Year |
Citation |
Score |
1999 |
Luo Y, Rydzewski J, De Graaf RA, Gruetter R, Garwood M, Schleich T. In vivo observation of lactate methyl proton magnetization transfer in rat C6 glioma Magnetic Resonance in Medicine. 41: 676-685. PMID 10332842 DOI: 10.1002/(Sici)1522-2594(199904)41:4<676::Aid-Mrm5>3.0.Co;2-D |
0.527 |
|
1997 |
Kuwata K, Liu H, Schleich T, James TL. Rotational correlation times of internuclear vectors in a DNA duplex with G-A mismatch determined in aqueous solution by complete relaxation matrix analysis of off-resonance ROESY (O-ROESY) spectra. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 128: 70-81. PMID 9345778 DOI: 10.1006/Jmre.1997.1212 |
0.327 |
|
1996 |
Willis JA, Schleich T. Oxidative-stress induced protein glutathione mixed-disulfide formation in the ocular lens Biochimica Et Biophysica Acta - Molecular Cell Research. 1313: 20-28. PMID 8781545 DOI: 10.1016/0167-4889(96)00049-3 |
0.317 |
|
1995 |
Willis JA, Schleich T. 13C-NMR spectroscopic studies of 2-mercaptoethanol-stimulated glutathione synthesis in the intact ocular lens Bba - Molecular Cell Research. 1265: 1-7. PMID 7857978 DOI: 10.1016/0167-4889(94)00195-K |
0.309 |
|
1994 |
Brooks D, Kuwata K, Schleich T. Determination of proton magnetization transfer rate constants in heterogeneous biological systems Magnetic Resonance in Medicine. 31: 331-336. PMID 8057807 DOI: 10.1002/Mrm.1910310315 |
0.304 |
|
1994 |
Kuwata K, Brooks D, Yang H, Schleich T. Relaxation-Matrix Formalism for Rotating-Frame Spin-Lattice Proton NMR Relaxation and Magnetization Transfer in the Presence of an Off-Resonance Irradiation Field Journal of Magnetic Resonance, Series B. 104: 11-25. PMID 8025811 DOI: 10.1006/Jmrb.1994.1049 |
0.37 |
|
1994 |
Kuwata K, Schleich T. Off-Resonance Rotating-Frame Nuclear Overhauser Effect Spectroscopy Journal of Magnetic Resonance, Series A. 111: 43-49. DOI: 10.1006/Jmra.1994.1224 |
0.314 |
|
1993 |
Rydzewski JM, Wang SX, Stevens A, Serdahl C, Schleich T. 13C NMR studies of protein motional dynamics in bovine, human, rat, and chicken ocular lenses Experimental Eye Research. 56: 305-316. PMID 8472786 DOI: 10.1006/Exer.1993.1040 |
0.37 |
|
1992 |
Willis JA, Schleich T. 13C NMR spectroscopic measurement of glutathione synthesis and antioxidant metabolism in the intact ocular lens Biochemical and Biophysical Research Communications. 186: 931-935. PMID 1497676 DOI: 10.1016/0006-291X(92)90835-9 |
0.319 |
|
1992 |
Schleich T, Stevens A, Michael D. FT-IR spectroscopic elucidation of lens crystallin protein secondary structure in solution Experimental Eye Research. 55: 195. DOI: 10.1016/0014-4835(92)90893-W |
0.321 |
|
1991 |
Caines GH, Schleich T, Rydzewski JM. Incorporation of magnetization transfer into the formalism for rotating-frame spin-lattice proton NMR relaxation in the presence of an off-resonance-irradiation field Journal of Magnetic Resonance (1969). 95: 558-566. DOI: 10.1016/0022-2364(91)90169-T |
0.352 |
|
1989 |
Haner RL, Schleich T. Measurement of translational motion by pulse-gradient spin-echo nuclear magnetic resonance Methods in Enzymology. 176: 418-446. PMID 2811696 DOI: 10.1016/0076-6879(89)76023-7 |
0.339 |
|
1989 |
Morgan CF, Schleich T, Caines GH, Farnsworth PN. Elucidation of intermediate (mobile) and slow (solidlike) protein motions in bovine lens homogenates by carbon-13 NMR spectroscopy. Biochemistry. 28: 5065-74. PMID 2765525 DOI: 10.1021/Bi00438A025 |
0.359 |
|
1987 |
GARWOOD M, SCHLEICH T, UGURBIL K. The Fourier Series Window Method for Spatially Localized NMR Spectroscopy. Annals of the New York Academy of Sciences. 508: 512-515. DOI: 10.1111/J.1749-6632.1987.Tb32953.X |
0.595 |
|
1987 |
Garwood M, Schleich T, Robin Bendall M. Simulation of selective pulse techniques for localized NMR spectroscopy Journal of Magnetic Resonance (1969). 73: 191-212. DOI: 10.1016/0022-2364(87)90191-0 |
0.504 |
|
1987 |
Garwood M, Schleich T, Ugurbil K. The Fourier Series Window method for spatially localized NMR spectroscopy. Implementation with composite pulses and multiple coils Annals of the New York Academy of Sciences. 508: 512-515. |
0.457 |
|
1986 |
Willis JA, Williams WF, Schleich T. Dynamic assessment of hexose monophosphate shunt activity in the intact rabbit lens by proton NMR spectroscopy Biochemical and Biophysical Research Communications. 138: 1068-1073. PMID 3753487 DOI: 10.1016/S0006-291X(86)80390-4 |
0.316 |
|
1986 |
Bogusky RT, Garwood M, Matson GB, Acosta G, Cowgill LD, Schleich T. Localization of phosphorus metabolites and sodium ions in the rat kidney. Magnetic Resonance in Medicine : Official Journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine. 3: 251-61. PMID 3713489 DOI: 10.1002/Mrm.1910030208 |
0.488 |
|
1986 |
Garwood M, U?urbil K, Schleich T, Petein M, Sublett E, From AHL, Bache RJ. In vivo spatially localized surface-coil NMR spectroscopy utilizing a fourier series window function and two surface coils Journal of Magnetic Resonance (1969). 69: 576-581. DOI: 10.1016/0022-2364(86)90179-4 |
0.51 |
|
1985 |
Schleich T, Matson GB, Willis JA, Acosta G, Serdahl C, Campbell P, Garwood M. Surface coil phosphorus-31 nuclear magnetic resonance studies of the intact eye. Experimental Eye Research. 40: 343-55. PMID 4065231 DOI: 10.1016/0014-4835(85)90148-4 |
0.533 |
|
1985 |
Farnsworth PN, Schleich T. Progress toward the establishment of nuclear magnetic resonance measurements as an index of in vivo lens functional integrity. Current Eye Research. 4: 291-7. PMID 4017627 DOI: 10.3109/02713688509000860 |
0.348 |
|
1985 |
Garwood M, Schleich T, Robin Bendall M, Pegg DT. Improved fourier series windows for localization in in vivo NMR spectroscopy Journal of Magnetic Resonance (1969). 65: 510-515. DOI: 10.1016/0022-2364(85)90138-6 |
0.53 |
|
1985 |
Garwood M, Schleich T, Ross BD, Matson GB, Winters WD. A modified rotating frame experiment based on a fourier series window function. Application to in vivo spatially localized NMR spectroscopy Journal of Magnetic Resonance (1969). 65: 239-251. DOI: 10.1016/0022-2364(85)90005-8 |
0.522 |
|
1984 |
Garwood M, Schleich T, Matson GB, Acosta G. Spatial localization of tissue metabolites by phosphorus-31 NMR rotating-frame zeugmatography Journal of Magnetic Resonance (1969). 60: 268-279. DOI: 10.1016/0022-2364(84)90330-5 |
0.514 |
|
1980 |
Schleich T, Verwolf GL, Twombly K. A circular dichroism study of Escherichia coli initiation factor-1 binding to polynucleotides Biochimica Et Biophysica Acta. 609: 313-320. PMID 6996729 DOI: 10.1016/0005-2787(80)90243-9 |
0.387 |
|
1979 |
Bear DG, Schleich T, Noller HF, Douthwaite S, Garrett RA. The ribosomal S4-RNA fragment melts cooperatively when complexed with protein S4 Febs Letters. 100: 99-102. PMID 374120 DOI: 10.1016/0014-5793(79)81139-4 |
0.561 |
|
1979 |
Omar S, Brown MF, Silver P, Schleich T. Histidyl and tyrosyl residue ionization studies of subtilisin novo Bba - Protein Structure. 578: 261-268. PMID 39621 DOI: 10.1016/0005-2795(79)90156-9 |
0.5 |
|
1977 |
Brown MF, Omar S, Raubach RA, Schleich T. Quenching of the tyrosyl and tryptophyl fluorescence of subtilisins Carlsberg and Novo by iodide Biochemistry. 16: 987-992. PMID 843526 DOI: 10.1021/Bi00624A028 |
0.447 |
|
1977 |
Bear DG, Schleich T, Noller HF, Garrett RA. Alteration of 5S RNA conformation by ribosomal proteins L18 and L25 Nucleic Acids Research. 4: 2511-2526. PMID 333392 DOI: 10.1093/Nar/4.7.2511 |
0.689 |
|
1977 |
Brown MF, Schleich T. Resolution of independently titrating spectral components of the ultraviolet circular dichroism of subtilisin enzymes by matrix rank analysis Bba - Enzymology. 485: 37-51. PMID 20969 DOI: 10.1016/0005-2744(77)90191-7 |
0.446 |
|
1976 |
Bear DG, Ng R, van Derveer D, Johnson NP, Thomas G, Schleich T, Noller HF. Alteration of polynucleotide secondary structure by ribosomal protein S1 Proceedings of the National Academy of Sciences of the United States of America. 73: 1824-1828. PMID 778845 DOI: 10.1073/Pnas.73.6.1824 |
0.7 |
|
1975 |
Brown MF, Schleich T. Circular dichroism and gel filtration behavior of subtilisin enzymes in concentrated solutions of guanidine hydrochloride Biochemistry. 14: 3069-3074. PMID 238582 DOI: 10.1021/Bi00685A005 |
0.47 |
|
1974 |
Rahn RO, Schleich T. Proton magnetic resonance studies of ultraviolet-irradiated apurinic acid. Nucleic Acids Research. 1: 999-1005. PMID 10793730 DOI: 10.1093/Nar/1.8.999 |
0.316 |
|
1973 |
Lerner DA, Schleich T. The solution behavior of poly L proline: II. Fluorescence behavior of labeled polyproline in water and concentrated aqueous neutral salt solutions Biopolymers. 12: 1011-1019. DOI: 10.1002/Bip.1973.360120506 |
0.304 |
|
1973 |
Schleich T, Yeh Y. The solution behavior of poly L proline: I. Light scattering studies in water and concentrated aqueous neutral salt solutions Biopolymers. 12: 993-1010. DOI: 10.1002/Bip.1973.360120505 |
0.307 |
|
1972 |
Schleich T, Blackburn BJ, Lapper RD, Smith ICP. A nuclear magnetic resonance study of the influence of aqueous sodium perchlorate and temperature on the solution conformations of uracil nucleosides and nucleotides Biochemistry. 11: 137-145. PMID 4333200 DOI: 10.1021/Bi00752A001 |
0.329 |
|
1971 |
Schleich T, Rollefson B, Von Hippel PH. Proton exchange of N-methylacetamide in concentrated aqueous electrolyte solutions. II. Acid catalysis in water-dioxane mixtures and base catalysis Journal of the American Chemical Society. 93: 7070-7074. |
0.594 |
|
1970 |
Schleich T, von Hippel PH. Ion-induced water-proton chemical shifts and the conformational stability of macromolecules. Biochemistry. 9: 1059-66. PMID 4313934 |
0.606 |
|
1966 |
Schleich T, Goldstein J. Gel filtration heterogeneity of Escherichia coli soluble RNA. Journal of Molecular Biology. 15: 136-146. PMID 5330214 DOI: 10.1016/S0022-2836(66)80215-2 |
0.494 |
|
1965 |
Schleich T, Goldstein J. Sulfur: Incorporation into the transfer fraction of soluble ribonucleic acid Science. 150: 1168-1170. PMID 5322339 DOI: 10.1126/Science.150.3700.1168 |
0.508 |
|
1964 |
SCHLEICH T, GOLDSTEIN J. GEL FILTRATION PROPERTIES OF CCD-PREPARED E. COLI B SRNA. Proceedings of the National Academy of Sciences of the United States Of. 52: 744-749. PMID 14212552 DOI: 10.1073/Pnas.52.3.744 |
0.408 |
|
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