| Year |
Citation |
Score |
| 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 |
0.33 |
|
| 2018 |
Heyduk E, Heyduk T. DNA template sequence control of bacterial RNA polymerase escape from the promoter. Nucleic Acids Research. PMID 29546317 DOI: 10.1093/Nar/Gky172 |
0.471 |
|
| 2017 |
Feklistov A, Bae B, Hauver J, Lass-Napiorkowska A, Kalesse M, Glaus F, Altmann KH, Heyduk T, Landick R, Darst SA. RNA polymerase motions during promoter melting. Science (New York, N.Y.). 356: 863-866. PMID 28546214 DOI: 10.1126/Science.Aam7858 |
0.491 |
|
| 2016 |
Lass-Napiorkowska A, Heyduk T. Real-time observation of backtracking by bacterial RNA polymerase. Biochemistry. PMID 26745324 DOI: 10.1021/Acs.Biochem.5B01184 |
0.556 |
|
| 2015 |
Heyduk T, Heyduk E. Next Generation Sequencing-based analysis of RNA polymerase functions. Methods (San Diego, Calif.). 86: 37-44. PMID 25937393 DOI: 10.1016/J.Ymeth.2015.04.030 |
0.467 |
|
| 2014 |
Ko J, Heyduk T. Kinetics of promoter escape by bacterial RNA polymerase: effects of promoter contacts and transcription bubble collapse. The Biochemical Journal. 463: 135-44. PMID 24995916 DOI: 10.1042/Bj20140179 |
0.74 |
|
| 2014 |
Heyduk E, Heyduk T. Next generation sequencing-based parallel analysis of melting kinetics of 4096 variants of a bacterial promoter. Biochemistry. 53: 282-92. PMID 24359527 DOI: 10.1021/Bi401277W |
0.458 |
|
| 2013 |
Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation. The Journal of Biological Chemistry. 288: 22734-44. PMID 23775088 DOI: 10.1074/Jbc.M113.466946 |
0.306 |
|
| 2012 |
Lass-Napiorkowska A, Heyduk E, Tian L, Heyduk T. Detection methodology based on target molecule-induced sequence-specific binding to a single-stranded oligonucleotide. Analytical Chemistry. 84: 3382-9. PMID 22401560 DOI: 10.1021/Ac3001034 |
0.551 |
|
| 2011 |
Sztiller-Sikorska M, Heyduk E, Heyduk T. Promoter spacer DNA plays an active role in integrating the functional consequences of RNA polymerase contacts with -10 and -35 promoter elements. Biophysical Chemistry. 159: 73-81. PMID 21621902 DOI: 10.1016/J.Bpc.2011.05.008 |
0.498 |
|
| 2011 |
Heyduk E, Lass A, Tian L, Heyduk T. Heterogeneous Immunosensors that Do not Require Protein Immobilization Biophysical Journal. 100: 485a. DOI: 10.1016/J.Bpj.2010.12.2844 |
0.498 |
|
| 2010 |
Heyduk E, Heyduk T. Fluorescent homogeneous immunosensors for detecting pathogenic bacteria. Analytical Biochemistry. 396: 298-303. PMID 19782039 DOI: 10.1016/J.Ab.2009.09.039 |
0.356 |
|
| 2009 |
Tian L, Heyduk T. Antigen peptide-based immunosensors for rapid detection of antibodies and antigens. Analytical Chemistry. 81: 5218-25. PMID 19563210 DOI: 10.1021/Ac900845A |
0.501 |
|
| 2009 |
Bogdanova E, Zakharova M, Streeter S, Taylor J, Heyduk T, Kneale G, Severinov K. Transcription regulation of restriction-modification system Esp1396I. Nucleic Acids Research. 37: 3354-66. PMID 19336410 DOI: 10.1093/Nar/Gkp210 |
0.418 |
|
| 2009 |
Tian L, Heyduk T. Bivalent ligands with long nanometer-scale flexible linkers. Biochemistry. 48: 264-75. PMID 19113836 DOI: 10.1021/Bi801630B |
0.496 |
|
| 2008 |
Heyduk E, Dummit B, Chang YH, Heyduk T. Molecular pincers: antibody-based homogeneous protein sensors. Analytical Chemistry. 80: 5152-9. PMID 18491925 DOI: 10.1021/Ac8004154 |
0.31 |
|
| 2008 |
Bogdanova E, Djordjevic M, Papapanagiotou I, Heyduk T, Kneale G, Severinov K. Transcription regulation of the type II restriction-modification system AhdI. Nucleic Acids Research. 36: 1429-42. PMID 18203750 DOI: 10.1093/Nar/Gkm1116 |
0.452 |
|
| 2007 |
Sevostyanova A, Feklistov A, Barinova N, Heyduk E, Bass I, Klimasauskas S, Heyduk T, Kulbachinskiy A. Specific recognition of the -10 promoter element by the free RNA polymerase sigma subunit. The Journal of Biological Chemistry. 282: 22033-9. PMID 17535803 DOI: 10.1074/Jbc.M702495200 |
0.521 |
|
| 2006 |
Feklistov A, Barinova N, Sevostyanova A, Heyduk E, Bass I, Vvedenskaya I, Kuznedelov K, Merkiene E, Stavrovskaya E, Klimasauskas S, Nikiforov V, Heyduk T, Severinov K, Kulbachinskiy A. A basal promoter element recognized by free RNA polymerase sigma subunit determines promoter recognition by RNA polymerase holoenzyme. Molecular Cell. 23: 97-107. PMID 16798040 DOI: 10.1016/J.Molcel.2006.06.010 |
0.487 |
|
| 2006 |
Heyduk E, Kuznedelov K, Severinov K, Heyduk T. A consensus adenine at position -11 of the nontemplate strand of bacterial promoter is important for nucleation of promoter melting. The Journal of Biological Chemistry. 281: 12362-9. PMID 16531399 DOI: 10.1074/Jbc.M601364200 |
0.469 |
|
| 2005 |
Semenova E, Minakhin L, Bogdanova E, Nagornykh M, Vasilov A, Heyduk T, Solonin A, Zakharova M, Severinov K. Transcription regulation of the EcoRV restriction-modification system. Nucleic Acids Research. 33: 6942-51. PMID 16332697 DOI: 10.1093/Nar/Gki998 |
0.329 |
|
| 2005 |
Bera S, Vora AC, Chiu R, Heyduk T, Grandgenett DP. Synaptic complex formation of two retrovirus DNA attachment sites by integrase: a fluorescence energy transfer study. Biochemistry. 44: 15106-14. PMID 16285714 DOI: 10.1021/Bi0508340 |
0.46 |
|
| 2005 |
Niedziela-Majka A, Heyduk T. Escherichia coli RNA polymerase contacts outside the -10 promoter element are not essential for promoter melting. The Journal of Biological Chemistry. 280: 38219-27. PMID 16169843 DOI: 10.1074/Jbc.M507984200 |
0.561 |
|
| 2005 |
Heyduk E, Heyduk T. Nucleic acid-based fluorescence sensors for detecting proteins. Analytical Chemistry. 77: 1147-56. PMID 15858998 DOI: 10.1021/Ac0487449 |
0.404 |
|
| 2004 |
Gregory BD, Nickels BE, Garrity SJ, Severinova E, Minakhin L, Urbauer RJ, Urbauer JL, Heyduk T, Severinov K, Hochschild A. A regulator that inhibits transcription by targeting an intersubunit interaction of the RNA polymerase holoenzyme. Proceedings of the National Academy of Sciences of the United States of America. 101: 4554-9. PMID 15070756 DOI: 10.1073/Pnas.0400923101 |
0.385 |
|
| 2004 |
Knoll E, Heyduk T. Unimolecular beacons for the detection of DNA-binding proteins. Analytical Chemistry. 76: 1156-64. PMID 14961750 DOI: 10.1021/Ac034985P |
0.499 |
|
| 2003 |
Borrmann L, Schwanbeck R, Heyduk T, Seebeck B, Rogalla P, Bullerdiek J, Wisniewski JR. High mobility group A2 protein and its derivatives bind a specific region of the promoter of DNA repair gene ERCC1 and modulate its activity. Nucleic Acids Research. 31: 6841-51. PMID 14627817 DOI: 10.1093/Nar/Gkg884 |
0.47 |
|
| 2003 |
Simeonov MF, Bieber Urbauer RJ, Gilmore JM, Adelman K, Brody EN, Niedziela-Majka A, Minakhin L, Heyduk T, Urbauer JL. Characterization of the interactions between the bacteriophage T4 AsiA protein and RNA polymerase. Biochemistry. 42: 7717-26. PMID 12820881 DOI: 10.1021/Bi0340797 |
0.463 |
|
| 2003 |
Heyduk E, Fei Y, Heyduk T. Homogeneous fluorescence assay for cyclic AMP. Combinatorial Chemistry & High Throughput Screening. 6: 347-54. PMID 12769678 DOI: 10.2174/138620703106298437 |
0.505 |
|
| 2003 |
Heyduk E, Knoll E, Heyduk T. Molecular beacons for detecting DNA binding proteins: mechanism of action. Analytical Biochemistry. 316: 1-10. PMID 12694720 DOI: 10.1016/S0003-2697(03)00004-6 |
0.494 |
|
| 2003 |
Bergendahl V, Heyduk T, Burgess RR. Luminescence resonance energy transfer-based high-throughput screening assay for inhibitors of essential protein-protein interactions in bacterial RNA polymerase. Applied and Environmental Microbiology. 69: 1492-8. PMID 12620834 DOI: 10.1128/Aem.69.3.1492-1498.2003 |
0.463 |
|
| 2003 |
Minakhin L, Niedziela-Majka A, Kuznedelov K, Adelman K, Urbauer JL, Heyduk T, Severinov K. Interaction of T4 AsiA with its target sites in the RNA polymerase sigma70 subunit leads to distinct and opposite effects on transcription. Journal of Molecular Biology. 326: 679-90. PMID 12581632 DOI: 10.1016/S0022-2836(02)01442-0 |
0.465 |
|
| 2003 |
Minakhin L, Niedziela-Majka A, Kuznedelov K, Adelman K, Urbauer JL, Heyduk T, Severinov K. Interaction of T4 AsiA with its target sites in the RNA polymerase σ70 subunit leads to distinct and opposite effects on transcription Journal of Molecular Biology. 326: 679-690. DOI: 10.1016/S0022-2836(02)01442-0 |
0.363 |
|
| 2002 |
Heyduk T. Measuring protein conformational changes by FRET/LRET. Current Opinion in Biotechnology. 13: 292-6. PMID 12323348 DOI: 10.1016/S0958-1669(02)00332-4 |
0.345 |
|
| 2002 |
Bergendahl V, Anthony LC, Heyduk T, Burgess RR. On-column tris(2-carboxyethyl)phosphine reduction and IC5-maleimide labeling during purification of a RpoC fragment on a nickel-nitrilotriacetic acid Column. Analytical Biochemistry. 307: 368-74. PMID 12202256 DOI: 10.1016/S0003-2697(02)00061-1 |
0.42 |
|
| 2002 |
Nechaev S, Yuzenkova Y, Niedziela-Majka A, Heyduk T, Severinov K. A novel bacteriophage-encoded RNA polymerase binding protein inhibits transcription initiation and abolishes transcription termination by host RNA polymerase. Journal of Molecular Biology. 320: 11-22. PMID 12079331 DOI: 10.1016/S0022-2836(02)00420-5 |
0.47 |
|
| 2002 |
Heyduk E, Heyduk T. Conformation of fork junction DNA in a complex with Escherichia coli RNA polymerase. Biochemistry. 41: 2876-83. PMID 11851436 DOI: 10.1021/Bi012133I |
0.496 |
|
| 2002 |
Kuznedelov K, Minakhin L, Niedziela-Majka A, Dove SL, Rogulja D, Nickels BE, Hochschild A, Heyduk T, Severinov K. A role for interaction of the RNA polymerase flap domain with the sigma subunit in promoter recognition. Science (New York, N.Y.). 295: 855-7. PMID 11823642 DOI: 10.1126/Science.1066303 |
0.431 |
|
| 2002 |
Heyduk T, Heyduk E. Molecular beacons for detecting DNA binding proteins. Nature Biotechnology. 20: 171-6. PMID 11821863 DOI: 10.1038/Nbt0202-171 |
0.499 |
|
| 2001 |
Heyduk T, Niedziela-Majka A. Fluorescence resonance energy transfer analysis of Escherichia coli RNA polymerase and polymerase-DNA complexes Biopolymers. 61: 201-213. PMID 11987181 DOI: 10.1002/Bip.10139 |
0.557 |
|
| 2001 |
Heyduk E, Baichoo N, Heyduk T. Interaction of the α-subunit of Escherichia coli RNA Polymerase with DNA: Rigid body nature of the protein-DNA contact Journal of Biological Chemistry. 276: 44598-44603. PMID 11571305 DOI: 10.1074/Jbc.M107760200 |
0.519 |
|
| 2001 |
Heyduk T. Luminescence resonance energy transfer analysis of rna polymerase complexes Methods. 25: 44-53. PMID 11558996 DOI: 10.1006/Meth.2001.1214 |
0.32 |
|
| 2001 |
Young BA, Anthony LC, Gruber TM, Arthur TM, Heyduk E, Lu CZ, Sharp MM, Heyduk T, Burgess RR, Gross CA. A coiled-coil from the RNA polymerase beta' subunit allosterically induces selective nontemplate strand binding by sigma(70). Cell. 105: 935-44. PMID 11439189 DOI: 10.1016/S0092-8674(01)00398-1 |
0.414 |
|
| 2001 |
Schwanbeck R, Gymnopoulos M, Petry I, Piekiełko A, Szewczuk Z, Heyduk T, Zechel K, Wiśniewski JR. Consecutive Steps of Phosphorylation Affect Conformation and DNA Binding of the Chironomus High Mobility Group A Protein Journal of Biological Chemistry. 276: 26012-26021. PMID 11335713 DOI: 10.1074/Jbc.M011053200 |
0.356 |
|
| 2001 |
Zhao T, Heyduk T, Eissenberg JC. Phosphorylation site mutations in heterochromatin protein 1 (HP1) reduce or eliminate silencing activity. The Journal of Biological Chemistry. 276: 9512-8. PMID 11121421 DOI: 10.1074/Jbc.M010098200 |
0.308 |
|
| 2001 |
Piekiełko A, Drung A, Rogalla P, Schwanbeck R, Heyduk T, Gerharz M, Bullerdiek J, Wisniewski JR. Distinct organization of DNA complexes of various HMGI/Y family proteins and their modulation upon mitotic phosphorylation Journal of Biological Chemistry. 276: 1984-1992. PMID 11034995 DOI: 10.1074/Jbc.M004065200 |
0.451 |
|
| 2000 |
Matlock DL, Heyduk T. Sequence determinants for the recognition of the fork junction DNA containing the -10 region of promoter DNA by E. coli RNA polymerase. Biochemistry. 39: 12274-83. PMID 11015206 DOI: 10.1021/Bi001433H |
0.755 |
|
| 2000 |
Zhao T, Heyduk T, Allis CD, Eissenberg JC. Heterochromatin protein 1 binds to nucleosomes and DNA in vitro. The Journal of Biological Chemistry. 275: 28332-8. PMID 10882726 DOI: 10.1074/jbc.M003493200 |
0.366 |
|
| 1999 |
Wiśniewski JR, Krohn NM, Heyduk E, Grasser KD, Heyduk T. HMG1 proteins from evolutionary distant organisms distort B-DNA conformation in similar way Biochimica Et Biophysica Acta - Gene Structure and Expression. 1447: 25-34. PMID 10500240 DOI: 10.1016/S0167-4781(99)00123-2 |
0.475 |
|
| 1999 |
Baichoo N, Heyduk T. DNA-induced conformational changes in cyclic AMP receptor protein: Detection and mapping by a protein footprinting technique using multiple chemical proteases Journal of Molecular Biology. 290: 37-48. PMID 10388556 DOI: 10.1006/Jmbi.1999.2858 |
0.508 |
|
| 1999 |
Matlock DL, Heyduk T. A real-time fluorescence method to monitor the melting of duplex DNA during transcription initiation by RNA polymerase. Analytical Biochemistry. 270: 140-7. PMID 10328775 DOI: 10.1006/Abio.1999.4078 |
0.75 |
|
| 1999 |
Baichoo N, Heyduk T. Mapping cyclic nucleotide-induced conformational changes in cyclicAMP receptor protein by a protein footprinting technique using different chemical proteases Protein Science. 8: 518-528. PMID 10091654 DOI: 10.1110/Ps.8.3.518 |
0.401 |
|
| 1999 |
Callaci S, Heyduk E, Heyduk T, Doisy EA. Core RNA polymerase from E. coli induces a major change in the domain arrangement of the σ70 subunit Molecular Cell. 3: 229-238. PMID 10078205 DOI: 10.1016/S1097-2765(00)80313-5 |
0.452 |
|
| 1999 |
Heyduk E, Heyduk T. Architecture of a complex between the σ70 subunit of Escherichia coli RNA polymerase and the nontemplate strand oligonucleotide. Luminescence resonance energy transfer study Journal of Biological Chemistry. 274: 3315-3322. PMID 9920872 DOI: 10.1074/Jbc.274.6.3315 |
0.495 |
|
| 1998 |
Callaci S, Heyduk E, Heyduk T. Conformational changes of Escherichia coli RNA polymerase σ70 factor induced by binding to the core enzyme Journal of Biological Chemistry. 273: 32995-33001. PMID 9830052 DOI: 10.1074/Jbc.273.49.32995 |
0.502 |
|
| 1998 |
Callaci S, Heyduk T. Conformation and DNA binding properties of a single-stranded DNA binding region of σ70 subunit from Escherichia coli RNA polymerase are modulated by an interaction with the core enzyme Biochemistry. 37: 3312-3320. PMID 9521651 DOI: 10.1021/Bi972041M |
0.548 |
|
| 1998 |
Heyduk E, Heyduk T. Probing the structure of macromolecules using microsecond time-resolved fluorescence of europium chelates Proceedings of Spie - the International Society For Optical Engineering. 3256: 218-222. DOI: 10.1117/12.307063 |
0.349 |
|
| 1997 |
Baichoo N, Heyduk T. Mapping conformational changes in a protein: Application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein Biochemistry. 36: 10830-10836. PMID 9283073 DOI: 10.1021/Bi970714V |
0.404 |
|
| 1997 |
Wang Y, Severinov K, Loizos N, Fenyö D, Heyduk E, Heyduk T, Chait BT, Darst SA. Determinants for Escherichia coli RNA polymerase assembly within the beta subunit. Journal of Molecular Biology. 270: 648-62. PMID 9245594 DOI: 10.1006/Jmbi.1997.1139 |
0.304 |
|
| 1997 |
Heyduk E, Heyduk T, Claus P, Wiśniewski JR. Conformational changes of DNA induced by binding of Chironomus high mobility group protein 1a (cHMG1a). Regions flanking an HMG1 box domain do not influence the bend angle of the DNA Journal of Biological Chemistry. 272: 19763-19770. PMID 9242635 DOI: 10.1074/Jbc.272.32.19763 |
0.476 |
|
| 1997 |
Heyduk E, Heyduk T. Thiol-reactive, luminescent europium chelates: Luminescence probes for resonance energy transfer distance measurements in biomolecules Analytical Biochemistry. 248: 216-227. PMID 9177747 DOI: 10.1006/Abio.1997.2148 |
0.354 |
|
| 1996 |
Niu W, Kim Y, Tau G, Heyduk T, Ebright RH. Transcription activation at class II CAP-dependent promoters: two interactions between CAP and RNA polymerase. Cell. 87: 1123-34. PMID 8978616 DOI: 10.1016/S0092-8674(00)81806-1 |
0.446 |
|
| 1996 |
Heyduk T, Ma Y, Tang H, Ebright RH. Fluorescence anisotrophy: Rapid, quantitative assay for protein-DNA and protein-protein interaction Methods in Enzymology. 274: 492-503. PMID 8902827 DOI: 10.1016/S0076-6879(96)74039-9 |
0.341 |
|
| 1994 |
Heyduk E, Heyduk T. Mapping protein domains involved in macromolecular interactions: A novel protein footprinting approach Biochemistry. 33: 9643-9650. PMID 8068641 DOI: 10.1021/Bi00198A033 |
0.446 |
|
| 1993 |
Heyduk T, Lee JC, Ebright YW, Blatter EE, Zhou Y, Ebright RH. CAP interacts with RNA polymerase in solution in the absence of promoter DNA Nature. 364: 548-549. PMID 8393148 DOI: 10.1038/364548A0 |
0.511 |
|
| 1993 |
Heyduk E, Heyduk T. Physical studies on interaction of transcription activator and RNA-polymerase: Fluorescent derivatives of CRP and RNA polymerase Cellular and Molecular Biology Research. 39: 401-407. PMID 8312976 |
0.386 |
|
| 1992 |
Heyduk T, Lee JC. Solution studies on the structure of bent DNA in the cAMP receptor protein-lac DNA complex Biochemistry. 31: 5165-5171. PMID 1606140 DOI: 10.1021/Bi00137A011 |
0.465 |
|
| 1992 |
Heyduk E, Heyduk T, Lee JC. Intersubunit communications in Escherichia coli cyclic AMP receptor protein: Studies of the ligand binding domain Biochemistry®. 31: 3682-3688. PMID 1314647 DOI: 10.1021/Bi00129A017 |
0.391 |
|
| 1990 |
Heyduk T, Lee JC. Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction Proceedings of the National Academy of Sciences of the United States of America. 87: 1744-1748. PMID 2155424 DOI: 10.1073/Pnas.87.5.1744 |
0.508 |
|
| 1989 |
Heyduk T, Lee JC. Escherichia coli cAMP receptor protein: Evidence for three protein conformational states with different promoter binding affinities Biochemistry. 28: 6914-6924. PMID 2554959 DOI: 10.1021/Bi00443A021 |
0.411 |
|
| 1986 |
Heyduk T, Moniewska A, Kochman M. The reactivity and function of cysteine residues in rabbit liver aldolase B Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 874: 337-346. PMID 3790575 DOI: 10.1016/0167-4838(86)90033-6 |
0.304 |
|
| Low-probability matches (unlikely to be authored by this person) |
| 1985 |
Dzugaj A, Heyduk T, Buczyz.xl;lko J, Kochman M. Structural changes of rabbit liver fructose-1,6-bisphosphatase: the effect of urea and subtilisin digestion Archives of Biochemistry and Biophysics. 239: 486-490. PMID 2988451 DOI: 10.1016/0003-9861(85)90716-7 |
0.297 |
|
| 2014 |
Heyduk E, Heyduk T. Ribosome display enhanced by next generation sequencing: a tool to identify antibody-specific peptide ligands. Analytical Biochemistry. 464: 73-82. PMID 25058925 DOI: 10.1016/J.Ab.2014.07.014 |
0.295 |
|
| 2018 |
Heyduk E, Hickey R, Pozzi N, Heyduk T. Peptide ligand-based ELISA reagents for antibody detection. Analytical Biochemistry. 559: 55-61. PMID 30130491 DOI: 10.1016/J.Ab.2018.08.012 |
0.293 |
|
| 2010 |
Heyduk T. Practical biophysics: Sensors for rapid detection of biological targets utilizing target-induced oligonucleotide annealing. Biophysical Chemistry. 151: 91-5. PMID 20542627 DOI: 10.1016/J.Bpc.2010.05.008 |
0.293 |
|
| 2004 |
Klein C, Heyduk T, Sunahara RK. Zinc inhibition of adenylyl cyclase correlates with conformational changes in the enzyme. Cellular Signalling. 16: 1177-85. PMID 15240012 DOI: 10.1016/J.Cellsig.2004.03.008 |
0.292 |
|
| 2000 |
Underwood MC, Zhong D, Mathur A, Heyduk T, Bajaj SP. Thermodynamic linkage between the S1 site, the Na+ site, and the Ca2+ site in the protease domain of human coagulation factor Xa. Studies on catalytic efficiency and inhibitor binding Journal of Biological Chemistry. 275: 36876-36884. PMID 10973949 DOI: 10.1074/Jbc.M001386200 |
0.292 |
|
| 1996 |
Waheed A, Okuyama T, Heyduk T, Sly WS. Carbonic anhydrase IV: Purification of a secretory form of the recombinant human enzyme and identification of the positions and importance of its disulfide bonds Archives of Biochemistry and Biophysics. 333: 432-438. PMID 8809084 DOI: 10.1006/Abbi.1996.0412 |
0.287 |
|
| 1985 |
Heyduk T, Kochman M. Temperature-induced conformational transition in rabbit muscle aldolase studied by temperature dependence of sulfhydryl reactivity European Journal of Biochemistry. 151: 337-343. PMID 4029138 DOI: 10.1111/J.1432-1033.1985.Tb09106.X |
0.282 |
|
| 2022 |
Koehler LC, Grese ZR, Bastos ACS, Mamede LD, Heyduk T, Ayala YM. TDP-43 Oligomerization and Phase Separation Properties Are Necessary for Autoregulation. Frontiers in Neuroscience. 16: 818655. PMID 35495061 DOI: 10.3389/fnins.2022.818655 |
0.28 |
|
| 1996 |
Heyduk T, Heyduk E, Severinov K, Tang H, Ebright RH. Determinants of RNA polymerase α subunit for interaction with β, β′, and σ subunits: Hydroxyl-radical protein footprinting Proceedings of the National Academy of Sciences of the United States of America. 93: 10162-10166. PMID 8816769 DOI: 10.1073/Pnas.93.19.10162 |
0.277 |
|
| 2002 |
Klein C, Sunahara RK, Hudson TY, Heyduk T, Howlett AC. Zinc inhibition of cAMP signaling. The Journal of Biological Chemistry. 277: 11859-65. PMID 11805091 DOI: 10.1074/Jbc.M108808200 |
0.273 |
|
| 2001 |
Heyduk T, Heyduk E. Luminescence energy transfer with lanthanide chelates: Interpretation of sensitized acceptor decay amplitudes Analytical Biochemistry. 289: 60-67. PMID 11161295 DOI: 10.1006/Abio.2000.4925 |
0.272 |
|
| 1993 |
Adamus G, Arendt A, Hargrave PA, Heyduk T, Palczewski K. The Kinetics of Multiphosphorylation of Rhodopsin Archives of Biochemistry and Biophysics. 304: 443-447. PMID 8346919 DOI: 10.1006/Abbi.1993.1373 |
0.27 |
|
| 1986 |
Heyduk T, Kochman M. Re-evaluation of the role of thiol groups in rabbit muscle aldolase A Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 874: 365-367. PMID 3790576 DOI: 10.1016/0167-4838(86)90036-1 |
0.263 |
|
| 1995 |
Heyduk E, Heyduk T. Mapping Protein Domains Involved in Macromolecular Interactions: A Novel Protein Footprinting Approach. [Erratum to document cited in CA121:103552] Biochemistry. 34: 15388-15388. DOI: 10.1021/Bi00046A048 |
0.259 |
|
| 2010 |
Heyduk E, Moxley MM, Salvatori A, Corbett JA, Heyduk T. Homogeneous insulin and C-Peptide sensors for rapid assessment of insulin and C-peptide secretion by the islets. Diabetes. 59: 2360-5. PMID 20622164 DOI: 10.2337/Db10-0088 |
0.248 |
|
| 1983 |
Jedrzejak J, Heyduk T, Kochman M. An approach to the elucidation of the quaternary structure role in the activity of pyruvate kinase studies on the immobilized enzyme International Journal of Biochemistry. 15: 695-702. PMID 6862082 DOI: 10.1016/0020-711X(83)90194-5 |
0.243 |
|
| 1997 |
Callaci S, Heyduk T. Conformation al changes of k.cou a factor induced by binding core RNA polymerase Faseb Journal. 11: A1377. |
0.24 |
|
| 1992 |
Heyduk E, Heyduk T, Lee JC. Global conformational changes in allosteric proteins: A study of Escherichia coli cAMP receptor protein and muscle pyruvate kinase Journal of Biological Chemistry. 267: 3200-3204. PMID 1737775 |
0.223 |
|
| 1991 |
Heyduk T, Michalczyk R, Kochman M. Long-range effects and conformational flexibility of aldolase Journal of Biological Chemistry. 266: 15650-15655. PMID 1874722 |
0.213 |
|
| 2001 |
Heyduk T, Baichoo N, Heyduk E. Hydroxyl radical footprinting of proteins using metal ion complexes Metal Ions in Biological Systems. 38: 255-287. PMID 11219012 |
0.09 |
|
| Hide low-probability matches. |