Year |
Citation |
Score |
2001 |
Tanaka T, Ames J, Kainosho M, Stryer L, Ikura M. Refinement of the Solution Structure of Calcium-Free, Myristoylated Recoverin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4030 |
0.667 |
|
2000 |
Ames JB, Ikura M, Stryer L. Molecular structure of membrane-targeting calcium sensors in vision: recoverin and guanylate cyclase-activating protein 2. Methods in Enzymology. 316: 121-32. PMID 10800672 DOI: 10.1016/S0076-6879(00)16720-5 |
0.717 |
|
1999 |
Ames JB, Dizhoor AM, Ikura M, Palczewski K, Stryer L. Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases. The Journal of Biological Chemistry. 274: 19329-37. PMID 10383444 DOI: 10.1074/Jbc.274.27.19329 |
0.718 |
|
1998 |
Tanaka T, Ames JB, Kainosho M, Stryer L, Ikura M. Differential isotype labeling strategy for determining the structure of myristoylated recoverin by NMR spectroscopy. Journal of Biomolecular Nmr. 11: 135-52. PMID 9679292 DOI: 10.1023/A:1008212316986 |
0.683 |
|
1998 |
Erickson MA, Lagnado L, Zozulya S, Neubert TA, Stryer L, Baylor DA. The effect of recombinant recoverin on the photoresponse of truncated rod photoreceptors. Proceedings of the National Academy of Sciences of the United States of America. 95: 6474-9. PMID 9600991 DOI: 10.1073/Pnas.95.11.6474 |
0.347 |
|
1997 |
Ames JB, Ishima R, Tanaka T, Gordon JI, Stryer L, Ikura M. Molecular mechanics of calcium-myristoyl switches. Nature. 389: 198-202. PMID 9296500 DOI: 10.1038/38310 |
0.718 |
|
1996 |
Ames JB, Tanaka T, Stryer L, Ikura M. Portrait of a myristoyl switch protein. Current Opinion in Structural Biology. 6: 432-8. PMID 8794166 DOI: 10.1016/S0959-440X(96)80106-0 |
0.701 |
|
1995 |
Ames JB, Tanaka T, Ikura M, Stryer L. Nuclear magnetic resonance evidence for Ca(2+)-induced extrusion of the myristoyl group of recoverin. The Journal of Biological Chemistry. 270: 30909-13. PMID 8537345 DOI: 10.1074/Jbc.270.52.30909 |
0.702 |
|
1995 |
Ames JB, Porumb T, Tanaka T, Ikura M, Stryer L. Amino-terminal myristoylation induces cooperative calcium binding to recoverin. The Journal of Biological Chemistry. 270: 4526-33. PMID 7876221 DOI: 10.1074/Jbc.270.9.4526 |
0.705 |
|
1995 |
Zozulya S, Ladant D, Stryer L. Expression and characterization of calcium-myristoyl switch proteins. Methods in Enzymology. 250: 383-93. PMID 7651166 DOI: 10.1016/0076-6879(95)50086-3 |
0.4 |
|
1995 |
Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature. 376: 444-7. PMID 7630423 DOI: 10.1038/376444A0 |
0.721 |
|
1994 |
Ames JB, Tanaka T, Stryer L, Ikura M. Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch. Biochemistry. 33: 10743-53. PMID 8075075 DOI: 10.1021/Bi00201A023 |
0.703 |
|
1993 |
Flaherty KM, Zozulya S, Stryer L, McKay DB. Three-dimensional structure of recoverin, a calcium sensor in vision. Cell. 75: 709-16. PMID 8242744 DOI: 10.1016/0092-8674(93)90491-8 |
0.304 |
|
1993 |
Boniface JJ, Allbritton NL, Reay PA, Kantor RM, Stryer L, Davis MM. pH affects both the mechanism and the specificity of peptide binding to a class II major histocompatibility complex molecule. Biochemistry. 32: 11761-8. PMID 8218246 DOI: 10.1021/Bi00095A003 |
0.504 |
|
1993 |
Hurley JB, Dizhoor AM, Ray S, Stryer L. Recoverin's role: conclusion withdrawn. Science (New York, N.Y.). 260: 740. PMID 8097896 DOI: 10.1126/Science.8097896 |
0.479 |
|
1993 |
Karpen JW, Brown RL, Stryer L, Baylor DA. Interactions between divalent cations and the gating machinery of cyclic GMP-activated channels in salamander retinal rods. The Journal of General Physiology. 101: 1-25. PMID 7679715 DOI: 10.1085/Jgp.101.1.1 |
0.322 |
|
1992 |
Allbritton NL, Meyer T, Stryer L. Range of messenger action of calcium ion and inositol 1,4,5-trisphosphate. Science (New York, N.Y.). 258: 1812-5. PMID 1465619 DOI: 10.1126/Science.1465619 |
0.539 |
|
1992 |
Zozulya S, Stryer L. Calcium-myristoyl protein switch. Proceedings of the National Academy of Sciences of the United States of America. 89: 11569-73. PMID 1454850 DOI: 10.1073/Pnas.89.23.11569 |
0.376 |
|
1992 |
Dizhoor AM, Ericsson LH, Johnson RS, Kumar S, Olshevskaya E, Zozulya S, Neubert TA, Stryer L, Hurley JB, Walsh KA. The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids. The Journal of Biological Chemistry. 267: 16033-6. PMID 1386601 |
0.507 |
|
1992 |
Ray S, Zozulya S, Niemi GA, Flaherty KM, Brolley D, Dizhoor AM, McKay DB, Hurley J, Stryer L. Cloning, expression, and crystallization of recoverin, a calcium sensor in vision. Proceedings of the National Academy of Sciences of the United States of America. 89: 5705-9. PMID 1385864 DOI: 10.1073/Pnas.89.13.5705 |
0.558 |
|
1992 |
Meyer T, Hanson PI, Stryer L, Schulman H. Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science (New York, N.Y.). 256: 1199-202. PMID 1317063 DOI: 10.1126/Science.256.5060.1199 |
0.324 |
|
1991 |
Wagner JA, Cozens AL, Schulman H, Gruenert DC, Stryer L, Gardner P. Activation of chloride channels in normal and cystic fibrosis airway epithelial cells by multifunctional calcium/calmodulin-dependent protein kinase. Nature. 349: 793-6. PMID 1705665 DOI: 10.1038/349793a0 |
0.322 |
|
1991 |
Dizhoor AM, Ray S, Kumar S, Niemi G, Spencer M, Brolley D, Walsh KA, Philipov PP, Hurley JB, Stryer L. Recoverin: a calcium sensitive activator of retinal rod guanylate cyclase. Science (New York, N.Y.). 251: 915-8. PMID 1672047 DOI: 10.1126/Science.1672047 |
0.565 |
|
1990 |
Mathies RA, Peck K, Stryer L. Optimization of high-sensitivity fluorescence detection. Analytical Chemistry. 62: 1786-91. PMID 2240569 DOI: 10.1021/Ac00216A012 |
0.595 |
|
1990 |
Wensel TG, Stryer L. Activation mechanism of retinal rod cyclic GMP phosphodiesterase probed by fluorescein-labeled inhibitory subunit. Biochemistry. 29: 2155-61. PMID 2158346 DOI: 10.1021/Bi00460A028 |
0.559 |
|
1990 |
Meyer T, Wensel T, Stryer L. Kinetics of calcium channel opening by inositol 1,4,5-trisphosphate. Biochemistry. 29: 32-7. PMID 1691015 DOI: 10.1021/Bi00453A004 |
0.589 |
|
1990 |
Mathies RA, Peck K, Stryer L. High-sensitivity single-molecule fluorescence detection Proceedings of Spie - the International Society For Optical Engineering. 1205: 52-59. |
0.544 |
|
1989 |
Peck K, Stryer L, Glazer AN, Mathies RA. Single-molecule fluorescence detection: autocorrelation criterion and experimental realization with phycoerythrin. Proceedings of the National Academy of Sciences of the United States of America. 86: 4087-91. PMID 2726766 DOI: 10.1073/Pnas.86.11.4087 |
0.587 |
|
1989 |
Brown RL, Stryer L. Expression in bacteria of functional inhibitory subunit of retinal rod cGMP phosphodiesterase. Proceedings of the National Academy of Sciences of the United States of America. 86: 4922-6. PMID 2544882 DOI: 10.1073/Pnas.86.13.4922 |
0.325 |
|
1988 |
Dangl JL, Wensel TG, Morrison SL, Stryer L, Herzenberg LA, Oi VT. Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. The Embo Journal. 7: 1989-94. PMID 3138110 DOI: 10.1002/J.1460-2075.1988.Tb03037.X |
0.525 |
|
1988 |
Schneider WP, Wensel TG, Stryer L, Oi VT. Genetically engineered immunoglobulins reveal structural features controlling segmental flexibility. Proceedings of the National Academy of Sciences of the United States of America. 85: 2509-13. PMID 3128789 DOI: 10.1073/Pnas.85.8.2509 |
0.552 |
|
1988 |
Meyer T, Stryer L. Molecular model for receptor-stimulated calcium spiking. Proceedings of the National Academy of Sciences of the United States of America. 85: 5051-5. PMID 2455890 DOI: 10.1073/Pnas.85.14.5051 |
0.308 |
|
1988 |
Koch KW, Stryer L. Highly cooperative feedback control of retinal rod guanylate cyclase by calcium ions. Nature. 334: 64-6. PMID 2455233 DOI: 10.1038/334064a0 |
0.354 |
|
1988 |
Meyer T, Holowka D, Stryer L. Highly cooperative opening of calcium channels by inositol 1,4,5-trisphosphate. Science (New York, N.Y.). 240: 653-6. PMID 2452482 DOI: 10.1126/Science.2452482 |
0.324 |
|
1988 |
Karpen JW, Zimmerman AL, Stryer L, Baylor DA. Gating kinetics of the cyclic-GMP-activated channel of retinal rods: flash photolysis and voltage-jump studies. Proceedings of the National Academy of Sciences of the United States of America. 85: 1287-91. PMID 2448798 DOI: 10.1073/Pnas.85.4.1287 |
0.32 |
|
1988 |
Dangl JL, Wensel TG, Morrison SL, Stryer L, Herzenberg LA, Oi VT. Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. The Embo Journal. 7: 1989-1994. DOI: 10.1002/j.1460-2075.1988.tb03037.x |
0.456 |
|
1986 |
Wensel TG, Stryer L. Reciprocal control of retinal rod cyclic GMP phosphodiesterase by its gamma subunit and transducin. Proteins. 1: 90-9. PMID 2835761 DOI: 10.1002/Prot.340010114 |
0.542 |
|
1986 |
Stryer L. Cyclic GMP cascade of vision. Annual Review of Neuroscience. 9: 87-119. PMID 2423011 DOI: 10.1146/annurev.ne.09.030186.000511 |
0.351 |
|
1986 |
Tsuda M, Tsuda T, Terayama Y, Fukada Y, Akino T, Yamanaka G, Stryer L, Katada T, Ui M, Ebrey T. Kinship of cephalopod photoreceptor G-protein with vertebrate transducin Febs Letters. 198: 5-10. DOI: 10.1016/0014-5793(86)81173-5 |
0.549 |
|
1985 |
Stryer L. Molecular design of an amplification cascade in vision. Biopolymers. 24: 29-47. PMID 2985139 DOI: 10.1002/bip.360240105 |
0.35 |
|
1985 |
Zimmerman AL, Yamanaka G, Eckstein F, Baylor DA, Stryer L. Interaction of hydrolysis-resistant analogs of cyclic GMP with the phosphodiesterase and light-sensitive channel of retinal rod outer segments. Proceedings of the National Academy of Sciences of the United States of America. 82: 8813-7. PMID 2417228 DOI: 10.1073/Pnas.82.24.8813 |
0.317 |
|
1984 |
Vuong TM, Chabre M, Stryer L. Millisecond activation of transducin in the cyclic nucleotide cascade of vision. Nature. 311: 659-61. PMID 6090950 DOI: 10.1038/311659A0 |
0.31 |
|
1983 |
Stryer L. Transducin and the cyclic GMP phosphodiesterase: amplifier proteins in vision. Cold Spring Harbor Symposia On Quantitative Biology. 48: 841-52. PMID 6327179 DOI: 10.1101/Sqb.1983.048.01.087 |
0.308 |
|
1983 |
Stryer L, Hurley JB, Fung BK. Transducin and the cyclic GMP phosphodiesterase of retinal rod outer segments. Methods in Enzymology. 96: 617-27. PMID 6318024 DOI: 10.1016/S0076-6879(83)96054-8 |
0.562 |
|
1982 |
Stryer L, Thomas DD, Carlsen WF. Fluorescence energy transfer measurements of distances in rhodopsin and the purple membrane protein. Methods in Enzymology. 81: 668-78. PMID 7098907 DOI: 10.1016/S0076-6879(82)81092-6 |
0.486 |
|
1982 |
Thomas DD, Stryer L. Transverse location of the retinal chromophore of rhodopsin in rod outer segment disc membranes. Journal of Molecular Biology. 154: 145-57. PMID 7077659 DOI: 10.1016/0022-2836(82)90422-3 |
0.489 |
|
1982 |
Stryer L, Thomas DD, Meares CF. Diffusion-enhanced fluorescence energy transfer. Annual Review of Biophysics and Bioengineering. 11: 203-22. PMID 7049062 DOI: 10.1146/annurev.bb.11.060182.001223 |
0.551 |
|
1982 |
Yamamoto K, Pardee JD, Reidler J, Stryer L, Spudich JA. Mechanism of interaction of Dictyostelium severin with actin filaments. The Journal of Cell Biology. 95: 711-9. PMID 6897549 DOI: 10.1083/Jcb.95.3.711 |
0.332 |
|
1982 |
Oi VT, Glazer AN, Stryer L. Fluorescent phycobiliprotein conjugates for analyses of cells and molecules. The Journal of Cell Biology. 93: 981-6. PMID 6749865 DOI: 10.1083/Jcb.93.3.981 |
0.307 |
|
1982 |
Hurley JB, Stryer L. Purification and characterization of the gamma regulatory subunit of the cyclic GMP phosphodiesterase from retinal rod outer segments. The Journal of Biological Chemistry. 257: 11094-9. PMID 6286681 |
0.466 |
|
1982 |
Abood ME, Hurley JB, Pappone MC, Bourne HR, Stryer L. Functional homology between signal-coupling proteins. Cholera toxin inactivates the GTPase activity of transducin. The Journal of Biological Chemistry. 257: 10540-3. PMID 6125514 |
0.513 |
|
1981 |
Fung BK, Hurley JB, Stryer L. Flow of information in the light-triggered cyclic nucleotide cascade of vision. Proceedings of the National Academy of Sciences of the United States of America. 78: 152-6. PMID 6264430 DOI: 10.1073/Pnas.78.1.152 |
0.552 |
|
1981 |
Stryer L, Hurley JB, Fung BKK. Chapter 5 First Stage of Amplification in the Cyclic-Nucleotide Cascade of Vision Current Topics in Membranes and Transport. 15: 93-108. DOI: 10.1016/S0070-2161(08)60496-7 |
0.547 |
|
1981 |
Stryer L, Hurley JB, Fung BKK. Transducin: an amplifier protein in vision Trends in Biochemical Sciences. 6: 245-247. DOI: 10.1016/0968-0004(81)90089-X |
0.549 |
|
1981 |
Meares CF, Yeh SM, Stryer L. Exchange interaction contribution to energy transfer between ions in the rapid-diffusion limit Journal of the American Chemical Society. 103: 1607-1609. DOI: 10.1002/Chin.198127297 |
0.504 |
|
1980 |
Yeager M, Schoenborn B, Engelman D, Moore P, Stryer L. Neutron diffraction analysis of the structure of rod photoreceptor membranes in intact retinas. Journal of Molecular Biology. 137: 315-48. PMID 6973637 DOI: 10.1016/0022-2836(80)90319-8 |
0.528 |
|
1980 |
Kwok-Keung Fung B, Stryer L. Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments. Proceedings of the National Academy of Sciences of the United States of America. 77: 2500-4. PMID 6930647 DOI: 10.1073/Pnas.77.5.2500 |
0.342 |
|
1979 |
Munro I, Pecht I, Stryer L. Subnanosecond motions of tryptophan residues in proteins. Proceedings of the National Academy of Sciences of the United States of America. 76: 56-60. PMID 284374 DOI: 10.1073/Pnas.76.1.56 |
0.314 |
|
1979 |
Morrow JS, Veatch WR, Stryer L. Transmembrane channel activity of gramicidin A analogs: effects of modification and deletion of the amino-terminal residue. Journal of Molecular Biology. 132: 733-8. PMID 93642 DOI: 10.1016/0022-2836(79)90386-3 |
0.713 |
|
1979 |
Koeppe RE, Berg JM, Hodgson KO, Stryer L. Gramicidin A crystals contain two cation binding sites per channel. Nature. 279: 723-5. PMID 88018 DOI: 10.1038/279723A0 |
0.548 |
|
1978 |
Thomas DD, Carlsen WF, Stryer L. Fluorescence energy transfer in the rapid-diffusion limit. Proceedings of the National Academy of Sciences of the United States of America. 75: 5746-50. PMID 16592590 DOI: 10.1073/Pnas.75.12.5746 |
0.447 |
|
1978 |
Fung BK, Stryer L. Surface density determination in membranes by fluorescence energy transfer. Biochemistry. 17: 5241-8. PMID 728398 DOI: 10.1021/Bi00617A025 |
0.305 |
|
1978 |
Koeppe RE, Hodgson KO, Stryer L. Helical channels in crystals of gramicidin A and of a cesium--gramicidin A complex: an x-ray diffraction study. Journal of Molecular Biology. 121: 41-54. PMID 77905 DOI: 10.1016/0022-2836(78)90261-9 |
0.505 |
|
1978 |
Pober JS, Iwanij V, Reich E, Stryer L. Transglutaminase-catalyzed insertion of a fluorescent probe into the protease-sensitive region of rhodopsin. Biochemistry. 17: 2163-8. PMID 27209 DOI: 10.1021/Bi00604A021 |
0.494 |
|
1978 |
Morrow JS, Veatch WR, Stryer L. Synthetic replacement of the N-terminal amino acid of gramicidin A: effect on transmembrane channel conductance Biophysical Journal. 21: 26a. |
0.694 |
|
1977 |
Mathies R, Freedman TB, Stryer L. Resonance Raman studies of the conformation of retinal in rhodopsin and isorhodopsin. Journal of Molecular Biology. 109: 367-72. PMID 839546 DOI: 10.1016/S0022-2836(77)80040-5 |
0.574 |
|
1977 |
Veatch WR, Stryer L. Effect of cholesterol on the rotational mobility of diphenylhexatriene in liposomes: a nanosecond fluorescence anisotrophy study. Journal of Molecular Biology. 117: 1109-13. PMID 606835 DOI: 10.1016/S0022-2836(77)80017-X |
0.716 |
|
1977 |
Shaper JH, Stryer L. Accessibility of the carbohydrate moiety of membrane-boound rhodopsin to enzymatic and chemical modification. Journal of Supramolecular Structure. 6: 291-9. PMID 592816 DOI: 10.1002/jss.400060302 |
0.329 |
|
1977 |
Veatch W, Stryer L. The dimeric nature of the gramicidin A transmembrane channel: conductance and fluorescence energy transfer studies of hybrid channels. Journal of Molecular Biology. 113: 89-102. PMID 69713 DOI: 10.1016/0022-2836(77)90042-0 |
0.738 |
|
1976 |
Mathies R, Stryer L. Retinal has a highly dipolar vertically excited singlet state: implications for vision. Proceedings of the National Academy of Sciences of the United States of America. 73: 2169-73. PMID 1065867 DOI: 10.1073/pnas.73.7.2169 |
0.589 |
|
1976 |
Mathies R, Oseroff AR, Stryer L. Rapid-flow resonance Raman spectroscopy of photolabile molecules: rhodopsin and isorhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 73: 1-5. PMID 1061102 DOI: 10.1073/pnas.73.1.1 |
0.575 |
|
1975 |
Pober JS, Stryer L. Letter to the editor: Light dissociates enzymatically-cleaved rhodopsin into two different fragments. Journal of Molecular Biology. 95: 477-81. PMID 1171252 DOI: 10.1016/0022-2836(75)90204-1 |
0.472 |
|
1975 |
Veatch WR, Mathies R, Eisenberg M, Stryer L. Simultaneous fluorescence and conductance studies of planar bilayer membranes containing a highly active and fluorescent analog of gramicidin A. Journal of Molecular Biology. 99: 75-92. PMID 54431 DOI: 10.1016/S0022-2836(75)80160-4 |
0.771 |
|
1973 |
Steinemann A, Wu C, Stryer L. Conformational aspects of rhodopsin and retinal disc membranes. Journal of Supramolecular Structure. 1: 348-53. PMID 4767463 DOI: 10.1002/jss.400010410 |
0.562 |
|
1973 |
Renthal R, Steinemann A, Stryer L. The carbohydrate moiety of rhodopsin: lectin-binding, chemical modification and fluorescence studies. Experimental Eye Research. 17: 511-5. PMID 4361169 DOI: 10.1016/0014-4835(73)90081-X |
0.362 |
|
1972 |
Wu CW, Stryer L. Proximity relationships in rhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 69: 1104-8. PMID 4504322 DOI: 10.1073/Pnas.69.5.1104 |
0.567 |
|
1971 |
Yguerabide J, Stryer L. Fluorescence spectroscopy of an oriented model membrane. Proceedings of the National Academy of Sciences of the United States of America. 68: 1217-21. PMID 5288369 DOI: 10.1073/Pnas.68.6.1217 |
0.332 |
|
1971 |
Waggoner AS, Stryer L. Induced optical activity of the metarhodopsins. Biochemistry. 10: 3250-4. PMID 5119249 DOI: 10.1021/Bi00793A014 |
0.489 |
|
1970 |
Waggoner AS, Stryer L. Fluorescent probes of biological membranes. Proceedings of the National Academy of Sciences of the United States of America. 67: 579-89. PMID 5289011 DOI: 10.1073/Pnas.67.2.579 |
0.563 |
|
1969 |
Galley WC, Stryer L. Triplet-singlet energy transfer in proteins. Biochemistry. 8: 1831-8. PMID 5785207 DOI: 10.1021/Bi00833A008 |
0.683 |
|
1968 |
Stryer L. Fluorescence spectroscopy of proteins. Science (New York, N.Y.). 162: 526-33. PMID 5706935 DOI: 10.1126/Science.162.3853.526 |
0.325 |
|
1968 |
Galley WC, Stryer L. Triplet-triplet energy transfer in proteins as a criterion of proximity. Proceedings of the National Academy of Sciences of the United States of America. 60: 108-14. PMID 4968632 |
0.663 |
|
1965 |
Stryer L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. Journal of Molecular Biology. 13: 482-95. PMID 5867031 DOI: 10.1016/S0022-2836(65)80111-5 |
0.333 |
|
1965 |
Stryer L, Griffith OH. A spin-labeled hapten. Proceedings of the National Academy of Sciences of the United States of America. 54: 1785-91. PMID 4286565 |
0.377 |
|
1964 |
STRYER L, KENDREW JC, WATSON HC. THE MODE OF ATTACHMENT OF THE AZIDE ION TO SPERM WHALE METMYOGLOBIN. Journal of Molecular Biology. 8: 96-104. PMID 14149967 DOI: 10.1016/S0022-2836(64)80152-2 |
0.638 |
|
1964 |
Watson H, Kendrew J, Stryer L. The binding of p-chloromercuribenzene sulphonate to crystals of sperm whale myoglobin Journal of Molecular Biology. 8: 166-169. DOI: 10.1016/S0022-2836(64)80157-1 |
0.615 |
|
1963 |
STRYER L, COHEN C, LANGRIDGE R. Axial period of fibrinogen and fibrin. Nature. 197: 793-4. PMID 13993227 DOI: 10.1038/197793a0 |
0.356 |
|
1962 |
Stryer L, Blout ER. Dispersion der optischen Drehung von an Makromolekülen gebundenen Farbstoffen. Kationische Farbstoffe: Polyglutaminsäure-Komplexe Kolloid-Zeitschrift & Zeitschrift FüR Polymere. 183: 93-93. DOI: 10.1007/BF02260610 |
0.4 |
|
1961 |
Stryer L, Blout ER. Optical rotatory dispersion of dyes bound to macromolecules. Cationic dyes: Polyglutamic acid complexes Journal of the American Chemical Society. 83: 1411-1418. DOI: 10.1021/Ja01467A036 |
0.514 |
|
1959 |
Blout ER, Stryer L. ANOMALOUS OPTICAL ROTATORY DISPERSION OF DYE: POLYPEPTIDE COMPLEXES. Proceedings of the National Academy of Sciences of the United States of America. 45: 1591-3. PMID 16590549 |
0.582 |
|
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