| Year |
Citation |
Score |
| 2019 |
Bergasa-Caceres F, Haas E, Rabitz HA. Nature's Shortcut to Protein Folding. The Journal of Physical Chemistry. B. PMID 30901220 DOI: 10.1021/Acs.Jpcb.8B11634 |
0.313 |
|
| 2018 |
Woodard J, Srivastava KR, Rahamim G, Grupi A, Hogan S, Witalka DJ, Nawrocki G, Haas E, Feig M, Lapidus LJ. Intramolecular Diffusion in α-Synuclein: It Depends on How You Measure It. Biophysical Journal. PMID 30224053 DOI: 10.1016/J.Bpj.2018.08.023 |
0.469 |
|
| 2018 |
Graen T, Klement R, Grupi A, Haas E, Grubmüller H. Transient Secondary and Tertiary Structure Formation Kinetics in the Intrinsically Disordered State of α-Synuclein from Atomistic Simulations. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 30047198 DOI: 10.1002/Cphc.201800504 |
0.331 |
|
| 2018 |
Jacob MH, D'Souza RN, Schwarzlose T, Wang X, Huang F, Haas E, Nau WM. A Method-Unifying View on Loop Formation Kinetics in Peptide and Protein Folding. The Journal of Physical Chemistry. B. PMID 29617564 DOI: 10.1021/Acs.Jpcb.8B00879 |
0.499 |
|
| 2018 |
Haas E, Rahamim G, Amir D. Sequential Folding of Globular Protein Initiated by Fast Loop Closure Biophysical Journal. 114: 579a. DOI: 10.1016/J.Bpj.2017.11.3168 |
0.325 |
|
| 2017 |
Rahamim G, Amir D, Haas E. Simultaneous Determination of Two Subdomain Folding Rates Using the "Transfer-Quench" Method. Biophysical Journal. 112: 1786-1796. PMID 28494950 DOI: 10.1016/J.Bpj.2017.01.037 |
0.472 |
|
| 2017 |
Rahamim G, Amir D, Haas E. Resolution of the Time Sequence of Fast Folding Transition by the “Transfer-Quench” Method Biophysical Journal. 112: 41a. DOI: 10.1016/J.Bpj.2016.11.262 |
0.448 |
|
| 2016 |
Klement R, Graen T, Grupi A, Haas E, Grubmüller H. Molecular Dynamics Simulations of Alpha-Synuclein Ensemble FRET Measurements from Different Force Fields Biophysical Journal. 110: 551a. DOI: 10.1016/J.Bpj.2015.11.2949 |
0.349 |
|
| 2016 |
Haas E, Amir D, Orevi T, Rahamim G, Kathuria S, Matthews RC, Bilsel O. Fast Closuer of Long Loops at the Initiation of a Protein Folding Pathway Biophysical Journal. 110: 390a. DOI: 10.1016/J.Bpj.2015.11.2106 |
0.437 |
|
| 2015 |
Rahamim G, Chemerovski-Glikman M, Rahimipour S, Amir D, Haas E. Resolution of Two Sub-Populations of Conformers and Their Individual Dynamics by Time Resolved Ensemble Level FRET Measurements. Plos One. 10: e0143732. PMID 26699718 DOI: 10.1371/Journal.Pone.0143732 |
0.439 |
|
| 2015 |
Orevi T, Rahamim G, Amir D, Kathuria S, Bilsel O, Matthews CR, Haas E. Sequential Closure of Loop Structures Forms the Folding Nucleus during the Refolding Transition of the Escherichia coli Adenylate Kinase Molecule. Biochemistry. PMID 26666584 DOI: 10.1021/Acs.Biochem.5B00849 |
0.435 |
|
| 2015 |
Haas E. Fast Closure of Long Loops at the Initiation of Folding of Globular Proteins Studied by FRET Based Methods Biophysical Journal. 108: 51a. DOI: 10.1016/J.Bpj.2014.11.311 |
0.375 |
|
| 2014 |
Orevi T, Ben Ishay E, Gershanov SL, Dalak MB, Amir D, Haas E. Fast closure of N-terminal long loops but slow formation of β strands precedes the folding transition state of Escherichia coli adenylate kinase. Biochemistry. 53: 3169-78. PMID 24787383 DOI: 10.1021/Bi500069W |
0.398 |
|
| 2014 |
Lerner E, Orevi T, Ben Ishay E, Amir D, Haas E. Kinetics of fast changing intramolecular distance distributions obtained by combined analysis of FRET efficiency kinetics and time-resolved FRET equilibrium measurements. Biophysical Journal. 106: 667-76. PMID 24507607 DOI: 10.1016/J.Bpj.2013.11.4500 |
0.434 |
|
| 2014 |
Orevi T, Lerner E, Rahamim G, Amir D, Haas E. Ensemble and single-molecule detected time-resolved FRET methods in studies of protein conformations and dynamics. Methods in Molecular Biology (Clifton, N.J.). 1076: 113-69. PMID 24108626 DOI: 10.1007/978-1-62703-649-8_7 |
0.476 |
|
| 2014 |
Orevi T, Rahamim G, Shemesh S, Ben Ishay E, Amir D, Haas E. Fast closure of long loops at the initiation of the folding transition of globular proteins studied by time-resolved FRET-based methods Bio-Algorithms and Med-Systems. 10. DOI: 10.1515/Bams-2014-0018 |
0.421 |
|
| 2014 |
Haas E, Orevi T, Rahamim G, Amir D. Non Local Interactions are Essential Elements of the Initiation and Guidance of the Folding Pathway of Proteins Biophysical Journal. 106: 672a. DOI: 10.1016/J.Bpj.2013.11.3724 |
0.368 |
|
| 2013 |
Orevi T, Rahamim G, Hazan G, Amir D, Haas E. The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways. Biophysical Reviews. 5: 85-98. PMID 28510159 DOI: 10.1007/S12551-013-0113-3 |
0.343 |
|
| 2013 |
Lerner E, Hilzenrat G, Amir D, Tauber E, Garini Y, Haas E. Preparation of homogeneous samples of double-labelled protein suitable for single-molecule FRET measurements. Analytical and Bioanalytical Chemistry. 405: 5983-91. PMID 23649926 DOI: 10.1007/S00216-013-7002-2 |
0.423 |
|
| 2013 |
Haas E, Orevi T, Ben-Ishay E, Rahamim G, Gershonov S, Shulman A, Ben-Dalak M, Hazan G, Amir D. Non-Local Interactions Lead the Folding Transition of a Globular Protein Biophysical Journal. 104: 369a. DOI: 10.1016/J.Bpj.2012.11.2053 |
0.393 |
|
| 2012 |
Ishay EB, Hazan G, Rahamim G, Amir D, Haas E. An instrument for fast acquisition of fluorescence decay curves at picosecond resolution designed for "double kinetics" experiments: application to fluorescence resonance excitation energy transfer study of protein folding. The Review of Scientific Instruments. 83: 084301. PMID 22938314 DOI: 10.1063/1.4737632 |
0.477 |
|
| 2012 |
Ben Ishay E, Rahamim G, Orevi T, Hazan G, Amir D, Haas E. Fast subdomain folding prior to the global refolding transition of E. coli adenylate kinase: a double kinetics study. Journal of Molecular Biology. 423: 613-23. PMID 22898349 DOI: 10.1016/J.Jmb.2012.08.001 |
0.475 |
|
| 2012 |
Haas E. Ensemble FRET methods in studies of intrinsically disordered proteins. Methods in Molecular Biology (Clifton, N.J.). 895: 467-98. PMID 22760335 DOI: 10.1007/978-1-61779-927-3_28 |
0.45 |
|
| 2012 |
Klement R, Grubmüller H, Haas E. α-Synuclein Monomer Conformations Studied by in Silico and in Vitro FRET Biophysical Journal. 102: 630a. DOI: 10.1016/J.Bpj.2011.11.3430 |
0.391 |
|
| 2012 |
Haas E, Orevi T, Een-Ishai E, Rahamim G, Gershonov S, Hazan G, Amir D. Non-Local Interactions Essential for Initiation of Protein Folding Biophysical Journal. 102: 57a. DOI: 10.1016/J.Bpj.2011.11.341 |
0.394 |
|
| 2011 |
Phillips NB, Racca J, Chen YS, Singh R, Jancso-Radek A, Radek JT, Wickramasinghe NP, Haas E, Weiss MA. Mammalian testis-determining factor SRY and the enigma of inherited human sex reversal: frustrated induced fit in a bent protein-DNA complex. The Journal of Biological Chemistry. 286: 36787-807. PMID 21849498 DOI: 10.1074/Jbc.M111.260091 |
0.309 |
|
| 2011 |
Nagarajan S, Amir D, Grupi A, Goldenberg DP, Minton AP, Haas E. Modulation of functionally significant conformational equilibria in adenylate kinase by high concentrations of trimethylamine oxide attributed to volume exclusion. Biophysical Journal. 100: 2991-9. PMID 21689533 DOI: 10.1016/J.Bpj.2011.03.065 |
0.334 |
|
| 2011 |
Ulman A, Ioffe M, Patolsky F, Haas E, Reuvenov D. Highly active engineered-enzyme oriented monolayers: formation, characterization and sensing applications. Journal of Nanobiotechnology. 9: 26. PMID 21689418 DOI: 10.1186/1477-3155-9-26 |
0.315 |
|
| 2011 |
Grupi A, Haas E. Time-resolved FRET detection of subtle temperature-induced conformational biases in ensembles of α-synuclein molecules. Journal of Molecular Biology. 411: 234-47. PMID 21570984 DOI: 10.1016/J.Jmb.2011.04.056 |
0.385 |
|
| 2011 |
Grupi A, Haas E. Segmental conformational disorder and dynamics in the intrinsically disordered protein α-synuclein and its chain length dependence. Journal of Molecular Biology. 405: 1267-83. PMID 21108951 DOI: 10.1016/J.Jmb.2010.11.011 |
0.437 |
|
| 2009 |
Huang F, Rajagopalan S, Settanni G, Marsh RJ, Armoogum DA, Nicolaou N, Bain AJ, Lerner E, Haas E, Ying L, Fersht AR. Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer Proceedings of the National Academy of Sciences of the United States of America. 106: 20758-20763. PMID 19933326 DOI: 10.1073/Pnas.0909644106 |
0.358 |
|
| 2009 |
Huang F, Lerner E, Sato S, Amir D, Haas E, Fersht AR. Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the b domain of protein A Biochemistry. 48: 3468-3476. PMID 19222162 DOI: 10.1021/Bi801890W |
0.448 |
|
| 2009 |
Orevi T, Ben Ishay E, Pirchi M, Jacob MH, Amir D, Haas E. Early closure of a long loop in the refolding of adenylate kinase: a possible key role of non-local interactions in the initial folding steps. Journal of Molecular Biology. 385: 1230-42. PMID 19013178 DOI: 10.1016/J.Bpj.2010.12.1364 |
0.458 |
|
| 2009 |
Haas E, Amir D, Lerner E. Time-resolved Fret Study Shows Sub-populations of A Globular Protein Molecules at The Refolding Transition Zone Biophysical Journal. 96: 389a. DOI: 10.1016/J.Bpj.2008.12.2905 |
0.436 |
|
| 2008 |
Haas E. Folding on the assembly line. Acs Chemical Biology. 3: 527-9. PMID 18803369 DOI: 10.1021/Cb800216N |
0.428 |
|
| 2008 |
Sherman E, Itkin A, Kuttner YY, Rhoades E, Amir D, Haas E, Haran G. Using fluorescence correlation spectroscopy to study conformational changes in denatured proteins. Biophysical Journal. 94: 4819-27. PMID 18326651 DOI: 10.1529/Biophysj.107.120220 |
0.78 |
|
| 2008 |
Haas E. Fluorescence Resonance Energy Transfer (FRET) and Single Molecule Fluorescence Detection Studies of the Mechanism of Protein Folding and Unfolding Protein Folding Handbook. 2: 573-633. DOI: 10.1002/9783527619498.ch17 |
0.396 |
|
| 2006 |
Magg C, Kubelka J, Holtermann G, Haas E, Schmid FX. Specificity of the Initial Collapse in the Folding of the Cold Shock Protein Journal of Molecular Biology. 360: 1067-1080. PMID 16815441 DOI: 10.1016/J.Jmb.2006.05.073 |
0.42 |
|
| 2005 |
Jacob MH, Amir D, Ratner V, Gussakowsky E, Haas E. Predicting reactivities of protein surface cysteines as part of a strategy for selective multiple labeling. Biochemistry. 44: 13664-72. PMID 16229456 DOI: 10.1021/Bi051205T |
0.381 |
|
| 2005 |
Ratner V, Amir D, Kahana E, Haas E. Fast collapse but slow formation of secondary structure elements in the refolding transition of E. coli adenylate kinase Journal of Molecular Biology. 352: 683-699. PMID 16098987 DOI: 10.1016/J.Jmb.2005.06.074 |
0.457 |
|
| 2005 |
Haas E. The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 6: 858-70. PMID 15884068 DOI: 10.1002/Cphc.200400617 |
0.423 |
|
| 2004 |
Ittah V, Kahana E, Amir D, Haas E. Applications of time-resolved resonance energy transfer measurements in studies of the molecular crowding effect. Journal of Molecular Recognition : Jmr. 17: 448-55. PMID 15362104 DOI: 10.1002/Jmr.702 |
0.484 |
|
| 2002 |
Navon A, Ittah V, Scheraga HA, Haas E. Formation of the hydrophobic core of ribonuclease A through sequential coordinated conformational transitions. Biochemistry. 41: 14225-31. PMID 12450386 DOI: 10.1021/Bi020506P |
0.445 |
|
| 2002 |
Ratner V, Kahana E, Eichler M, Haas E. A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies Bioconjugate Chemistry. 13: 1163-1170. PMID 12236801 DOI: 10.1021/Bc025537B |
0.421 |
|
| 2002 |
Ratner V, Kahana E, Haas E. The natively helical chain segment 169-188 of Escherichia coli adenylate kinase is formed in the latest phase of the refolding transition Journal of Molecular Biology. 320: 1135-1145. PMID 12126631 DOI: 10.1016/S0022-2836(02)00520-X |
0.455 |
|
| 2001 |
Chakraborty S, Ittah V, Bai P, Luo L, Haas E, Peng ZY. Structure and dynamics of the α-lactalbumin molten globule: Fluorescence studies using proteins containing a single tryptophan residue Biochemistry. 40: 7228-7238. PMID 11401570 DOI: 10.1021/Bi010004W |
0.441 |
|
| 2001 |
Navon A, Ittah V, Landsman P, Scheraga HA, Haas E. Distributions of intramolecular distances in the reduced and denatured states of bovine pancreatic ribonuclease A. Folding initiation structures in the C-terminal portions of the reduced protein. Biochemistry. 40: 105-18. PMID 11141061 DOI: 10.1021/Bi001946O |
0.445 |
|
| 2001 |
Navon A, Ittah V, Laity JH, Scheraga HA, Haas E, Gussakovsky EE. Local and long-range interactions in the thermal unfolding transition of bovine pancreatic ribonuclease A. Biochemistry. 40: 93-104. PMID 11141060 DOI: 10.1021/Bi001945W |
0.338 |
|
| 2000 |
Ratner V, Sinev M, Haas E. Determination of intramolecular distance distribution during protein folding on the millisecond timescale Journal of Molecular Biology. 299: 1363-1371. PMID 10873459 DOI: 10.1006/Jmbi.2000.3814 |
0.441 |
|
| 2000 |
Sinev M, Landsmann P, Sineva E, Ittah V, Haas E. Design consideration and probes for fluorescence resonance energy transfer studies Bioconjugate Chemistry. 11: 352-362. PMID 10821651 DOI: 10.1021/Bc990132L |
0.494 |
|
| 1999 |
Gakamsky DM, Davis DM, Haas E, Strominger JL, Pecht I. Photophysical analysis of class I major histocompatibility complex protein assembly using a xanthene-derivatized β2-microglobulin Biophysical Journal. 76: 1552-1560. PMID 10049335 DOI: 10.1016/S0006-3495(99)77314-5 |
0.442 |
|
| 1998 |
Ratner V, Haas E. An instrument for time resolved monitoring of fast chemical transitions: Application to the kinetics of refolding of a globular protein Review of Scientific Instruments. 69: 2147-2154. DOI: 10.1063/1.1148914 |
0.466 |
|
| 1996 |
Sinev MA, Sineva EV, Ittah V, Haas E. Towards a mechanism of AMP-substrate inhibition in adenylate kinase from Escherichia coli Febs Letters. 397: 273-276. PMID 8955362 DOI: 10.1016/S0014-5793(96)01195-7 |
0.358 |
|
| 1996 |
Sinev MA, Sineva EV, Ittah V, Haas E. Domain closure in adenylate kinase Biochemistry. 35: 6425-6437. PMID 8639589 DOI: 10.1021/Bi952687J |
0.37 |
|
| 1996 |
Barenholz Y, Cohen T, Haas E, Ottolenghi M. Lateral organization of pyrene-labeled lipids in bilayers as determined from the deviation from equilibrium between pyrene monomers and excimers Journal of Biological Chemistry. 271: 3085-3090. PMID 8621705 DOI: 10.1074/Jbc.271.6.3085 |
0.321 |
|
| 1995 |
Gussakovsky EE, Haas E. Two steps in the transition between the native and acid states of bovine α-lactalbumin detected by circular polarization of luminescence: Evidence for a premolten globule state? Protein Science. 4: 2319-2326. PMID 8563628 DOI: 10.1002/Pro.5560041109 |
0.38 |
|
| 1995 |
Buckler DR, Haas E, Scheraga HA. Analysis of the structure of ribonuclease A in native and partially denatured states by time-resolved noradiative dynamic excitation energy transfer between site-specific extrinsic probes. Biochemistry. 34: 15965-78. PMID 8519753 DOI: 10.1021/Bi00049A011 |
0.533 |
|
| 1995 |
Gakamsky DM, Haas E, Robbins P, Strominger JL, Pecht I. Selective steady-state and time-resolved fluorescence spectroscopy of an HLA-A2-peptide complex Immunology Letters. 44: 195-201. PMID 7797251 DOI: 10.1016/0165-2478(94)00214-C |
0.472 |
|
| 1995 |
Ittah V, Haas E. Nonlocal interactions stabilize long range loops in the initial folding intermediates of reduced bovine pancreatic trypsin inhibitor. Biochemistry. 34: 4493-506. PMID 7535565 DOI: 10.1021/Bi00013A042 |
0.427 |
|
| 1994 |
Dittes K, Gakamsky DM, Haran G, Haas E, Ojcius DM, Kourilsky P, Pecht I. Picosecond fluorescence spectroscopy of a single-chain class I major histocompatibility complex encoded protein in its peptide loaded and unloaded states. Immunology Letters. 40: 125-32. PMID 8088870 DOI: 10.1016/0165-2478(94)90183-X |
0.742 |
|
| 1994 |
Haran G, Haas E, Rapaport DC. Molecular dynamics simulations of simple peptide models: Solvent effects and comparison with experiment Journal of Physical Chemistry. 98: 10294-10302. DOI: 10.1021/J100091A053 |
0.667 |
|
| 1993 |
Buckler DR, Haas E, Scheraga HA. C-terminal labeling of ribonuclease A with an extrinsic fluorescent probe by carboxypeptidase Y-catalyzed transpeptidation in the presence of urea. Analytical Biochemistry. 209: 20-31. PMID 8465956 DOI: 10.1006/Abio.1993.1078 |
0.397 |
|
| 1993 |
Forster Y, Haas E. Preparation and characterization of three fluorescent labels for proteins, suitable for structural studies Analytical Biochemistry. 209: 9-14. PMID 7682038 DOI: 10.1006/Abio.1993.1076 |
0.41 |
|
| 1993 |
Gottfried DS, Haas E. Nonlocal interactions stabilize compact folding intermediates in reduced unfolded bovine pancreatic trypsin inhibitor. Biochemistry. 31: 12353-62. PMID 1281424 DOI: 10.1021/Bi00164A009 |
0.45 |
|
| 1992 |
Haran G, Haas E, Szpikowska BK, Mas MT. Domain motions in phosphoglycerate kinase: determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer. Proceedings of the National Academy of Sciences of the United States of America. 89: 11764-8. PMID 1465395 DOI: 10.1073/Pnas.89.24.11764 |
0.742 |
|
| 1992 |
Amir D, Krausz S, Haas E. Detection of local structures in reduced unfolded bovine pancreatic trypsin inhibitor. Proteins. 13: 162-73. PMID 1377825 DOI: 10.1002/Prot.340130210 |
0.484 |
|
| 1989 |
Beechem JM, Haas E. Simultaneous determination of intramolecular distance distributions and conformational dynamics by global analysis of energy transfer measurements Biophysical Journal. 55: 1225-1236. PMID 2765658 DOI: 10.1016/S0006-3495(89)82918-2 |
0.518 |
|
| 1989 |
Haas E. Folding and dynamics of globular proteins studied by time resolved fluorescence spectroscopy Progress in Clinical and Biological Research. 289: 157-170. PMID 2726797 |
0.333 |
|
| 1988 |
Haas E, McWherter CA, Scheraga HA. Conformational unfolding in the N-terminal region of ribonuclease A detected by nonradiative energy transfer: distribution of interresidue distances in the native, denatured, and reduced-denatured states Biopolymers - Peptide Science Section. 27: 1-21. PMID 3342273 DOI: 10.1002/Bip.360270102 |
0.51 |
|
| 1988 |
Amir D, Haas E. Reduced bovine pancreatic trypsin inhibitor has a compact structure Biochemistry. 27: 8889-8893. PMID 2466482 DOI: 10.1021/Bi00425A003 |
0.444 |
|
| 1987 |
Haas E, Montelione GT, McWherter CA, Scheraga HA. Local structure in a tryptic fragment of performic acid oxidized ribonuclease A corresponding to a proposed polypeptide chain-folding initiation site detected by tyrosine fluorescence lifetime and proton magnetic resonance measurements Biochemistry. 26: 1672-1683. PMID 3593685 DOI: 10.1021/Bi00380A028 |
0.444 |
|
| 1987 |
Amir D, Haas E. Estimation of intramolecular distance distributions in Bovine Pancreatic Trypsin Inhibitor by site-specific labeling and nonradiative excitation energy-transfer measurements Biochemistry. 26: 2162-2175. PMID 2441742 DOI: 10.1021/Bi00382A015 |
0.493 |
|
| 1986 |
McWherter CA, Haas E, Leed AR, Scheraga HA. Conformational unfolding in the N-terminal region of ribonuclease A detected by nonradiative energy transfer. Biochemistry. 25: 1951-63. PMID 3707922 DOI: 10.1021/bi00356a018 |
0.353 |
|
| 1986 |
Amir D, Levy DP, Levin Y, Haas E. Selective fluorescent labeling of amino groups of bovine pancreatic trypsin inhibitor by reductive alkylation Biopolymers. 25: 1645-1658. PMID 2429713 DOI: 10.1002/Bip.360250908 |
0.409 |
|
| 1986 |
Amir D, Haas E. Determination of intramolecular distance distributions in a globular protein by nonradiative excitation energy transfer measurements Biopolymers. 25: 235-240. PMID 2420384 DOI: 10.1002/Bip.360250205 |
0.439 |
|
| 1986 |
Amir D, Haas E. A series of site-specific fluorescently labeled BPTI derivatives prepared by nonselective acylation and chromatographic separations International Journal of Peptide and Protein Research. 27: 7-17. PMID 2419267 DOI: 10.1111/J.1399-3011.1986.Tb02760.X |
0.442 |
|
| 1985 |
Amir D, Varshavski L, Haas E. Selective fluorescent labeling at the α-amino group of bovine pancreatic trypsin inhibitor Biopolymers. 24: 623-638. DOI: 10.1002/Bip.360240404 |
0.471 |
|
| 1984 |
Ausio J, Greulich KO, Haas E, Wachtel E. Characterization of the fluorescence of the protamine thynnine and studies of binding to double-stranded DNA Biopolymers - Peptide Science Section. 23: 2559-2571. PMID 6518265 DOI: 10.1002/Bip.360231128 |
0.365 |
|
| 1984 |
Haas E, Steinberg IZ. Intramolecular dynamics of chain molecules monitored by fluctuations in efficiency of excitation energy transfer. A theoretical study. Biophysical Journal. 46: 429-37. PMID 6498263 DOI: 10.1016/S0006-3495(84)84040-0 |
0.77 |
|
| 1981 |
Katchalski-Katzir E, Haas E, Steinberg IZ. STUDY OF CONFORMATION AND INTRAMOLECULAR MOTILITY OF POLYPEPTIDES IN SOLUTION BY A NOVEL FLUORESCENCE METHOD Annals of the New York Academy of Sciences. 366: 44-61. DOI: 10.1111/J.1749-6632.1981.Tb20745.X |
0.751 |
|
| 1981 |
Berkovic GE, Ludmer Z, Haas E. Electronic energy trapping in a crystal with a dopant of higher singlet level than the host Journal of Luminescence. 543-546. DOI: 10.1016/0022-2313(81)90036-3 |
0.337 |
|
| 1978 |
Haas E, Katchalski-Katzir E, Steinberg IZ. Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarization. Biochemistry. 17: 5064-70. PMID 718874 DOI: 10.1021/Bi00616A032 |
0.735 |
|
| 1978 |
Haas E, Fischer G, Fischer E. Conformational equilibria in 1,2-diarylethylenes manifested in their emission spectra and lifetimes Journal of Physical Chemistry. 82: 1638-1643. DOI: 10.1021/J100503A014 |
0.322 |
|
| 1978 |
Haas E, Katchalski-Katzir E, Steinberg IZ. Brownian motion of the ends of oligopeptide chains in solution as estimated by energy transfer between the chain ends Biopolymers. 17: 11-31. DOI: 10.1002/Bip.1978.360170103 |
0.769 |
|
| 1976 |
Hazan G, Haas E, Steinberg IZ. The fluorescence decay of human serum albumin and its subfractions. Biochimica Et Biophysica Acta. 434: 144-53. PMID 938659 DOI: 10.1016/0005-2795(76)90044-1 |
0.748 |
|
| 1975 |
Haas E, Wilchek M, Katchalski-Katzir E, Steinberg IZ. Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer. Proceedings of the National Academy of Sciences of the United States of America. 72: 1807-11. PMID 1057171 DOI: 10.1073/Pnas.72.5.1807 |
0.78 |
|
| 1972 |
Grinvald A, Haas E, Steinberg IZ. Evaluation of the distribution of distances between energy donors and acceptors by fluorescence decay. Proceedings of the National Academy of Sciences of the United States of America. 69: 2273-7. PMID 16592008 DOI: 10.1073/Pnas.69.8.2273 |
0.762 |
|
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