| Year |
Citation |
Score |
| 2023 |
Stuchell-Brereton MD, Zimmerman MI, Miller JJ, Mallimadugula UL, Incicco JJ, Roy D, Smith LG, Cubuk J, Baban B, DeKoster GT, Frieden C, Bowman GR, Soranno A. Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms. Proceedings of the National Academy of Sciences of the United States of America. 120: e2215371120. PMID 36749730 DOI: 10.1073/pnas.2215371120 |
0.766 |
|
| 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 |
0.72 |
|
| 2020 |
Chinnaraj M, Barrios DA, Frieden C, Heyduk T, Flaumenhaft R, Pozzi N. Bioorthogonal Chemistry Enables Single-Molecule FRET Measurements of Catalytically Active Protein Disulfide Isomerase. Chembiochem : a European Journal of Chemical Biology. PMID 32857455 DOI: 10.1002/Cbic.202000537 |
0.324 |
|
| 2020 |
Ruben EA, Gandhi PS, Chen Z, Koester SK, DeKoster GT, Frieden C, Di Cera E. 19F NMR reveals the conformational properties of free thrombin and its zymogen precursor prethrombin-2. The Journal of Biological Chemistry. PMID 32358061 DOI: 10.1074/Jbc.Ra120.013419 |
0.647 |
|
| 2020 |
Stuchell-Brereton MD, Calderone L, Baban B, Cubuk J, DeKoster G, Frieden C, Soranno A. Single-Molecule Fluorescence Spectroscopy of Non-Lipidated Forms of Apolipoprotein E Biophysical Journal. 118: 192a. DOI: 10.1016/J.Bpj.2019.11.1165 |
0.746 |
|
| 2019 |
Wang H, Eschweiler J, Cui W, Zhang H, Frieden C, Ruotolo BT, Gross ML. Native Mass Spectrometry, Ion Mobility, Electron-Capture Dissociation, and Modeling Provide Structural Information for Gas-Phase Apolipoprotein E Oligomers. Journal of the American Society For Mass Spectrometry. PMID 30887458 DOI: 10.1007/S13361-019-02148-Z |
0.332 |
|
| 2019 |
Frieden C. Protein oligomerization as a metabolic control mechanism. Application to apoE. Protein Science : a Publication of the Protein Society. PMID 30701627 DOI: 10.1002/Pro.3583 |
0.316 |
|
| 2018 |
Klein RD, Shu Q, Cusumano ZT, Nagamatsu K, Gualberto NC, Lynch AJL, Wu C, Wang W, Jain N, Pinkner JS, Amarasinghe GK, Hultgren SJ, Frieden C, Chapman MR. Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation. Mbio. 9. PMID 30018113 DOI: 10.1128/Mbio.01349-18 |
0.344 |
|
| 2017 |
Wang H, Shu Q, Rempel DL, Frieden C, Gross ML. Understanding Curli Amyloid-Protein Aggregation by Hydrogen-Deuterium Exchange and Mass Spectrometry. International Journal of Mass Spectrometry. 420: 16-23. PMID 29056864 DOI: 10.1016/J.Ijms.2016.10.006 |
0.313 |
|
| 2017 |
Wang H, Rempel DL, Giblin DE, Frieden C, Gross ML. Peptide-level interactions between proteins and small-molecule drug candidates by HDX-MS, PLIMSTEX and modified SUPREX: the example of ApoE3. Analytical Chemistry. PMID 28901129 DOI: 10.1021/Acs.Analchem.7B01121 |
0.325 |
|
| 2017 |
Frieden C, Wang H, Ho CMW. A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions. Proceedings of the National Academy of Sciences of the United States of America. PMID 28559318 DOI: 10.1073/Pnas.1705080114 |
0.338 |
|
| 2017 |
Wang H, Shu Q, Frieden C, Gross ML. Deamidation slows Curli Amyloid-Protein Aggregation. Biochemistry. PMID 28497950 DOI: 10.1021/Acs.Biochem.7B00241 |
0.371 |
|
| 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 |
0.358 |
|
| 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 |
0.346 |
|
| 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 |
0.319 |
|
| 2015 |
Frieden C. ApoE: the role of conserved residues in defining function. Protein Science : a Publication of the Protein Society. 24: 138-44. PMID 25377861 DOI: 10.1002/Pro.2597 |
0.336 |
|
| 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 |
0.358 |
|
| 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 |
0.758 |
|
| 2013 |
Frieden C, Garai K. Concerning the structure of apoE Protein Science. 22: 1820-1825. PMID 24115173 DOI: 10.1002/Pro.2379 |
0.34 |
|
| 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 |
0.353 |
|
| 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 |
0.73 |
|
| 2013 |
Garai K, Frieden C. Determination of the Rate Constants of Oligomerization of Amyloid-β Peptides using Fluorescence Quenching of Tetramethylrhodamine Biophysical Journal. 104: 56a. DOI: 10.1016/J.Bpj.2012.11.349 |
0.359 |
|
| 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 |
0.347 |
|
| 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 |
0.732 |
|
| 2012 |
Garai K, Frieden C. Modulation of Amyloid Beta Peptide Aggregation by Apolipoprotein E Isoforms Biophysical Journal. 102: 256a. DOI: 10.1016/J.Bpj.2011.11.1412 |
0.363 |
|
| 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 |
0.351 |
|
| 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 |
0.352 |
|
| 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 |
0.327 |
|
| 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 |
0.355 |
|
| 2011 |
Garai K, Frieden C. Association-Dissociation Behavior of the Apolipoprotein E Proteins: Implications for Lipid Binding Biophysical Journal. 100: 510a. DOI: 10.1016/J.Bpj.2010.12.2986 |
0.342 |
|
| 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 |
0.381 |
|
| 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 |
0.349 |
|
| 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 |
0.363 |
|
| 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 |
0.721 |
|
| 2010 |
Gleick PH, Adams RM, Amasino RM, Anders E, Anderson DJ, Anderson WW, Anselin LE, Arroyo MK, Asfaw B, Ayala FJ, Bax A, Bebbington AJ, Bell G, Bennett MV, Bennetzen JL, ... ... Frieden C, et al. Climate change and the integrity of science. Science (New York, N.Y.). 328: 689-90. PMID 20448167 DOI: 10.1126/Science.328.5979.689 |
0.414 |
|
| 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 |
0.352 |
|
| 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 |
0.761 |
|
| 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 |
0.323 |
|
| 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 |
0.737 |
|
| 2009 |
Lee J, Crick S, Pappu R, Frieden C, Hu X. P1-004: Amyloid seeds formed by cellular uptake, concentration, and aggergation of the Abeta1-42
peptide Alzheimer's & Dementia. 5: P173-P173. DOI: 10.1016/J.Jalz.2009.04.007 |
0.747 |
|
| 2007 |
Frieden C. Protein aggregation processes: In search of the mechanism Protein Science. 16: 2334-2344. PMID 17962399 DOI: 10.1110/Ps.073164107 |
0.366 |
|
| 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 |
0.388 |
|
| 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 |
0.301 |
|
| 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 |
0.766 |
|
| 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 |
0.365 |
|
| 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 |
0.658 |
|
| 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 |
0.374 |
|
| 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 |
0.359 |
|
| 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 |
0.738 |
|
| 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 |
0.331 |
|
| 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 |
0.729 |
|
| 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 |
0.348 |
|
| 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 |
0.304 |
|
| 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 |
0.309 |
|
| 2003 |
Frieden C. The Kinetics of Side Chain Stabilization during Protein Folding Biochemistry. 42: 12439-12446. PMID 14580188 DOI: 10.1021/Bi030192L |
0.333 |
|
| 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 |
0.359 |
|
| 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 |
0.33 |
|
| 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 |
0.718 |
|
| 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 |
0.732 |
|
| 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 |
0.368 |
|
| 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 |
0.656 |
|
| 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 |
0.321 |
|
| 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 |
0.387 |
|
| 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 |
0.35 |
|
| 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 |
0.339 |
|
| 1998 |
FRIEDEN C. Coenzyme binding, observed by fluorescence enhancement, apparently unrelated to the enzymic activity of glutamic dehydrogenase. Biochimica Et Biophysica Acta. 47: 428-30. PMID 13701959 DOI: 10.1016/0006-3002(61)90316-X |
0.313 |
|
| 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 |
0.376 |
|
| 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 |
0.314 |
|
| 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 |
0.311 |
|
| 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 |
0.374 |
|
| 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 |
0.39 |
|
| 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 |
0.378 |
|
| 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 |
0.586 |
|
| 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 |
0.337 |
|
| 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 |
0.362 |
|
| 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 |
0.578 |
|
| 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 |
0.307 |
|
| 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 |
0.377 |
|
| 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 |
0.337 |
|
| 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 |
0.349 |
|
| 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 |
0.344 |
|
| 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 |
0.313 |
|
| 1994 |
Hoeltzli SD, Ropson IJ, Frieden C. Application of Equilibrium and Stopped-Flow 19F NMR Spectroscopy to Protein Folding: Studies of E. coli Dihydrofolate Reductase Techniques in Protein Chemistry. 5: 455-465. DOI: 10.1016/B978-0-12-194710-1.50056-4 |
0.32 |
|
| 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 |
0.336 |
|
| 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 |
0.376 |
|
| 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 |
0.389 |
|
| 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 |
0.559 |
|
| 1992 |
Ropson IJ, Gordon JI, Cistola DP, Frieden C. Stopped-Flow Circular Dichroism And 19F Nmr As Probes For The Folding Of Rat Intestinal Fatty-Acid Binding Protein (Ifabp) Techniques in Protein Chemistry. 437-443. DOI: 10.1016/B978-0-12-058756-8.50049-3 |
0.372 |
|
| 1991 |
Ahrweiler PM, Frieden C. Effects of point mutations in a hinge region on the stability, folding, and enzymatic activity of Escherichia coli dihydrofolate reductase. Biochemistry. 30: 7801-9. PMID 1868058 DOI: 10.1021/Bi00245A020 |
0.353 |
|
| 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 |
0.371 |
|
| 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 |
0.381 |
|
| 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 |
0.54 |
|
| 1988 |
Frieden C, Patane K. Mechanism for nucleotide exchange in monomeric actin. Biochemistry. 27: 3812-20. PMID 3408729 DOI: 10.1021/Bi00410A044 |
0.313 |
|
| 1988 |
Zimmerle CT, Frieden C. Effect of pH on the mechanism of actin polymerization. Biochemistry. 27: 7766-72. PMID 3207708 DOI: 10.1021/Bi00420A027 |
0.324 |
|
| 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 |
0.35 |
|
| 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 |
0.303 |
|
| 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 |
0.628 |
|
| 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 |
0.318 |
|
| 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 |
0.325 |
|
| 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 |
0.618 |
|
| 1986 |
Zimmerle CT, Frieden C. Effect of temperature on the mechanism of actin polymerization Biochemistry. 25: 6432-6438. DOI: 10.1021/Bi00369A014 |
0.321 |
|
| 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 |
0.313 |
|
| 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 |
0.329 |
|
| 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 |
0.33 |
|
| 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 |
0.319 |
|
| 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 |
0.301 |
|
| 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 |
0.311 |
|
| 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 |
0.306 |
|
| 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 |
0.311 |
|
| 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 |
0.317 |
|
| 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 |
0.333 |
|
| 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 |
0.596 |
|
| 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 |
0.627 |
|
| 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 |
0.322 |
|
| 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 |
0.308 |
|
| 1974 |
Bock PE, Frieden C. pH-induced cold lability of rabbit skeletal muscle phosphofructokinase Biochemistry. 13: 4191-4196. PMID 4277765 DOI: 10.1021/Bi00717A020 |
0.58 |
|
| 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 |
0.304 |
|
| 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 |
0.448 |
|
| 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 |
0.451 |
|
| 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 |
0.449 |
|
| 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 |
0.502 |
|
| 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 |
0.644 |
|
| 1957 |
Frieden C, Wolfe RG, Alberty RA. Studies of the enzyme fumarase. IV. The dependence of the kinetic constants at 25° on buffer concentration, composition and pH Journal of the American Chemical Society. 79: 1523-1525. DOI: 10.1021/Ja01564A001 |
0.533 |
|
| 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 |
0.444 |
|
| 1955 |
Fisher HF, Frieden C, McKee JSM, Alberty RA. CONCERNING THE STEREOSPECIFICITY OF THE FUMARASE REACTION AND THE DEMONSTRATION OF A NEW INTERMEDIATE1 Journal of the American Chemical Society. 77: 4436-4436. DOI: 10.1021/Ja01621A091 |
0.474 |
|
| 1954 |
Alberty RA, Massey V, Frieden C, Fuhlbrigge AR. Studies of the Enzyme Fumarase. III.1The Dependence of the Kinetic Constants at 25° upon the Concentration and pH of Phosphate Buffers Journal of the American Chemical Society. 76: 2485-2493. DOI: 10.1021/Ja01638A053 |
0.637 |
|
| 1954 |
Frieden C, Bock RM, Alberty RA. Studies of the Enzyme Fumarase. II.1Isolation and Physical Properties of Crystalline Enzyme Journal of the American Chemical Society. 76: 2482-2484. DOI: 10.1021/Ja01638A052 |
0.646 |
|
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