed by cryoEM Proceedings of the National Academy of Sciences of the United States of America. 106: 4653-4658. PMID 19264960 DOI: 10.1073/Pnas.0901085106  1
2009 Garai K, Crick SL, Mustafi SM, Frieden C. Expression and purification of amyloid-β peptides from Escherichia coli Protein Expression and Purification. 66: 107-112. PMID 19233290 DOI: 10.1016/J.Pep.2009.02.009  1
2008 Frieden C. A lifetime of kinetics. The Journal of Biological Chemistry. 283: 19873-19878. PMID 18442970 DOI: 10.1074/Jbc.X800003200  1
2007 Frieden C. Protein aggregation processes: In search of the mechanism Protein Science. 16: 2334-2344. PMID 17962399 DOI: 10.1110/Ps.073164107  1
2007 Li H, Frieden C. Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR Proceedings of the National Academy of Sciences of the United States of America. 104: 11993-11998. PMID 17615232 DOI: 10.1073/Pnas.0705253104  1
2007 Li H, Frieden C. Comparison of C40/82A and P27A C40/82A barstar mutants using 19F NMR Biochemistry. 46: 4337-4347. PMID 17371049 DOI: 10.1021/Bi6026083  1
2006 Crick SL, Jayaraman M, Frieden C, Wetzel R, Pappu RV. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions Proceedings of the National Academy of Sciences of the United States of America. 103: 16764-16769. PMID 17075061 DOI: 10.1073/Pnas.0608175103  1
2006 Li H, Frieden C. Fluorine-19 NMR studies on the acid state of the intestinal fatty acid binding protein Biochemistry. 45: 6272-6278. PMID 16700539 DOI: 10.1021/Bi0602922  1
2006 Chattopadhyay K, Frieden C. Steady-state and time-resolved fluorescence studies of the intestinal fatty acid binding protein Proteins: Structure, Function and Genetics. 63: 327-335. PMID 16421929 DOI: 10.1002/Prot.20861  1
2005 Justice SS, Hunstad DA, Harper JR, Duguay AR, Pinkner JS, Bann J, Frieden C, Silhavy TJ, Hultgren SJ. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli Journal of Bacteriology. 187: 7680-7686. PMID 16267292 DOI: 10.1128/Jb.187.22.7680-7686.2005  1
2005 Li H, Frieden C. Phenylalanine side chain behavior of the intestinal fatty acid-binding protein: The effect of urea on backbone and side chain stability Journal of Biological Chemistry. 280: 38556-38561. PMID 16162507 DOI: 10.1074/Jbc.M505435200  1
2005 Li H, Frieden C. NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: Evidence for conformational heterogeneity in the native state Biochemistry. 44: 2369-2377. PMID 15709749 DOI: 10.1021/Bi047600L  1
2005 Chattopadhyay K, Elson EL, Frieden C. The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods Proceedings of the National Academy of Sciences of the United States of America. 102: 2385-2389. PMID 15701687 DOI: 10.1073/Pnas.0500127102  1
2005 Shu Q, Frieden C. Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies Journal of Molecular Biology. 345: 599-610. PMID 15581901 DOI: 10.1016/J.Jmb.2004.10.057  1
2005 Chattopadhyay K, Saffarian S, Elson EL, Frieden C. Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy. Biophysical Journal. 88: 1413-22. PMID 15556973 DOI: 10.1529/Biophysj.104.053199  1
2004 Bann JG, Pinkner JS, Frieden C, Hultgren SJ. Catalysis of protein folding by chaperones in pathogenic bacteria Proceedings of the National Academy of Sciences of the United States of America. 101: 17389-17393. PMID 15583129 DOI: 10.1073/Pnas.0408072101  1
2004 Sullivan B, Kornfeld SA, Frieden C, Goldberg DE. The Washington University Medical Scientist Training Program. Missouri Medicine. 101: 491-5. PMID 15535025  1
2004 Bann JG, Frieden C. Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR Biochemistry. 43: 13775-13786. PMID 15504040 DOI: 10.1021/Bi048614U  1
2004 Frieden C, Hoeltzli SD, Bann JG. The Preparation of 19F-Labeled Proteins for NMR Studies Methods in Enzymology. 380: 400-415. PMID 15051347 DOI: 10.1016/S0076-6879(04)80018-1  1
2004 Shu Q, Frieden C. Urea-Dependent Unfolding of Murine Adenosine Deaminase: Sequential Destabilization As Measured by 19F NMR Biochemistry. 43: 1432-1439. PMID 14769019 DOI: 10.1021/Bi035651X  1
2003 Frieden C. The Kinetics of Side Chain Stabilization during Protein Folding Biochemistry. 42: 12439-12446. PMID 14580188 DOI: 10.1021/Bi030192L  1
2003 Rajabzadeh M, Kao J, Frieden C. Consequences of Single-Site Mutations in the Intestinal Fatty Acid Binding Protein Biochemistry. 42: 12192-12199. PMID 14567680 DOI: 10.1021/Bi0301688  1
2003 Nikiforovich GV, Andersen NH, Fesinmeyer RM, Frieden C. Possible locally driven folding pathways of TC5b, a 20-residue protein Proteins: Structure, Function and Genetics. 52: 292-302. PMID 12833552 DOI: 10.1002/Prot.10409  1
2003 Vorobiev S, Strokopytov B, Drubin DG, Frieden C, Ono S, Condeelis J, Rubenstein PA, Almo SC. The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism. Proceedings of the National Academy of Sciences of the United States of America. 100: 5760-5. PMID 12732734 DOI: 10.1073/Pnas.0832273100  1
2002 Frieden C, Chattopadhyay K, Elson EL. What fluorescence correlation spectroscopy can tell us about unfolded proteins Advances in Protein Chemistry. 62: 91-109. PMID 12418102 DOI: 10.1016/S0065-3233(02)62006-6  1
2002 Chattopadhyay K, Saffarian S, Elson EL, Frieden C. Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 99: 14171-6. PMID 12381795 DOI: 10.1073/Pnas.172524899  1
2002 Nikiforovich GV, Frieden C. The search for local native-like nucleation centers in the unfolded state of β-sheet proteins Proceedings of the National Academy of Sciences of the United States of America. 99: 10388-10393. PMID 12140369 DOI: 10.1073/Pnas.162362199  1
2002 Chattopadhyay K, Zhong S, Yeh SR, Rousseau DL, Frieden C. The intestinal fatty acid binding protein: the role of turns in fast and slow folding processes. Biochemistry. 41: 4040-7. PMID 11900547 DOI: 10.1021/Bi012042L  1
2002 Bann JG, Pinkner J, Hultgren SJ, Frieden C. Real-time and equilibrium 19F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD Proceedings of the National Academy of Sciences of the United States of America. 99: 709-714. PMID 11792867 DOI: 10.1073/Pnas.022649599  1
2001 Frieden C, Huang ES, Ponder JW. Turn scanning. Experimental and theoretical approaches to the role of turns. Methods in Molecular Biology (Clifton, N.J.). 168: 133-158. PMID 11357623  1
2001 Hodsdon ME, Frieden C. Intestinal fatty acid binding protein: The folding mechanism as determined by NMR studies Biochemistry. 40: 732-742. PMID 11170390 DOI: 10.1021/Bi001518I  1
2000 Barnhart MM, Pinkner JS, Soto GE, Sauer FG, Langermann S, Waksman G, Frieden C, Hultgren SJ. PapD-like chaperones provide the missing information for folding of pilin proteins. Proceedings of the National Academy of Sciences of the United States of America. 97: 7709-14. PMID 10859353 DOI: 10.1073/Pnas.130183897  1
2000 Frieden C, Du J, Schriefer L, Buzan J. Purification and polymerization properties of two lethal yeast actin mutants Biochemical and Biophysical Research Communications. 271: 464-468. PMID 10799320 DOI: 10.1006/Bbrc.2000.2650  1
1999 Clark AC, Karon BS, Frieden C. Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL Protein Science. 8: 2166-2176. PMID 10548063 DOI: 10.1110/Ps.8.10.2166  1
1999 Buzan J, Du J, Karpova T, Frieden C. Histidine-tagged wild-type yeast actin: Its properties and use in an approach for obtaining yeast actin mutants Proceedings of the National Academy of Sciences of the United States of America. 96: 2823-2827. PMID 10077595 DOI: 10.1073/Pnas.96.6.2823  1
1999 Clark AC, Frieden C. The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases Journal of Molecular Biology. 285: 1777-1788. PMID 9917411 DOI: 10.1006/Jmbi.1998.2403  1
1999 Clark AC, Frieden C. Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures Journal of Molecular Biology. 285: 1765-1776. PMID 9917410 DOI: 10.1006/jmbi.1998.2402  1
1998 Kim K, Frieden C. Turn scanning by site-directed mutagenesis: Application to the protein folding problem using the intestinal fatty acid binding protein Protein Science. 7: 1821-1828. PMID 10082380 DOI: 10.1002/Pro.5560070818  1
1998 Corsico B, Cistola DP, Frieden C, Storch J. The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes Proceedings of the National Academy of Sciences of the United States of America. 95: 12174-12178. PMID 9770459 DOI: 10.1073/Pnas.95.21.12174  1
1998 Du J, Frieden C. Kinetic studies on the effect of yeast cofilin on yeast actin polymerization Biochemistry. 37: 13276-13284. PMID 9748335 DOI: 10.1021/Bi981117R  1
1998 Steele RA, Emmert DA, Kao J, Hodsdon ME, Frieden C, Cistola DP. The three-dimensional structure of a helix-less variant of intestinal fatty acid-binding protein Protein Science. 7: 1332-1339. PMID 9655337 DOI: 10.1002/Pro.5560070609  1
1998 Clark AC, Ramanathan R, Frieden C. Purification of GroEL with low fluorescence background Methods in Enzymology. 290: 100-118. PMID 9534154 DOI: 10.1016/S0076-6879(98)90010-6  1
1998 Hoeltzli SD, Frieden C. Refolding of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: A stopped-flow NMR spectroscopy study Biochemistry. 37: 387-398. PMID 9425060 DOI: 10.1021/Bi971962U  1
1997 Dang Q, Frieden C. New PC versions of the kinetic-simulation and fitting programs, KINSIM and FITSIM Trends in Biochemical Sciences. 22: 317. PMID 9270307 DOI: 10.1016/S0968-0004(97)01062-1  1
1997 Clark AC, Frieden C. GroEL-mediated folding of structurally homologous dihydrofolate reductases Journal of Molecular Biology. 268: 512-525. PMID 9159487 DOI: 10.1006/Jmbi.1997.0969  1
1997 Frieden C, Clark AC. Protein folding: How the mechanism of GroEL action is defined by kinetics Proceedings of the National Academy of Sciences of the United States of America. 94: 5535-5538. PMID 9159107 DOI: 10.1073/pnas.94.11.5535  1
1997 Kim K, Ramanathan R, Frieden C. Intestinal fatty acid binding protein: A specific residue in one turn appears to stabilize the native structure and be responsible for slow refolding Protein Science. 6: 364-372. PMID 9041638 DOI: 10.1002/Pro.5560060212  1
1996 Hoeltzli SD, Frieden C. Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy Biochemistry. 35: 16843-16851. PMID 8988023 DOI: 10.1021/Bi961896G  1
1996 Cistola DP, Kim K, Rogl H, Frieden C. Fatty acid interactions with a helix-less variant of intestinal fatty acid-binding protein Biochemistry. 35: 7559-7565. PMID 8652536 DOI: 10.1021/Bi952912X  1
1996 Kim K, Cistola DP, Frieden C. Intestinal fatty acid-binding protein: The structure and stability of a helix-less variant Biochemistry. 35: 7553-7558. PMID 8652535 DOI: 10.1021/Bi9529115  1
1996 Clark AC, Hugo E, Frieden C. Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL Biochemistry. 35: 5893-5901. PMID 8639551 DOI: 10.1021/bi953051v  1
1996 Buzan JM, Frieden C. Yeast actin: Polymerization kinetic studies of wild type and a poorly polymerizing mutant Proceedings of the National Academy of Sciences of the United States of America. 93: 91-95. PMID 8552682 DOI: 10.1073/Pnas.93.1.91  1
1995 Frieden C, Jiang N, Cistola DP. Intestinal fatty acid binding protein: folding of fluorescein-modified proteins. Biochemistry. 34: 2724-30. PMID 7873555 DOI: 10.1021/Bi00008A040  0.4
1995 Thomas JL, Frieden C, Nash WE, Strickler RC. An NADH-induced conformational change that mediates the sequential 3β- hydroxysteroid dehydrogenase/isomerase activities is supported by affinity labeling and the time-dependent activation of isomerase Journal of Biological Chemistry. 270: 21003-21008. PMID 7673125 DOI: 10.1074/Jbc.270.36.21003  1
1995 Kurz LC, Shah S, Frieden C, Nakra T, Stein RE, Drysdale GR, Evans CT, Srere PA. Catalytic strategy of citrate synthase: Subunit interactions revealed as a consequence of a single amino acid change in the oxaloacetate binding site Biochemistry. 34: 13278-13288. PMID 7577912 DOI: 10.1021/Bi00041A003  1
1995 Hoeltzli SD, Frieden C. Stopped-flow NMR spectroscopy: Real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase Proceedings of the National Academy of Sciences of the United States of America. 92: 9318-9322. PMID 7568125 DOI: 10.1073/Pnas.92.20.9318  1
1995 Frieden C. Intestinal fatty acid binding protein: Folding of fluorescein-modified proteins Biochemistry®. 34: 2724-2730.  1
1994 Kloek AP, Yang J, Mathews FS, Frieden C, Goldberg DE. The tyrosine B10 hydroxyl is crucial for oxygen avidity of Ascaris hemoglobin Journal of Biological Chemistry. 269: 2377-2379. PMID 8300562  1
1994 Hoeltzli SD, Frieden C. 19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: Equilibrium folding and ligand binding studies Biochemistry. 33: 5502-5509. PMID 8180172 DOI: 10.1021/Bi00184A019  1
1994 Frieden C. Numerical integration of rate equations by computer: an update Trends in Biochemical Sciences. 19: 181-182. PMID 8016870 DOI: 10.1016/0968-0004(94)90282-8  1
1994 Striker R, Jacob-Dubuisson F, Frieden C, Hultgren SJ. Stable fiber-forming and nonfiber-forming chaperone-subunit complexes in pilus biogenesis Journal of Biological Chemistry. 269: 12233-12239. PMID 7909317  1
1994 Frieden C. Analysis of kinetic data: Practical applications of computer simulation and fitting programs Methods in Enzymology. 240: 311-322. PMID 7823836 DOI: 10.1016/S0076-6879(94)40053-9  1
1993 Frieden C. Numerical integration of rate equations by computer. Trends in Biochemical Sciences. 18: 58-60. PMID 8488560 DOI: 10.1016/0968-0004(93)90056-S  1
1993 Neuwald AF, Krishnan BR, Ahrweiler PM, Frieden C, Berg DE. Conditional dihydrofolate reductase deficiency due to transposon Tn5tac1 insertion downstream from the folA gene in Escherichia coli. Gene. 125: 69-73. PMID 8383626 DOI: 10.1016/0378-1119(93)90747-Q  1
1993 Frieden C, Hoeltzli SD, Ropson IJ. NMR and protein folding: Equilibrium and stopped-flow studies Protein Science. 2: 2007-2014. PMID 8298453 DOI: 10.1002/Pro.5560021202  1
1993 Frieden C. Intestinal Fatty Acid Binding Protein: Characterization of Mutant Proteins Containing Inserted Cysteine Residues Biochemistry. 32: 11015-11021. PMID 8218166 DOI: 10.1021/Bi00092A010  1
1992 Kurz LC, Moix L, Riley MC, Frieden C. The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: Implications for the mechanism Biochemistry. 31: 39-48. PMID 1731884 DOI: 10.1021/Bi00116A008  1
1992 Ropson IJ, Frieden C. Dynamic NMR spectral analysis and protein folding: Identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by19F NMR Proceedings of the National Academy of Sciences of the United States of America. 89: 7222-7226. PMID 1496015 DOI: 10.1073/Pnas.89.15.7222  1
1992 Qian H, Elson EL, Frieden C. Studies on the structure of actin gels using time correlation spectroscopy of fluorescent beads Biophysical Journal. 63: 1000-1010. PMID 1420920 DOI: 10.1016/S0006-3495(92)81686-7  1
1991 Gordon JI, Sacchettini JC, Ropson IJ, Frieden C, Li E, Rubin DC, Roth KA, Cistola DP. Intracellular fatty-acid-binding proteins and their genes: Useful models for diverse biological questions Current Opinion in Lipidology. 2: 125-137. DOI: 10.1097/00041433-199104000-00011  1
1991 Frieden C. Effects of Point Mutations in a Hinge Region on the Stability, Folding, and Enzymatic Activity of Escherichia coli Dihydrofolate Reductase Biochemistry®. 30: 7801-7809.  1
1990 Ropson IJ, Gordon JI, Frieden C. Folding of a predominantly β-structure protein: Rat intestinal fatty acid binding protein Biochemistry. 29: 9591-9599. PMID 2271603 DOI: 10.1021/Bi00493A013  1
1990 Frieden C. Refolding of Escherichia coli dihydrofolate reductase: Sequential formation of substrate binding sites Proceedings of the National Academy of Sciences of the United States of America. 87: 4413-4416. PMID 2191290 DOI: 10.1073/Pnas.87.12.4413  1
1990 Cortese JD, Frieden C. Effect of filamin and controlled linear shear on the microheterogeneity of F-actin/gelsolin gels Cell Motility and the Cytoskeleton. 17: 236-249. PMID 2176572 DOI: 10.1002/Cm.970170310  1
1989 Zimmerle CT, Frieden C. Analysis of progress curves by simulations generated by numerical integration Biochemical Journal. 258: 381-387. PMID 2705989 DOI: 10.1042/Bj2580381  1
1989 Frieden C. The regulation of protein polymerization. Trends in Biochemical Sciences. 14: 283-6. PMID 2672450 DOI: 10.1016/0968-0004(89)90065-0  1
1989 Hall JG, Frieden C. Protein fragments as probes in the study of protein folding mechanisms: Differential effects of dihydrofolate reductase fragments on the refolding of the intact protein Proceedings of the National Academy of Sciences of the United States of America. 86: 3060-3064. PMID 2654934  1
1989 Cortese JD, Schwab B, Frieden C, Elson EL. Actin polymerization induces a shape change in actin-containing vesicles Proceedings of the National Academy of Sciences of the United States of America. 86: 5773-5777. PMID 2548187 DOI: 10.1073/Pnas.86.15.5773  1
1988 Frieden C, Patane K. Mechanism for nucleotide exchange in monomeric actin. Biochemistry. 27: 3812-20. PMID 3408729 DOI: 10.1021/Bi00410A044  1
1988 Ahrweiler PM, Frieden C. Construction of a fol mutant strain of Escherichia coli for use in dihydrofolate reductase mutagenesis experiments. Journal of Bacteriology. 170: 3301-4. PMID 3290203 DOI: 10.1128/Jb.170.7.3301-3304.1988  1
1988 Zimmerle CT, Frieden C. Effect of pH on the mechanism of actin polymerization. Biochemistry. 27: 7766-72. PMID 3207708 DOI: 10.1021/Bi00420A027  1
1988 Zimmerle CT, Frieden C. pH-induced changes in G-actin conformation and metal affinity. Biochemistry. 27: 7759-65. PMID 3207707 DOI: 10.1021/Bi00420A026  1
1988 Cortese JD, Frieden C. Microheterogeneity of actin gels formed under controlled linear shear. The Journal of Cell Biology. 107: 1477-87. PMID 2844828 DOI: 10.1083/Jcb.107.4.1477  1
1988 Cooper JA, Loftus DJ, Frieden C, Bryan J, Elson EL. Localization and mobility of gelsolin in cells. The Journal of Cell Biology. 106: 1229-40. PMID 2834402 DOI: 10.1083/Jcb.106.4.1229  1
1987 Kurz LC, Frieden C. Adenosine deaminase converts purine riboside into an analogue of a reactive intermediate: a 13C NMR and kinetic study. Biochemistry. 26: 8450-7. PMID 3442668 DOI: 10.1021/Bi00399A063  1
1987 Zimmerle CT, Patane K, Frieden C. Divalent cation binding to the high- and low-affinity sites on G-actin. Biochemistry. 26: 6545-52. PMID 3427024 DOI: 10.1021/Bi00394A039  1
1987 Penner MH, Frieden C. Kinetic analysis of the mechanism of Escherichia coli dihydrofolate reductase. The Journal of Biological Chemistry. 262: 15908-14. PMID 3316211  1
1987 Cooper JA, Bryan J, Schwab B, Frieden C, Loftus DJ, Elson EL. Microinjection of gelsolin into living cells Journal of Cell Biology. 104: 491-501. PMID 3029140 DOI: 10.1083/Jcb.104.3.491  1
1986 Goddette DW, Uberbacher EC, Bunick GJ, Frieden C. Formation of actin dimers as studied by small angle neutron scattering Journal of Biological Chemistry. 261: 2605-2609. PMID 3949737  1
1986 Goddette DW, Frieden C. The kinetics of cytochalasin D binding to monomeric actin Journal of Biological Chemistry. 261: 15970-15973. PMID 3782101  1
1986 Goddette DW, Frieden C. Actin polymerization. The mechanism of action of cytochalasin D Journal of Biological Chemistry. 261: 15974-15980. PMID 3023337  1
1986 Zimmerle CT, Frieden C. Effect of temperature on the mechanism of actin polymerization Biochemistry. 25: 6432-6438. DOI: 10.1021/Bi00369A014  1
1985 Frieden C, Patane K. Differences in G-actin containing bound ATP or ADP: The Mg2+-induced conformational change requires ATP Biochemistry. 24: 4192-4196. PMID 4052388 DOI: 10.1021/Bi00336A056  1
1985 Goddette DW, Frieden C. The binding of cytochalasin D to monomeric actin Biochemical and Biophysical Research Communications. 128: 1087-1092. PMID 4004848 DOI: 10.1016/0006-291X(85)91051-4  1
1985 Kurz LC, LaZard D, Frieden C. Protein structural changes accompanying formation of enzymatic transition states: Tryptophan environment in ground-state and transition-state analogue complexes of adenosine deaminase Biochemistry. 24: 1342-1346. PMID 3986181 DOI: 10.1021/Bi00327A011  1
1985 Arakawa T, Frieden C. The use of the fluorescence photobleaching recovery technique to study the self-assembly of tubulin Analytical Biochemistry. 146: 134-142. PMID 3922241 DOI: 10.1016/0003-2697(85)90407-5  1
1985 Frieden C. Actin and tubulin polymerization: the use of kinetic methods to determine mechanism Annual Review of Biophysics and Biophysical Chemistry. 14: 189-210. PMID 3890879  1
1985 Penner MH, Frieden C. Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase Journal of Biological Chemistry. 260: 5366-5369. PMID 3886655  1
1985 Penner M, Frieden C. Hysteretic behavior of E. coli dihydrofolate reductase Federation Proceedings. 44: No. 8171.  1
1984 Doi Y, Frieden C. Actin polymerization. The effect of brevin on filament size and rate of polymerization Journal of Biological Chemistry. 259: 11868-11875. PMID 6480587  1
1984 Arakawa T, Frieden C. Interaction of microtubule-associated protein with actin filaments. Studies using the fluorescence-photobleaching recovery technique Journal of Biological Chemistry. 259: 11730-11734. PMID 6480581  1
1984 Barshop BA, Frieden C. Analysis of the interaction of rabbit skeletal muscle adenylate deaminase with myosin subfragments. A kinetically regulated system Journal of Biological Chemistry. 259: 60-66. PMID 6368542  1
1984 Goddette DW, Frieden C. Cytochalasin D binds to the Mg2+-induced conformational form of monomeric G-actin Federation Proceedings. 43: no. 2535.  1
1983 Gilbert HR, Frieden C. Preparation, purification and properties of a crosslinked trimer of G-actin Biochemical and Biophysical Research Communications. 111: 404-408. PMID 6838567 DOI: 10.1016/0006-291X(83)90320-0  1
1983 Kurz LC, Frieden C. Adenosine deaminase: Solvent isotope and pH effects on the binding of transition-state and ground-state analogue inhibitors Biochemistry. 22: 382-389. PMID 6824635 DOI: 10.1021/Bi00271A023  1
1983 Barshop BA, Wrenn RF, Frieden C. Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM-A flexible, portable system Analytical Biochemistry. 130: 134-145. PMID 6688159 DOI: 10.1016/0003-2697(83)90660-7  1
1983 Frieden C, Goddette DW. Polymerization of actin and actin-like systems: Evaluation of the time course of polymerization in relation to the mechanism Biochemistry. 22: 5836-5843. PMID 6661414 DOI: 10.1021/Bi00294A023  1
1983 Frieden C. Polymerization of actin: Mechanism of the Mg2+-induced process at pH 8 and 20°C Proceedings of the National Academy of Sciences of the United States of America. 80: 6513-6517. PMID 6579538 DOI: 10.1073/Pnas.80.21.6513  1
1982 Tait JF, Frieden C. Chemical modification of actin. Acceleration of polymerization and reduction of network formation by reaction with N-ethylmaleimide, (iodoacetamido)tetramethylrhodamine, or 7-chloro-4-nitro-2,13-benzoxadiazole Biochemistry. 21: 6046-6053. PMID 7150541 DOI: 10.1021/Bi00267A004  1
1982 Tait JF, Frieden C. Polymerization and gelation of actin studied by fluorescence photobleaching recovery Biochemistry. 21: 3666-3674. PMID 7115692 DOI: 10.1021/Bi00258A022  1
1982 Tait JF, Frieden C. Polymerization-induced changes in the fluorescence of actin labeled with iodoacetamidotetramethylrhodamine Archives of Biochemistry and Biophysics. 216: 133-141. PMID 7103505 DOI: 10.1016/0003-9861(82)90197-7  1
1982 Frieden C. The Mg2+-induced conformational change in rabbit skeletal muscle G-actin Journal of Biological Chemistry. 257: 2882-2886. PMID 7061452  1
1982 Tellam R, Frieden C. Cytochalasin D and platelet gelsolin accelerate actin polymer formation. A model for regulation of the extent of actin polymer formation in vivo Biochemistry. 21: 3207-3214. PMID 6285961 DOI: 10.1021/Bi00256A027  1
1981 Holden HM, Banaszak LJ, Frieden C, McLoughlin DJ. Differences in the binding of coenzyme to L-3-hydroxyacyl-coenzyme A dehydrogenase in the crystalline state and in solution. Febs Letters. 132: 15-8. PMID 7297684 DOI: 10.1016/0014-5793(81)80417-6  1
1981 Tellam R, Frieden C. The purification and properties of frog skeletal muscle phosphofructokinase Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 69: 517-522. DOI: 10.1016/0305-0491(81)90344-8  1
1980 Frieden C, Kurz LC, Gilbert HR. Adenosine deaminase and adenylate deaminase: Comparative kinetic studies with transition state and ground state analogue inhibitors Biochemistry. 19: 5303-5309. PMID 7448172 DOI: 10.1021/Bi00564A024  1
1980 Birktoft JJ, Miake F, Frieden C, Banaszak LJ. Crystallographic studies of glutamate dehydrogenase. II. Preliminary crystal data for the tuna liver enzyme. Journal of Molecular Biology. 138: 145-8. PMID 7411604 DOI: 10.1016/S0022-2836(80)80010-6  1
1980 Koretz JF, Frieden C. Adenylate deaminase binding to synthetic thick filaments of myosin Proceedings of the National Academy of Sciences of the United States of America. 77: 7186-7188. PMID 6938963 DOI: 10.1073/Pnas.77.12.7186  1
1980 Frieden C, Lieberman D, Gilbert HR. A fluorescent probe for conformational changes in skeletal muscle G-actin Journal of Biological Chemistry. 255: 8991-8993. PMID 6893329  1
1980 Kurz LC, Frieden C. Anomalous equilibrium and kinetic α-deuterium secondary isotope effects accompanying hydride transfer from reduced. Nicotinamide adenine dinucleotide Journal of the American Chemical Society. 102: 4198-4203.  1
1979 Frieden C, Gilbert HR, Miller WH, Miller RL. Adenylate deaminase: Potent inhibition by 2′-deoxycoformycin 5′-phosphate Biochemical and Biophysical Research Communications. 91: 278-283. PMID 518627 DOI: 10.1016/0006-291X(79)90614-4  1
1979 Shumate JB, Katnik R, Ruiz M, Kaiser K, Frieden C, Brooke MH, Carroll JE. Myoadenylate deaminase deficiency Muscle and Nerve. 2: 213-216. PMID 503106 DOI: 10.1002/Mus.880020309  1
1979 Birktoft JJ, Miake F, Banaszak LJ, Frieden C. Crystallographic studies of glutamate dehydrogenase. Preliminary crystal data. The Journal of Biological Chemistry. 254: 4915-8. PMID 438222  1
1979 Frieden C. Slow transitions and hysteretic behavior in enzymes Annual Review of Biochemistry. 48: 471-489. PMID 382990 DOI: 10.1146/Annurev.Bi.48.070179.002351  1
1979 Ashby B, Frieden C, Bischoff R. Immunofluorescent and histochemical localization of AMP deaminase in skeletal muscle Journal of Cell Biology. 81: 361-373. PMID 381318 DOI: 10.1083/Jcb.81.2.361  1
1979 Pettigrew DW, Frieden C. Rabbit muscle phosphofructokinase. A model for regulatory kinetic behavior Journal of Biological Chemistry. 254: 1896-1901. PMID 154516  1
1979 Pettigrew DW, Frieden C. Binding of regulatory ligands to rabbit muscle phosphofructokinase. A model for nucleotide binding as a function of temperature and pH Journal of Biological Chemistry. 254: 1887-1895. PMID 33988  1
1978 Ashby B, Frieden C. Adenylate deaminase. Kinetic and binding studies on the rabbit muscle enzyme Journal of Biological Chemistry. 253: 8728-8735. PMID 721807  1
1978 Frieden C, Honegger J, Gilbert HR. Malate dehydrogenases. The lack of evidence for dissociation of the dimeric enzyme in kinetic analyses Journal of Biological Chemistry. 253: 816-820. PMID 563864  1
1978 Pettigrew DW, Frieden C. Rabbit muscle phosphofructokinase. Modification of molecular and regulatory kinetic properties with the affinity label 5'-p-(fluorosulfonyl)benzoyl adenosine Journal of Biological Chemistry. 253: 3623-3627. PMID 148461  1
1978 Bock PE, Frieden C. Another look at the cold lability of enzymes Trends in Biochemical Sciences. 3: 100-103. DOI: 10.1016/S0968-0004(78)80013-9  1
1977 Pettigrew DW, Frieden C. Treatment of enzyme kinetic data: extension of the concerted allosteric model to the two substrate case Journal of Biological Chemistry. 252: 4546-4551. PMID 873905  1
1977 Ashby B, Frieden C. Interaction of AMP aminohydrolase with myosin and its subfragments Journal of Biological Chemistry. 252: 1869-1872. PMID 321446  1
1977 Kurz LC, Frieden C. Comparison of the structures of enzymatic and nonenzymatic transition states. Reductive desulfonation of 4-X-2,6-dinitrobenzenesulfonates by reduced nicotinamide adenine dinucleotide Biochemistry. 16: 5207-5216. PMID 200257 DOI: 10.1021/Bi00643A008  1
1976 Frieden C. On the kinetic distinction of ordered and random bireactant enzyme systems Biochemical and Biophysical Research Communications. 68: 914-917. PMID 1259739 DOI: 10.1016/0006-291X(76)91232-8  1
1976 Frieden C, Gilbert HR, Bock PE. Phosphofructokinase. III. Correlation of the regulatory kinetic and molecular properties of the rabbit muscle enzyme Journal of Biological Chemistry. 251: 5644-5647. PMID 9395  1
1976 Bock PE, Frieden C. Phosphofructokinase. II. Role of ligands in pH dependent structural changes of the rabbit muscle enzyme Journal of Biological Chemistry. 251: 5637-5643. PMID 9394  1
1976 Bock PE, Frieden C. Phosphofructokinase. I. Mechanism of the pH dependent inactivation and reactivation of the rabbit muscle enzyme Journal of Biological Chemistry. 251: 5630-5636. PMID 9393  1
1975 Kurz LC, Frieden C. Letter: A model dehydrogenase reaction. Charge distribution in the transition state Journal of the American Chemical Society. 97: 676-679. PMID 1133370 DOI: 10.1021/Ja00836A055  1
1975 Bock PE, Gilbert HR, Frieden C. Analysis of the cold lability behavior of rabbit muscle phosphofructokinase Biochemical and Biophysical Research Communications. 66: 564-569. PMID 241341 DOI: 10.1016/0006-291X(75)90547-1  1
1975 Emerk K, Frieden C. Rabbit muscle phosphofructokinase: The effect of the state of the enzyme and assay procedure on the kinetic properties Archives of Biochemistry and Biophysics. 168: 210-218. PMID 237475 DOI: 10.1016/0003-9861(75)90243-X  1
1975 Frieden C, Fernandez Sousa J. Kinetic studies on pig heart cytoplasmic malate dehydrogenase Journal of Biological Chemistry. 250: 2106-2111. PMID 234957  1
1975 Kurz LC, Frieden C. A model dehydrogenase reaction. Charge distribution in the transition state [28] Journal of the American Chemical Society. 97: 677-679.  1
1975 Frieden C. The use of full time course experiments in the determination of rate constants for an ordered two substrate reaction Journal of Biological Chemistry. 250: 2111-2113.  1
1974 Emerk K, Frieden C. The effect of trypsin treatment on rabbit muscle phosphofructokinase Archives of Biochemistry and Biophysics. 164: 233-240. PMID 4372946 DOI: 10.1016/0003-9861(74)90027-7  1
1974 Bock PE, Frieden C. pH-induced cold lability of rabbit skeletal muscle phosphofructokinase Biochemistry. 13: 4191-4196. PMID 4277765 DOI: 10.1021/Bi00717A020  1
1973 Bates DJ, Frieden C. Treatment of enzyme kinetic data. 3. The use of the full time course of a reaction, as examined by computer simulation, in defining enzyme mechanisms. The Journal of Biological Chemistry. 248: 7878-84. PMID 4796073  1
1973 Bates DJ, Frieden C. A small computer system for the routine analysis of enzyme kinetic mechanisms. Computers and Biomedical Research, An International Journal. 6: 474-86. PMID 4747108 DOI: 10.1016/0010-4809(73)90080-3  1
1973 Coffee CJ, Aaronson RP, Frieden C. Rabbit muscle phosphofructokinase: studies of the subunit molecular weight and structure. Isolation of carboxymethylated cysteinyl peptides and sedimentation equilibrium studies Journal of Biological Chemistry. 248: 1381-1387. PMID 4265645  1
1973 Bates DJ, Frieden C. Full time course studies on the oxidation of reduced coenzyme by bovine liver glutamate dehydrogenase. Use of computer simulation to obtain rate and dissociation constants. The Journal of Biological Chemistry. 248: 7885-90. PMID 4147984  1
1972 Huang CY, Frieden C. The mechanism of ligand-induced structural changes in glutamate dehydrogenase. Studies of the rate of depolymerization and isomerization effected by coenzymes and guanine nucleotides Journal of Biological Chemistry. 247: 3638-3646. PMID 4402280  1
1972 Goldin BR, Frieden C. The effect of pyridoxal phosphate modification on the catalytic and regulatory properties of bovine liver glutamate dehydrogenase Journal of Biological Chemistry. 247: 2139-2144. PMID 4335864  1
1972 Aaronson RP, Frieden C. Rabbit muscle phosphofructokinase: studies on the polymerization. The behavior of the enzyme at pH 8, pH 6, and intermediate pH values Journal of Biological Chemistry. 247: 7502-7509. PMID 4264130  1
1971 Goldin BR, Frieden C. Effect of trinitrophenylation of specific lysyl residues on the catalytic, regulatory, and molecular properties of bovine liver glutamate dehydrogenase Biochemistry. 10: 3527-3534. PMID 4401723  1
1971 Frieden C. Protein-protein interaction and enzymatic activity Annual Review of Biochemistry. 40: 653-696. PMID 4399448 DOI: 10.1146/Annurev.Bi.40.070171.003253  1
1971 Coffee CJ, Bradshaw RA, Goldin BR, Frieden C. Identification of the sites of modification of bovine liver glutamate dehydrogenase reacted with trinitrobenzenesulfonate Biochemistry. 10: 3516-3526. PMID 4336413  1
1970 King KS, Frieden C. The purification and physical properties of glutamate dehydrogenase from rat liver Journal of Biological Chemistry. 245: 4391-4396. PMID 5498427  1
1970 Frieden C. Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept Journal of Biological Chemistry. 245: 5788-5799. PMID 5472372  1
1970 Bates DJ, Goldin BR, Frieden C. A new reaction of glutamate dehydrogenase: the enzyme-catalyzed formation of trinitrobenzene from TNBS in the presence of reduced coenzyme. Biochemical and Biophysical Research Communications. 39: 502-7. PMID 4393049 DOI: 10.1016/0006-291X(70)90606-6  1
1969 Huang CY, Frieden C. Rates of GDP-induced and GTP-induced depolymerization of glutamate dehydrogenase: a possible factor in metabolic regulation Proceedings of the National Academy of Sciences of the United States of America. 64: 338-344. PMID 4312753 DOI: 10.1073/Pnas.64.1.338  1
1968 Sedgwick KA, Frieden C. The molecular weight and some kinetic properties of crystalline rat liver glutamate dehydrogenase Biochemical and Biophysical Research Communications. 32: 392-397. PMID 4386283 DOI: 10.1016/0006-291X(68)90673-6  1
1967 Frieden C. Treatment of enzyme kinetic data. II. The multisite case: comparison of allosteric models and a possible new mechanism Journal of Biological Chemistry. 242: 4045-4052. PMID 6061697  1
1967 Frieden C, Colman RF. Glutamate dehydrogenase concentration as a determinant in the effect of purine nucleotides on enzymatic activity. The Journal of Biological Chemistry. 242: 1705-15. PMID 4381598  1
1966 Colman RF, Frieden C. On the role of amino groups in the structure and function of glutamate dehydrogenase. II. Effect of acetylation on molecular properties. The Journal of Biological Chemistry. 241: 3661-70. PMID 4288133  1
1966 Colman RF, Frieden C. On the role of amino groups in the structure and function of glutamate dehydrogenase. I. Effect of acetylation on catalytic and regulatory properties. The Journal of Biological Chemistry. 241: 3652-60. PMID 4288132  1
1966 Colman RF, Frieden C. Cooperative interaction between the GTP binding sites of glutamate dehydrogenase. Biochemical and Biophysical Research Communications. 22: 100-5. PMID 4287088 DOI: 10.1016/0006-291X(66)90609-7  1
1963 Frieden C. Different structural forms of reversibly dissociated glutamic dehydrogenase: Relation between enzymatic activity and molecular weight Biochemical and Biophysical Research Communications. 10: 410-415. DOI: 10.1016/0006-291X(63)90547-3  1
1957 FRIEDEN C, VELICK SF. Imino acid as the intermediate in the L-amino acid oxidase reaction. Biochimica Et Biophysica Acta. 23: 439-40. PMID 13412747 DOI: 10.1016/0006-3002(57)90354-2  1
1955 FRIEDEN C, ALBERTY RA. The effect of pH on fumarase activity in acetate buffer. The Journal of Biological Chemistry. 212: 859-68. PMID 14353887  0.96
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