Year |
Citation |
Score |
2000 |
Richards FM, Lamed R, Wynn R, Patel D, Olack G. Methylene as a possible universal footprinting reagent that will include hydrophobic surface areas: overview and feasibility: properties of diazirine as a precursor. Protein Science : a Publication of the Protein Society. 9: 2506-17. PMID 11206072 DOI: 10.1110/Ps.9.12.2506 |
0.348 |
|
2000 |
Fleming PJ, Richards FM. Protein packing: dependence on protein size, secondary structure and amino acid composition. Journal of Molecular Biology. 299: 487-98. PMID 10860754 DOI: 10.1006/Jmbi.2000.3750 |
0.408 |
|
1997 |
Wynn R, Harkins PC, Richards FM, Fox RO. Comparison of straight chain and cyclic unnatural amino acids embedded in the core of staphylococcal nuclease. Protein Science : a Publication of the Protein Society. 6: 1621-6. PMID 9260275 DOI: 10.1002/Pro.5560060803 |
0.537 |
|
1996 |
Wynn R, Harkins PC, Richards FM, Fox RO. Mobile unnatural amino acid side chains in the core of staphylococcal nuclease. Protein Science : a Publication of the Protein Society. 5: 1026-31. PMID 8762134 DOI: 10.1002/Pro.5560050605 |
0.552 |
|
1995 |
Wynn R, Anderson CL, Richards FM, Fox RO. Interactions in nonnative and truncated forms of staphylococcal nuclease as indicated by mutational free energy changes. Protein Science : a Publication of the Protein Society. 4: 1815-23. PMID 8528079 DOI: 10.1002/Pro.5560040916 |
0.566 |
|
1995 |
Wynn R, Richards FM. Measuring thiol-disulfide exchange equilibrium constants for single cysteine-containing proteins. Methods in Enzymology. 251: 375-82. PMID 7651219 DOI: 10.1016/0076-6879(95)51141-5 |
0.334 |
|
1995 |
Wynn R, Richards FM. Chemical modification of protein thiols: formation of mixed disulfides. Methods in Enzymology. 251: 351-6. PMID 7651216 DOI: 10.1016/0076-6879(95)51138-5 |
0.353 |
|
1995 |
Wynn R, Cocco MJ, Richards FM. Mixed disulfide intermediates during the reduction of disulfides by Escherichia coli thioredoxin. Biochemistry. 34: 11807-13. PMID 7547914 DOI: 10.1021/Bi00037A019 |
0.313 |
|
1995 |
Lim WA, Richards FM, Fox RO. Erratum: Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains Nature. 374: 94-94. DOI: 10.1038/374094a0 |
0.634 |
|
1994 |
Lim WA, Hodel A, Sauer RT, Richards FM. The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proceedings of the National Academy of Sciences of the United States of America. 91: 423-7. PMID 8278404 DOI: 10.1073/Pnas.91.1.423 |
0.694 |
|
1994 |
Thomson J, Ratnaparkhi GS, Varadarajan R, Sturtevant JM, Richards FM. Thermodynamic and structural consequences of changing a sulfur atom to a methylene group in the M13Nle mutation in ribonuclease-S. Biochemistry. 33: 8587-93. PMID 8031793 DOI: 10.1021/Bi00194A025 |
0.614 |
|
1994 |
Wishart DS, Boyko RF, Willard L, Richards FM, Sykes BD. SEQSEE: a comprehensive program suite for protein sequence analysis. Computer Applications in the Biosciences : Cabios. 10: 121-32. PMID 8019859 DOI: 10.1093/Bioinformatics/10.2.121 |
0.472 |
|
1994 |
Hellinga HW, Richards FM. Optimal sequence selection in proteins of known structure by simulated evolution. Proceedings of the National Academy of Sciences of the United States of America. 91: 5803-7. PMID 8016069 DOI: 10.1073/Pnas.91.13.5803 |
0.356 |
|
1994 |
Lim WA, Fox RO, Richards FM. Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5. Protein Science : a Publication of the Protein Society. 3: 1261-6. PMID 7987221 DOI: 10.1002/Pro.5560030812 |
0.676 |
|
1994 |
Lim WA, Richards FM, Fox RO. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature. 372: 375-9. PMID 7802869 DOI: 10.1038/372375A0 |
0.669 |
|
1994 |
Lim WA, Richards FM. Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition. Nature Structural Biology. 1: 221-5. PMID 7656049 DOI: 10.1038/Nsb0494-221 |
0.578 |
|
1993 |
Wynn R, Richards FM. Unnatural amino acid packing mutants of Escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques. Protein Science : a Publication of the Protein Society. 2: 395-403. PMID 8453377 DOI: 10.1002/Pro.5560020311 |
0.351 |
|
1993 |
Wishart DS, Sykes BD, Richards FM. Improved synthetic methods for the selective deuteration of aromatic amino acids: applications of selective protonation towards the identification of protein folding intermediates through nuclear magnetic resonance. Biochimica Et Biophysica Acta. 1164: 36-46. PMID 8390859 DOI: 10.1016/0167-4838(93)90109-5 |
0.479 |
|
1993 |
Wynn R, Richards FM. Partitioning the effects of changes in a protein to the folded or unfolded forms by using a thermodynamic cycle: a change in Escherichia coli thioredoxin does not affect the unfolded state. Biochemistry. 32: 12922-7. PMID 8251515 DOI: 10.1021/Bi00210A046 |
0.386 |
|
1993 |
Richards FM, Lim WA. An analysis of packing in the protein folding problem. Quarterly Reviews of Biophysics. 26: 423-98. PMID 8058892 DOI: 10.1017/S0033583500002845 |
0.621 |
|
1992 |
Wishart DS, Sykes BD, Richards FM. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31: 1647-51. PMID 1737021 DOI: 10.1021/Bi00121A010 |
0.519 |
|
1992 |
Varadarajan R, Connelly PR, Sturtevant JM, Richards FM. Heat capacity changes for protein-peptide interactions in the ribonuclease S system. Biochemistry. 31: 1421-6. PMID 1736999 DOI: 10.1021/Bi00120A019 |
0.615 |
|
1992 |
Varadarajan R, Richards FM. Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: packing and cavities. Biochemistry. 31: 12315-27. PMID 1463720 DOI: 10.1021/Bi00164A005 |
0.607 |
|
1992 |
Kim EE, Varadarajan R, Wyckoff HW, Richards FM. Refinement of the crystal structure of ribonuclease S. Comparison with and between the various ribonuclease A structures. Biochemistry. 31: 12304-14. PMID 1463719 DOI: 10.1021/Bi00164A004 |
0.784 |
|
1992 |
Hellinga HW, Wynn R, Richards FM. The hydrophobic core of Escherichia coli thioredoxin shows a high tolerance to nonconservative single amino acid substitutions. Biochemistry. 31: 11203-9. PMID 1445859 DOI: 10.1021/Bi00160A034 |
0.347 |
|
1992 |
Kaminsky SM, Richards FM. Differences in hydrogen exchange behavior between the oxidized and reduced forms of Escherichia coli thioredoxin. Protein Science : a Publication of the Protein Society. 1: 10-21. PMID 1339022 DOI: 10.1002/Pro.5560010103 |
0.397 |
|
1992 |
Kaminsky SM, Richards FM. Reduction of thioredoxin significantly decreases its partial specific volume and adiabatic compressibility. Protein Science : a Publication of the Protein Society. 1: 22-30. PMID 1304879 DOI: 10.1002/Pro.5560010104 |
0.343 |
|
1992 |
Wishart DS, Sykes BD, Richards FM. An improved synthesis of α-13C glycine and heteronuclear NMR studies of its incorporation into thioredoxin Journal of Labelled Compounds and Radiopharmaceuticals. 31: 1019-1028. DOI: 10.1002/Jlcr.2580311209 |
0.471 |
|
1991 |
Wishart DS, Sykes BD, Richards FM. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. Journal of Molecular Biology. 222: 311-33. PMID 1960729 DOI: 10.1016/0022-2836(91)90214-Q |
0.495 |
|
1991 |
Wishart DS, Sykes BD, Richards FM. Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy. Febs Letters. 293: 72-80. PMID 1959674 DOI: 10.1016/0014-5793(91)81155-2 |
0.5 |
|
1991 |
Hellinga HW, Richards FM. Construction of new ligand binding sites in proteins of known structure. I. Computer-aided modeling of sites with pre-defined geometry. Journal of Molecular Biology. 222: 763-85. PMID 1749000 DOI: 10.1016/0022-2836(91)90510-D |
0.348 |
|
1991 |
Hellinga HW, Caradonna JP, Richards FM. Construction of new ligand binding sites in proteins of known structure. II. Grafting of a buried transition metal binding site into Escherichia coli thioredoxin. Journal of Molecular Biology. 222: 787-803. PMID 1660933 DOI: 10.1016/0022-2836(91)90511-4 |
0.312 |
|
1991 |
Anfinsen CB, Edsall JT, Eisenberg D, Richards FM. Preface Advances in Protein Chemistry. 42: vii-viii. DOI: 10.1016/S0065-3233(08)60229-6 |
0.394 |
|
1991 |
Kundrot CE, Ponder JW, Richards FM. Algorithms for calculating excluded volume and its derivatives as a function of molecular conformation and their use in energy minimization Journal of Computational Chemistry. 12: 402-409. DOI: 10.1002/Jcc.540120314 |
0.303 |
|
1990 |
Connelly PR, Varadarajan R, Sturtevant JM, Richards FM. Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry. Biochemistry. 29: 6108-14. PMID 2383573 DOI: 10.1021/Bi00477A031 |
0.636 |
|
1990 |
Borden KL, Richards FM. Folding of the reduced form of the thioredoxin from bacteriophage T4. Biochemistry. 29: 8207-10. PMID 2252882 DOI: 10.1021/Bi00488A002 |
0.623 |
|
1990 |
Borden KL, Richards FM. Folding kinetics of phage T4 thioredoxin. Biochemistry. 29: 3071-7. PMID 2186806 DOI: 10.1021/Bi00464A025 |
0.592 |
|
1989 |
Forman-Kay JD, Clore GM, Driscoll PC, Wingfield P, Richards FM, Gronenborn AM. A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin. Biochemistry. 28: 7088-97. PMID 2684271 DOI: 10.1021/Bi00443A045 |
0.348 |
|
1988 |
Richards FM, Kundrot CE. Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure. Proteins. 3: 71-84. PMID 3399495 DOI: 10.1002/Prot.340030202 |
0.385 |
|
1988 |
Kundrot CE, Richards FM. Effect of hydrostatic pressure on the solvent in crystals of hen egg-white lysozyme. Journal of Molecular Biology. 200: 401-10. PMID 3373535 DOI: 10.1016/0022-2836(88)90249-5 |
0.319 |
|
1988 |
Segawa S, Richards FM. Identification of regions of potential flexibility in protein structures: folding units and correlations with intron positions. Biopolymers. 27: 23-40. PMID 3342276 DOI: 10.1002/Bip.360270103 |
0.367 |
|
1988 |
LeMaster DM, Richards FM. NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation. Biochemistry. 27: 142-50. PMID 3280013 DOI: 10.1021/Bi00401A022 |
0.334 |
|
1987 |
Kundrot CE, Richards FM. Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. Journal of Molecular Biology. 193: 157-70. PMID 3586017 DOI: 10.1016/0022-2836(87)90634-6 |
0.349 |
|
1987 |
Kelley RF, Richards FM. Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding. Biochemistry. 26: 6765-74. PMID 3322388 DOI: 10.1021/Bi00395A028 |
0.328 |
|
1987 |
Ponder JW, Richards FM. Internal packing and protein structural classes. Cold Spring Harbor Symposia On Quantitative Biology. 52: 421-8. PMID 2841069 DOI: 10.1101/Sqb.1987.052.01.049 |
0.393 |
|
1987 |
Ponder JW, Richards FM. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. Journal of Molecular Biology. 193: 775-91. PMID 2441069 DOI: 10.1016/0022-2836(87)90358-5 |
0.379 |
|
1987 |
Kundrot CE, Richards FM. Use of the occupancy factor in the refinement of solvent molecules in protein crystal structures Acta Crystallographica Section B. 43: 544-547. DOI: 10.1107/S0108768187097349 |
0.322 |
|
1985 |
Dumont ME, Trewhella J, Engelman DM, Richards FM. Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysis. The Journal of Membrane Biology. 88: 233-47. PMID 3913776 DOI: 10.1007/Bf01871088 |
0.341 |
|
1985 |
Warwicker J, Ollis D, Richards FM, Steitz TA. Electrostatic field of the large fragment of Escherichia coli DNA polymerase I. Journal of Molecular Biology. 186: 645-9. PMID 3912509 DOI: 10.1016/0022-2836(85)90136-6 |
0.498 |
|
1984 |
Richards FM. Comments on some present and future problems in protein structure Basic Life Sciences. 27: 1-24. PMID 6712561 DOI: 10.1007/978-1-4899-0375-4_1 |
0.346 |
|
1984 |
Shoham M, Levinson BL, Richards FM. Crystallization and preliminary X-ray diffraction studies of colicin E3 immunity protein. Journal of Molecular Biology. 177: 563-5. PMID 6471104 DOI: 10.1107/S0108767384098299 |
0.311 |
|
1982 |
Rosa JJ, Richards FM. Effects of binding of S-peptide and 2′-cytidine monophosphate on hydrogen exchange from the S-protein component of ribonuclease S. The amide protons of serine 123 and valine 124 Journal of Molecular Biology. 160: 517-530. PMID 6818352 DOI: 10.1016/0022-2836(82)90311-4 |
0.383 |
|
1982 |
Fox RO, Richards FM. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution. Nature. 300: 325-30. PMID 6292726 DOI: 10.1038/300325A0 |
0.544 |
|
1982 |
Eden D, Matthew JB, Rosa JJ, Richards FM. Increase in apparent compressibility of cytochrome c upon oxidation Proceedings of the National Academy of Sciences of the United States of America. 79: 815-819. PMID 6278497 DOI: 10.1073/Pnas.79.3.815 |
0.303 |
|
1982 |
Fox RO, Richards FM. The crystal structure of alamethicin Biophysical Journal. 37: 179A. |
0.467 |
|
1981 |
Rosa JJ, Richards FM. Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH, and the binding of S-peptide Journal of Molecular Biology. 145: 835-851. PMID 7265224 DOI: 10.1016/0022-2836(81)90318-1 |
0.41 |
|
1981 |
Lord ST, Richards FM. The labeling with 8-azido-cyclic adenosine monophosphate of proteins in vesicles of sarcoplasmic reticulum from rabbit skeletal muscle. Biochimica Et Biophysica Acta. 649: 13-23. PMID 6272856 DOI: 10.1016/0005-2736(81)90003-1 |
0.556 |
|
1979 |
Cohen FE, Richmond TJ, Richards FM. Protein folding: evaluation of some simple rules for the assembly of helices into tertiary structures with myoglobin as an example. Journal of Molecular Biology. 132: 275-88. PMID 533892 DOI: 10.1016/0022-2836(79)90260-2 |
0.651 |
|
1979 |
Rosa JJ, Richards FM. An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: Application to ribonuclease S peptide Journal of Molecular Biology. 133: 399-416. PMID 43900 DOI: 10.1016/0022-2836(79)90400-5 |
0.4 |
|
1979 |
Richards FM. Packing defects, cavities, volume fluctuations, and access to the interior of proteins. Including some general comments on surface area and protein structure Carlsberg Research Communications. 44: 47-63. DOI: 10.1007/Bf02906521 |
0.364 |
|
1978 |
Richmond TJ, Richards FM. Packing of alpha-helices: geometrical constraints and contact areas. Journal of Molecular Biology. 119: 537-55. PMID 642001 DOI: 10.1016/0022-2836(78)90201-2 |
0.658 |
|
1977 |
Richards FM, Richmond T. Solvents, interfaces and protein structure Ciba Foundation Symposium. 23-45. PMID 252454 DOI: 10.1002/9780470720424.ch2 |
0.618 |
|
1975 |
Staros JV, Richards FM. Photochemical labeling of the cytoplasmic surface of the membranes of intact human erythrocytes. The Journal of Biological Chemistry. 250: 8174-8. PMID 1176465 |
0.593 |
|
1974 |
Staros JV, Richards FM. Photochemical labeling of the surface proteins of human erythrocytes. Biochemistry. 13: 2720-6. PMID 4847541 DOI: 10.1021/Bi00710A010 |
0.633 |
|
1974 |
Staros JV, Haley BE, Richards FM. Human erythrocytes and resealed ghosts. A comparison of membrane topology. The Journal of Biological Chemistry. 249: 5004-7. PMID 4846757 |
0.568 |
|
1974 |
Richards FM. The interpretation of protein structures: Total volume, group volume distributions and packing density Journal of Molecular Biology. 82: 1-14. PMID 4818482 DOI: 10.1016/0022-2836(74)90570-1 |
0.358 |
|
1972 |
Richards FM, Wyckoff HW, Carlson WD, Allewell NM, Lee B, Mitsui Y. Protein structure, ribonuclease-S and nucleotide interactions. Cold Spring Harbor Symposia On Quantitative Biology. 36: 35-43. PMID 4508150 DOI: 10.1101/SQB.1972.036.01.008 |
0.718 |
|
1971 |
Lee B, Richards FM. The interpretation of protein structures: Estimation of static accessibility Journal of Molecular Biology. 55: 379-380,IN3,381-398,. PMID 5551392 DOI: 10.1016/0022-2836(71)90324-X |
0.348 |
|
1971 |
Richards FM, Wyckoff HW. 24 Bovine Pancreatic Ribonuclease Enzymes. 4: 647-656,656A,656B,65. DOI: 10.1016/S1874-6047(08)60384-4 |
0.699 |
|
1970 |
Wyckoff HW, Tsernoglou D, Hanson AW, Knox JR, Lee B, Richards FM. The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A. The Journal of Biological Chemistry. 245: 305-28. PMID 5460889 |
0.677 |
|
1968 |
Richards FM, Knowles JR. Glutaraldehyde as a protein cross-linking reagent Journal of Molecular Biology. 37: 231-233. PMID 5760492 DOI: 10.1016/0022-2836(68)90086-7 |
0.53 |
|
1968 |
Bishop WH, Richards FM. Isoelectric point of a protein in the crosslinked crystalline state: β-Lactoglobulin Journal of Molecular Biology. 33: 415-421. PMID 5700702 DOI: 10.1016/0022-2836(68)90198-8 |
0.317 |
|
1968 |
Perham RN, Richards FM. Reactivity and structural role of protein amino groups in tobacco mosaic virus. Journal of Molecular Biology. 33: 795-807. PMID 5700423 DOI: 10.1016/0022-2836(68)90320-3 |
0.345 |
|
1967 |
Wyckoff HW, Doscher M, Tsernoglou D, Inagami T, Johnson LN, Hardman KD, Allewell NM, Kelly DM, Richards FM. Design of a diffractometer and flow cell system for X-ray analysis of crystalline proteins with applications to the crystal chemistry of ribonuclease-S. Journal of Molecular Biology. 27: 563-78. PMID 6049685 DOI: 10.1016/0022-2836(67)90059-9 |
0.743 |
|
1967 |
Wyckoff HW, Hardman KD, Allewell NM, Inagami T, Tsernoglou D, Johnson LN, Richards FM. The structure of ribonuclease-S at 6 A resolution. The Journal of Biological Chemistry. 242: 3749-53. PMID 6038503 |
0.739 |
|
1967 |
Wyckoff HW, Hardman KD, Allewell NM, Inagami T, Johnson LN, Richards FM. The structure of ribonuclease-S at 3.5 A resolution. The Journal of Biological Chemistry. 242: 3984-8. PMID 6037556 |
0.739 |
|
1967 |
Quiocho FA, Bishop WH, Richards FM. Effects Of Changes In Some Solvent Parameters On Carboxypeptidase A In Solution And In Cross-Linked Crystals Proceedings of the National Academy of Sciences of the United States of America. 57: 525-537. DOI: 10.1073/Pnas.57.3.525 |
0.455 |
|
1966 |
Bishop WH, Quiocho FA, Richards FM. The Removal and Exchange of Metal Ions in Cross-Linked Crystals of Carboxypeptidase-A* Biochemistry. 5: 4077-4087. DOI: 10.1021/Bi00876A042 |
0.735 |
|
1966 |
Quiocho FA, Richards FM. The Enzymic Behavior of Carboxypeptidase-A in the Solid State* Biochemistry. 5: 4062-4076. DOI: 10.1021/Bi00876A041 |
0.557 |
|
1964 |
QUIOCHO FA, RICHARDS FM. INTERMOLECULAR CROSS LINKING OF A PROTEIN IN THE CRYSTALLINE STATE: CARBOXYPEPTIDASE-A. Proceedings of the National Academy of Sciences of the United States of America. 52: 833-9. PMID 14212562 DOI: 10.1073/Pnas.52.3.833 |
0.448 |
|
1962 |
ALLENDE JE, RICHARDS FM. The action of trypsin on ribonuclease-S. Biochemistry. 1: 295-304. PMID 13860586 DOI: 10.1021/Bi00908A017 |
0.551 |
|
1952 |
LOW BW, RICHARDS FM. Determination of protein crystal densities. Nature. 170: 412-3. PMID 12993180 DOI: 10.1038/170412B0 |
0.65 |
|
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