| Year |
Citation |
Score |
| 2016 |
Doolittle RF. [18] Terminal pyrrolidonecarboxylic acid: Cleavage with enzymes. Methods in Enzymology. 25: 231-44. PMID 23014405 DOI: 10.1016/S0076-6879(72)25020-0 |
0.342 |
|
| 2015 |
Doolittle RF. Bioinformatic Characterization of Genes and Proteins Involved in Blood Clotting in Lampreys. Journal of Molecular Evolution. 81: 121-30. PMID 26437661 DOI: 10.1007/S00239-015-9701-0 |
0.341 |
|
| 2014 |
Doolittle RF. Clotting of mammalian fibrinogens by papain: a re-examination. Biochemistry. 53: 6687-94. PMID 25283163 DOI: 10.1021/Bi5010987 |
0.331 |
|
| 2012 |
Doolittle RF, McNamara K, Lin K. Correlating structure and function during the evolution of fibrinogen-related domains. Protein Science : a Publication of the Protein Society. 21: 1808-23. PMID 23076991 DOI: 10.1002/Pro.2177 |
0.349 |
|
| 2012 |
Doolittle RF. The protochordate Ciona intestinalis has a protein like full-length vertebrate fibrinogen. Journal of Innate Immunity. 4: 219-22. PMID 21860218 DOI: 10.1159/000329823 |
0.358 |
|
| 2011 |
Watson JW, Doolittle RF. Peptide-derivatized albumins that inhibit fibrin polymerization. Biochemistry. 50: 9923-7. PMID 22010909 DOI: 10.1021/Bi201406C |
0.331 |
|
| 2010 |
Doolittle RF. The roots of bioinformatics in protein evolution. Plos Computational Biology. 6: e1000875. PMID 20686682 DOI: 10.1371/Journal.Pcbi.1000875 |
0.419 |
|
| 2009 |
Doolittle RF. Step-by-step evolution of vertebrate blood coagulation. Cold Spring Harbor Symposia On Quantitative Biology. 74: 35-40. PMID 19667012 DOI: 10.1101/Sqb.2009.74.001 |
0.319 |
|
| 2009 |
Pandi L, Kollman JM, Lopez-Lira F, Burrows JM, Riley M, Doolittle RF. Two families of synthetic peptides that enhance fibrin turbidity and delay fibrinolysis by different mechanisms. Biochemistry. 48: 7201-8. PMID 19588915 DOI: 10.1021/Bi900647G |
0.631 |
|
| 2009 |
Kollman JM, Pandi L, Sawaya MR, Riley M, Doolittle RF. Crystal structure of human fibrinogen. Biochemistry. 48: 3877-86. PMID 19296670 DOI: 10.1021/Bi802205G |
0.668 |
|
| 2008 |
Doolittle RF. Searching for differences between fibrinogen and fibrin that affect the initiation of fibrinolysis. Cardiovascular & Hematological Agents in Medicinal Chemistry. 6: 181-9. PMID 18673232 DOI: 10.2174/187152508784871954 |
0.341 |
|
| 2008 |
Doolittle RF, Jiang Y, Nand J. Genomic evidence for a simpler clotting scheme in jawless vertebrates. Journal of Molecular Evolution. 66: 185-96. PMID 18283387 DOI: 10.1007/S00239-008-9074-8 |
0.345 |
|
| 2007 |
Doolittle RF, Pandi L. Probing the beta-chain hole of fibrinogen with synthetic peptides that differ at their amino termini. Biochemistry. 46: 10033-8. PMID 17688324 DOI: 10.1021/Bi7010916 |
0.399 |
|
| 2006 |
Doolittle RF, Chen A, Pandi L. Differences in binding specificity for the homologous gamma- and beta-chain "holes" on fibrinogen: exclusive binding of Ala-His-Arg-Pro-amide by the beta-chain hole. Biochemistry. 45: 13962-9. PMID 17115691 DOI: 10.1021/Bi061219E |
0.395 |
|
| 2006 |
Doolittle RF, Pandi L. Binding of synthetic B knobs to fibrinogen changes the character of fibrin and inhibits its ability to activate tissue plasminogen activator and its destruction by plasmin. Biochemistry. 45: 2657-67. PMID 16489759 DOI: 10.1021/Bi0524767 |
0.337 |
|
| 2006 |
Doolittle RF, Kollman JM. Natively unfolded regions of the vertebrate fibrinogen molecule. Proteins. 63: 391-7. PMID 16288455 DOI: 10.1002/Prot.20758 |
0.628 |
|
| 2005 |
Doolittle RF. Evolutionary aspects of whole-genome biology. Current Opinion in Structural Biology. 15: 248-53. PMID 15963888 DOI: 10.1016/J.Sbi.2005.04.001 |
0.303 |
|
| 2005 |
Kollman JM, Doolittle RF. Unusual non-crystallographic symmetry in crystals of a 420 kDa crustacean clottable protein. Acta Crystallographica. Section D, Biological Crystallography. 61: 485-9. PMID 15805605 DOI: 10.1107/S0907444905000910 |
0.6 |
|
| 2005 |
Sirinupong N, Suwanmanee P, Doolittle RF, Suvachitanont W. Molecular cloning of a new cDNA and expression of 3-hydroxy-3-methylglutaryl-CoA synthase gene from Hevea brasiliensis. Planta. 221: 502-12. PMID 15744497 DOI: 10.1007/S00425-004-1463-7 |
0.399 |
|
| 2005 |
Yang S, Doolittle RF, Bourne PE. Phylogeny determined by protein domain content. Proceedings of the National Academy of Sciences of the United States of America. 102: 373-8. PMID 15630082 DOI: 10.1073/Pnas.0408810102 |
0.309 |
|
| 2003 |
Doolittle RF. X-ray crystallographic studies on fibrinogen and fibrin. Journal of Thrombosis and Haemostasis : Jth. 1: 1559-65. PMID 12871291 DOI: 10.1046/J.1538-7836.2003.00278.X |
0.335 |
|
| 2003 |
Doolittle RF. Structural basis of the fibrinogen-fibrin transformation: contributions from X-ray crystallography. Blood Reviews. 17: 33-41. PMID 12490209 DOI: 10.1016/S0268-960X(02)00060-7 |
0.307 |
|
| 2002 |
Yang Z, Pandi L, Doolittle RF. The crystal structure of fragment double-D from cross-linked lamprey fibrin reveals isopeptide linkages across an unexpected D-D interface. Biochemistry. 41: 15610-7. PMID 12501189 DOI: 10.1021/Bi026666I |
0.306 |
|
| 2002 |
Yang Z, Spraggon G, Pandi L, Everse SJ, Riley M, Doolittle RF. Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide. Biochemistry. 41: 10218-24. PMID 12162736 DOI: 10.1021/Bi020299T |
0.381 |
|
| 2002 |
Doolittle RF, York AL. Bacterial actins? An evolutionary perspective. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 24: 293-6. PMID 11948613 DOI: 10.1002/Bies.10079 |
0.312 |
|
| 2001 |
Yang Z, Kollman JM, Pandi L, Doolittle RF. Crystal structure of native chicken fibrinogen at 2.7 A resolution. Biochemistry. 40: 12515-23. PMID 11601975 DOI: 10.1021/Bi011394P |
0.656 |
|
| 2001 |
Doolittle RF, Yang Z, Mochalkin I. Crystal structure studies on fibrinogen and fibrin. Annals of the New York Academy of Sciences. 936: 31-43. PMID 11460486 DOI: 10.1111/J.1749-6632.2001.Tb03492.X |
0.362 |
|
| 2000 |
Yang Z, Mochalkin I, Doolittle RF. A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides. Proceedings of the National Academy of Sciences of the United States of America. 97: 14156-61. PMID 11121023 DOI: 10.1073/Pnas.97.26.14156 |
0.347 |
|
| 2000 |
Kollman JM, Doolittle RF. Determining the relative rates of change for prokaryotic and eukaryotic proteins with anciently duplicated paralogs. Journal of Molecular Evolution. 51: 173-81. PMID 10948274 DOI: 10.1007/S002390010078 |
0.615 |
|
| 2000 |
Doolittle RF. On the trail of protein sequences. Bioinformatics (Oxford, England). 16: 24-33. PMID 10812474 DOI: 10.1093/Bioinformatics/16.1.24 |
0.351 |
|
| 2000 |
Yang Z, Mochalkin I, Veerapandian L, Riley M, Doolittle RF. Crystal structure of native chicken fibrinogen at 5.5-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 97: 3907-12. PMID 10737772 DOI: 10.1073/Pnas.080065697 |
0.341 |
|
| 2000 |
Lin YC, Doolittle RF. A latent inhibitor of fibrin polymerization with ancillary anticoagulant activity. Thrombosis Research. 97: 375-8. PMID 10709915 DOI: 10.1016/S0049-3848(99)00170-X |
0.345 |
|
| 1999 |
Doolittle RF, Feng DF, Cho G. Determining divergence times with protein clocks. The Biological Bulletin. 196: 356-7; discussion 35. PMID 11536911 DOI: 10.2307/1542969 |
0.37 |
|
| 1999 |
Handy J, Doolittle RF. An attempt to pinpoint the phylogenetic introduction of glutaminyl-tRNA synthetase among bacteria. Journal of Molecular Evolution. 49: 709-15. PMID 10594171 DOI: 10.1007/Pl00006592 |
0.339 |
|
| 1999 |
Doolittle RF. Do you dig my groove? Nature Genetics. 23: 6-8. PMID 10471485 DOI: 10.1038/12597 |
0.349 |
|
| 1999 |
Everse SJ, Spraggon G, Veerapandian L, Doolittle RF. Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry. 38: 2941-6. PMID 10074346 DOI: 10.1021/Bi982626W |
0.34 |
|
| 1998 |
Doolittle RF, Spraggon G, Everse SJ. Three-dimensional structural studies on fragments of fibrinogen and fibrin. Current Opinion in Structural Biology. 8: 792-8. PMID 9914253 DOI: 10.1016/S0959-440X(98)80100-0 |
0.33 |
|
| 1998 |
Spraggon G, Applegate D, Everse SJ, Zhang JZ, Veerapandian L, Redman C, Doolittle RF, Grieninger G. Crystal structure of a recombinant alphaEC domain from human fibrinogen-420. Proceedings of the National Academy of Sciences of the United States of America. 95: 9099-104. PMID 9689040 DOI: 10.1073/Pnas.95.16.9099 |
0.374 |
|
| 1998 |
Everse SJ, Spraggon G, Doolittle RF. A three-dimensional consideration of variant human fibrinogens. Thrombosis and Haemostasis. 80: 1-9. PMID 9684777 DOI: 10.1055/S-0037-1615130 |
0.358 |
|
| 1998 |
Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF. Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry. 37: 8637-42. PMID 9628725 DOI: 10.1021/Bi9804129 |
0.362 |
|
| 1997 |
Feng DF, Cho G, Doolittle RF. Determining divergence times with a protein clock: update and reevaluation. Proceedings of the National Academy of Sciences of the United States of America. 94: 13028-33. PMID 9371794 DOI: 10.1073/Pnas.94.24.13028 |
0.402 |
|
| 1997 |
Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature. 389: 455-62. PMID 9333233 DOI: 10.1038/38947 |
0.354 |
|
| 1997 |
Doolittle RF. A bug with excess gastric avidity. Nature. 388: 515-6. PMID 9252182 DOI: 10.1038/41418 |
0.306 |
|
| 1997 |
Feng DF, Doolittle RF. Converting amino acid alignment scores into measures of evolutionary time: a simulation study of various relationships. Journal of Molecular Evolution. 44: 361-70. PMID 9089075 DOI: 10.1007/Pl00006155 |
0.342 |
|
| 1996 |
DOOLITTLE RF. CHARACTERIZATION OF LAMPREY FIBRINOPEPTIDES. The Biochemical Journal. 94: 742-50. PMID 14340066 DOI: 10.1042/Bj0940742 |
0.379 |
|
| 1996 |
DOOLITTLE RF. DIFFERENCES IN THE CLOTTING OF LAMPREY FIBRINOGEN BY LAMPREY AND BOVINE THROMBINS. The Biochemical Journal. 94: 735-41. PMID 14340065 DOI: 10.1042/Bj0940735 |
0.319 |
|
| 1996 |
Roger AJ, Smith MW, Doolittle RF, Doolittle WF. Evidence for the Heterolobosea from phylogenetic analysis of genes encoding glyceraldehyde-3-phosphate dehydrogenase. The Journal of Eukaryotic Microbiology. 43: 475-85. PMID 8976605 DOI: 10.1111/J.1550-7408.1996.Tb04507.X |
0.319 |
|
| 1996 |
Doolittle RF, Everse SJ, Spraggon G. Human fibrinogen: anticipating a 3-dimensional structure. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 1464-70. PMID 8940292 DOI: 10.1096/Fasebj.10.13.8940292 |
0.321 |
|
| 1996 |
Feng DF, Doolittle RF. Progressive alignment of amino acid sequences and construction of phylogenetic trees from them. Methods in Enzymology. 266: 368-82. PMID 8743694 DOI: 10.1016/S0076-6879(96)66023-6 |
0.359 |
|
| 1996 |
Doolittle RF, Feng DF, Tsang S, Cho G, Little E. Determining divergence times of the major kingdoms of living organisms with a protein clock. Science (New York, N.Y.). 271: 470-7. PMID 8560259 DOI: 10.1126/Science.271.5248.470 |
0.345 |
|
| 1995 |
Doolittle RF. The origins and evolution of eukaryotic proteins. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 349: 235-40. PMID 8577833 DOI: 10.1098/Rstb.1995.0107 |
0.329 |
|
| 1995 |
Shipwash E, Pan Y, Doolittle RF. The minor form alpha' chain from lamprey fibrinogen is rapidly crosslinked during clotting. Proceedings of the National Academy of Sciences of the United States of America. 92: 968-72. PMID 7862675 DOI: 10.1073/Pnas.92.4.968 |
0.363 |
|
| 1995 |
Nagel GM, Doolittle RF. Phylogenetic analysis of the aminoacyl-tRNA synthetases. Journal of Molecular Evolution. 40: 487-98. PMID 7783224 DOI: 10.1007/Bf00166617 |
0.376 |
|
| 1995 |
Doolittle RF. Of archae and eo: what's in a name? Proceedings of the National Academy of Sciences of the United States of America. 92: 2421-3. PMID 7708656 DOI: 10.1073/Pnas.92.7.2421 |
0.329 |
|
| 1995 |
Doolittle RF. The multiplicity of domains in proteins. Annual Review of Biochemistry. 64: 287-314. PMID 7574483 DOI: 10.1146/Annurev.Bi.64.070195.001443 |
0.314 |
|
| 1994 |
Bork P, Doolittle RF. Drosophila kelch motif is derived from a common enzyme fold. Journal of Molecular Biology. 236: 1277-82. PMID 8126718 DOI: 10.1016/0022-2836(94)90056-6 |
0.352 |
|
| 1994 |
Doolittle RF. Protein sequence comparisons: searching databases and aligning sequences. Current Opinion in Biotechnology. 5: 24-8. PMID 7764639 DOI: 10.1016/S0958-1669(05)80065-5 |
0.322 |
|
| 1994 |
Little E, Bork P, Doolittle RF. Tracing the spread of fibronectin type III domains in bacterial glycohydrolases. Journal of Molecular Evolution. 39: 631-43. PMID 7528812 DOI: 10.1007/Bf00160409 |
0.352 |
|
| 1993 |
Narumi H, Hishida T, Sasaki T, Feng DF, Doolittle RF. Molecular cloning of silkworm (Bombyx mori) antichymotrypsin. A new member of the serpin superfamily of proteins from insects. European Journal of Biochemistry / Febs. 214: 181-7. PMID 8508791 DOI: 10.1111/J.1432-1033.1993.Tb17911.X |
0.435 |
|
| 1993 |
Doolittle RF, Blundell TL. Sequences and topology. Unity and diversity all over again Current Opinion in Structural Biology. 3: 377-378. DOI: 10.1016/S0959-440X(05)80109-5 |
0.353 |
|
| 1992 |
Yamazumi K, Doolittle RF. Photoaffinity labeling of the primary fibrin polymerization site: localization of the label to gamma-chain Tyr-363. Proceedings of the National Academy of Sciences of the United States of America. 89: 2893-6. PMID 1557396 DOI: 10.1073/Pnas.89.7.2893 |
0.354 |
|
| 1992 |
Shimizu A, Nagel GM, Doolittle RF. Photoaffinity labeling of the primary fibrin polymerization site: isolation and characterization of a labeled cyanogen bromide fragment corresponding to gamma-chain residues 337-379. Proceedings of the National Academy of Sciences of the United States of America. 89: 2888-92. PMID 1557395 DOI: 10.1073/Pnas.89.7.2888 |
0.365 |
|
| 1992 |
Pan Y, Doolittle RF. cDNA sequence of a second fibrinogen alpha chain in lamprey: an archetypal version alignable with full-length beta and gamma chains. Proceedings of the National Academy of Sciences of the United States of America. 89: 2066-70. PMID 1549566 DOI: 10.1073/Pnas.89.6.2066 |
0.367 |
|
| 1992 |
Bork P, Doolittle RF. Proposed acquisition of an animal protein domain by bacteria. Proceedings of the National Academy of Sciences of the United States of America. 89: 8990-4. PMID 1409594 DOI: 10.1073/Pnas.89.19.8990 |
0.327 |
|
| 1992 |
Doolittle RF, Feng DF. Tracing the origin of retroviruses. Current Topics in Microbiology and Immunology. 176: 195-211. PMID 1376225 DOI: 10.1007/978-3-642-77011-1_13 |
0.355 |
|
| 1992 |
Doolittle RF. Stein and Moore Award address. Reconstructing history with amino acid sequences. Protein Science : a Publication of the Protein Society. 1: 191-200. PMID 1339026 DOI: 10.1002/Pro.5560010201 |
0.37 |
|
| 1992 |
Gray JE, Doolittle RF. Characterization, primary structure, and evolution of lamprey plasma albumin. Protein Science : a Publication of the Protein Society. 1: 289-302. PMID 1304910 DOI: 10.1002/Pro.5560010211 |
0.42 |
|
| 1992 |
Doolittle RF. A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives. Protein Science : a Publication of the Protein Society. 1: 1563-77. PMID 1304888 DOI: 10.1002/Pro.5560011204 |
0.432 |
|
| 1992 |
Doolittle RF. Amino acid sequence comparison as an aid to determining evolutionary origins Journal of Protein Chemistry. 11: 422. DOI: 10.1007/978-1-4899-1603-7_31 |
0.383 |
|
| 1991 |
Doolittle RF. The structure and evolution of vertebrate fibrinogen: A comparison of the lamprey and mammalian proteins Advances in Experimental Medicine and Biology. 281: 25-37. PMID 2102616 DOI: 10.1007/978-1-4615-3806-6_2 |
0.432 |
|
| 1991 |
Nagel GM, Doolittle RF. Evolution and relatedness in two aminoacyl-tRNA synthetase families. Proceedings of the National Academy of Sciences of the United States of America. 88: 8121-5. PMID 1896459 DOI: 10.1073/Pnas.88.18.8121 |
0.371 |
|
| 1991 |
Blundell TL, Doolittle RF. Sequences and topology Editorial overview Current Opinion in Structural Biology. 1: 319-320. DOI: 10.1016/0959-440X(91)90028-R |
0.35 |
|
| 1990 |
Xu X, Doolittle RF. Presence of a vertebrate fibrinogen-like sequence in an echinoderm Proceedings of the National Academy of Sciences of the United States of America. 87: 2097-2101. PMID 2315305 DOI: 10.1073/Pnas.87.6.2097 |
0.412 |
|
| 1990 |
Doolittle RF. Searching through sequence databases Methods in Enzymology. 183: 99-110. PMID 2314299 DOI: 10.1016/0076-6879(90)83008-W |
0.407 |
|
| 1990 |
Doolittle RF, Feng DF. Nearest neighbor procedure for relating progressively aligned amino acid sequences Methods in Enzymology. 183: 659-669. PMID 2314298 DOI: 10.1016/0076-6879(90)83043-9 |
0.329 |
|
| 1990 |
Feng DF, Doolittle RF. [23] Progressive alignment and phylogenetic tree construction of protein sequences Methods in Enzymology. 183: 375-387. PMID 2314283 DOI: 10.1016/0076-6879(90)83025-5 |
0.343 |
|
| 1990 |
Doolittle RF, Riley M. The amino-terminal sequence of lobster fibrinogen reveals common ancestry with vitellogenins Biochemical and Biophysical Research Communications. 167: 16-19. PMID 2310387 DOI: 10.1016/0006-291X(90)91723-6 |
0.417 |
|
| 1990 |
Doolittle RF, Feng DF, McClure MA, Johnson MS. Retrovirus phylogeny and evolution Current Topics in Microbiology and Immunology. 157: 1-18. PMID 2203607 DOI: 10.1007/978-3-642-75218-6_1 |
0.312 |
|
| 1990 |
Seely O, Feng DF, Smith DW, Sulzbach D, Doolittle RF. Construction of a facsimile data set for large genome sequence analysis. Genomics. 8: 71-82. PMID 2081603 DOI: 10.1016/0888-7543(90)90227-L |
0.346 |
|
| 1989 |
Doolittle RF. Similar amino acid sequences revisited Trends in Biochemical Sciences. 14: 244-245. PMID 2773041 DOI: 10.1016/0968-0004(89)90055-8 |
0.412 |
|
| 1989 |
Wang YZ, Patterson J, Gray JE, Yu C, Cottrell BA, Shimizu A, Graham D, Riley M, Doolittle RF. Complete sequence of the lamprey fibrinogen α chain Biochemistry. 28: 9801-9806. PMID 2611265 DOI: 10.1021/Bi00451A039 |
0.43 |
|
| 1989 |
Doolittle RF, Feng DF, Johnson MS, McClure MA. Origins and evolutionary relationships of retroviruses Quarterly Review of Biology. 64: 1-30. PMID 2469098 DOI: 10.1086/416128 |
0.375 |
|
| 1988 |
McClure MA, Johnson MS, Feng DF, Doolittle RF. Sequence comparisons of retroviral proteins: relative rates of change and general phylogeny Proceedings of the National Academy of Sciences of the United States of America. 85: 2469-2473. PMID 2451824 DOI: 10.1073/Pnas.85.8.2469 |
0.403 |
|
| 1987 |
Reeck GR, de Haën C, Teller DC, Doolittle RF, Fitch WM, Dickerson RE, Chambon P, McLachlan AD, Margoliash E, Jukes TH. "Homology" in proteins and nucleic acids: a terminology muddle and a way out of it. Cell. 50: 667. PMID 3621342 DOI: 10.1016/0092-8674(87)90322-9 |
0.324 |
|
| 1987 |
Pontes M, Xu X, Graham D, Riley M, Doolittle RF. cDNA sequences of two apolipoproteins from lamprey Biochemistry. 26: 1611-1617. PMID 3593681 |
0.321 |
|
| 1987 |
Vogt PK, Bos TJ, Doolittle RF. Homology between the DNA-binding domain of the GCN4 regulatory protein of yeast and the carboxyl-terminal region of a protein coded for by the oncogene jun Proceedings of the National Academy of Sciences of the United States of America. 84: 3316-3319. PMID 3554236 DOI: 10.1073/Pnas.84.10.3316 |
0.391 |
|
| 1987 |
Doolittle RF, Feng DF. Reconstructing the evolution of vertebrate blood coagulation from a consideration of the amino acid sequences of clotting proteins Cold Spring Harbor Symposia On Quantitative Biology. 52: 869-874. PMID 3483343 DOI: 10.1101/Sqb.1987.052.01.095 |
0.386 |
|
| 1987 |
Feng DF, Doolittle RF. Progressive sequence alignment as a prerequisitetto correct phylogenetic trees Journal of Molecular Evolution. 25: 351-360. PMID 3118049 DOI: 10.1007/Bf02603120 |
0.349 |
|
| 1987 |
McClure MA, Johnson MS, Doolittle RF. Relocation of a protease-like gene segment between two retroviruses Proceedings of the National Academy of Sciences of the United States of America. 84: 2693-2697. PMID 3106974 DOI: 10.1073/Pnas.84.9.2693 |
0.33 |
|
| 1987 |
DOOLITTLE RF. THE EVOLUTION OF THE VERTEBRATE PLASMA PROTEINS The Biological Bulletin. 172: 269-283. DOI: 10.2307/1541707 |
0.342 |
|
| 1986 |
Bohonus VL, Doolittle RF, Pontes M, Strong DD. Complementary DNA sequence of lamprey fibrinogen β chain Biochemistry. 25: 6512-6516. PMID 3790537 DOI: 10.1021/Bi00369A026 |
0.419 |
|
| 1986 |
Doolittle RF, Johnson MS, Husain I, Van Houten B, Thomas DC, Sancar A. Domainal evolution of a prokaryotic DNA repair protein and its relationship to active-transport proteins Nature. 323: 451-453. PMID 3762695 DOI: 10.1038/323451A0 |
0.311 |
|
| 1986 |
Doolittle RF, Feng DF, Johnson MS, McClure MA. Relationships of human protein sequences to those of other organisms Cold Spring Harbor Symposia On Quantitative Biology. 51: 447-455. PMID 3472734 DOI: 10.1101/Sqb.1986.051.01.054 |
0.334 |
|
| 1986 |
Mariottini P, Chomyn A, Riley M, Cottrell B, Doolittle RF, Attardi G. Identification of the polypeptides encoded in the unassigned reading frames 2, 4, 4L, and 5 of human mitochondrial DNA. Proceedings of the National Academy of Sciences of the United States of America. 83: 1563-7. PMID 3456601 DOI: 10.1073/Pnas.83.6.1563 |
0.313 |
|
| 1986 |
Johnson MS, Doolittle RF. A method for the simultaneous alignment of three or more amino acid sequences Journal of Molecular Evolution. 23: 267-278. PMID 3100815 DOI: 10.1007/Bf02115583 |
0.375 |
|
| 1986 |
Fong HKW, Hurley JB, Hopkins RS, Miake-Lye R, Johnson MS, Doolittle RF, Simon MI. Repetitive segmental structure of the transducin β subunit: Homology with the CDC4 gene and identification of related mRNAs Proceedings of the National Academy of Sciences of the United States of America. 83: 2162-2166. PMID 3083416 DOI: 10.1073/Pnas.83.7.2162 |
0.328 |
|
| 1986 |
Johnson MS, McClure MA, Feng DF, Gray J, Doolittle RF. Computer analysis of retroviral pol genes: Assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes Proceedings of the National Academy of Sciences of the United States of America. 83: 7648-7652. PMID 2429313 DOI: 10.1073/Pnas.83.20.7648 |
0.398 |
|
| 1985 |
Feng DF, Johnson MS, Doolittle RF. Aligning amino acid sequences: Comparison of commonly used methods Journal of Molecular Evolution. 21: 112-125. PMID 6100188 DOI: 10.1007/Bf02100085 |
0.38 |
|
| 1985 |
Doolittle RF. More homologies among the vertebrate plasma proteins Bioscience Reports. 5: 877-884. PMID 3938299 DOI: 10.1007/Bf01119899 |
0.312 |
|
| 1985 |
Strong DD, Moore M, Cottrell BA, Bohonus VL, Pontes M, Evans B, Riley M, Doolittle RF. Lamprey fibrinogen γ chain: Cloning, cDNA sequencing, and general characterization Biochemistry. 24: 92-101. PMID 2581603 DOI: 10.1021/Bi00322A014 |
0.449 |
|
| 1985 |
Jue RA, Doolittle RF. Determination of the relative positions of amino acids by partial specific cleavages of end-labeled proteins Biochemistry. 24: 162-170. DOI: 10.1021/Bi00322A023 |
0.374 |
|
| 1984 |
Doolittle RF, Feng DF, Johnson MS. Computer-based characterization of epidermal growth factor precursor Nature. 307: 558-560. PMID 6607417 DOI: 10.1038/307558A0 |
0.325 |
|
| 1984 |
Peterson TA, Yochem J, Byers B, Nunn MF, Duesberg PH, Doolittle RF, Reed SI. A relationship between the yeast cell cycle genes CDC4 and CDC36 and the ets sequence of oncogenic virus E26. Nature. 309: 556-8. PMID 6374468 DOI: 10.1038/309556A0 |
0.324 |
|
| 1984 |
Horwich AL, Fenton WA, Williams KR, Kalousek F, Kraus JP, Doolittle RF, Konigsberg W, Rosenberg LE. Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase. Science (New York, N.Y.). 224: 1068-74. PMID 6372096 DOI: 10.1126/Science.6372096 |
0.409 |
|
| 1983 |
Hoeprich PD, Doolittle RF. Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation Biochemistry. 22: 2049-2055. PMID 6860649 DOI: 10.1021/Bi00278A003 |
0.359 |
|
| 1983 |
Doolittle RF. Angiotensinogen is related to the antitrypsin-antithrombin-ovalbumin family Science. 222: 417-419. PMID 6604942 DOI: 10.1126/Science.6604942 |
0.372 |
|
| 1983 |
Mariottini P, Chomyn A, Attardi G, Trovato D, Strong DD, Doolittle RF. Antibodies against synthetic peptides reveal that the unidentified reading frame A6L, overlapping the ATPase 6 gene, is expressed in human mitochondria. Cell. 32: 1269-77. PMID 6301689 DOI: 10.1016/0092-8674(83)90308-2 |
0.326 |
|
| 1983 |
Chomyn A, Mariottini P, Gonzalez-Cadavid N, Attardi G, Strong DD, Trovato D, Riley M, Doolittle RF. Identification of the polypeptides encoded in the ATPase 6 gene and in the unassigned reading frames 1 and 3 of human mtDNA. Proceedings of the National Academy of Sciences of the United States of America. 80: 5535-9. PMID 6225122 DOI: 10.1073/Pnas.80.18.5535 |
0.323 |
|
| 1983 |
Hawiger J, Kloczewiak M, Timmons S, Strong D, Doolittle RF. Interaction of fibrinogen with staphylococcal clumping factor and with platelets. Annals of the New York Academy of Sciences. 408: 521-35. PMID 6223560 DOI: 10.1111/J.1749-6632.1983.Tb23270.X |
0.348 |
|
| 1983 |
Walter G, Doolittle RF. Antibodies Against Synthetic Peptides Genetic Engineering. 5: 61-91. DOI: 10.1007/978-1-4684-4556-5_5 |
0.377 |
|
| 1982 |
Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein Journal of Molecular Biology. 157: 105-132. PMID 7108955 DOI: 10.1016/0022-2836(82)90515-0 |
0.394 |
|
| 1982 |
Brown JP, Hewick RM, Hellström I, Hellström KE, Doolittle RF, Dreyer WJ. Human melanoma-associated antigen p97 is structurally and functionally related to transferrin. Nature. 296: 171-3. PMID 7063021 DOI: 10.1038/296171A0 |
0.374 |
|
| 1982 |
Sauer RT, Yocum RR, Doolittle RF, Lewis M, Pabo CO. Homology among DNA-binding proteins suggests use of a conserved super-secondary structure. Nature. 298: 447-51. PMID 6896364 DOI: 10.1038/298447A0 |
0.347 |
|
| 1982 |
Hawiger J, Timmons S, Kloczewiak M, Strong DD, Doolittle RF. γ and α chains of human fibrinogen possess sites reactive with human platelet receptors Proceedings of the National Academy of Sciences of the United States of America. 79: 2068-2071. PMID 6281794 DOI: 10.1073/Pnas.79.6.2068 |
0.323 |
|
| 1981 |
Doolittle RF. Similar amino acid sequences: Chance or common ancestry? Science. 214: 149-159. PMID 7280687 DOI: 10.1126/Science.7280687 |
0.411 |
|
| 1981 |
Laudano AP, Doolittle RF. Influence of calcium ion on the binding of fibrin amino terminal peptides to fibrinogen Science. 212: 457-459. PMID 7209542 DOI: 10.1126/Science.7209542 |
0.348 |
|
| 1981 |
Price TM, Strong DD, Rudee ML, Doolittle RF. Shadow-cast electron microscopy of fibrinogen with antibody fragments bound to specific regions. Proceedings of the National Academy of Sciences of the United States of America. 78: 200-4. PMID 6941244 DOI: 10.1073/Pnas.78.1.200 |
0.324 |
|
| 1981 |
Olexa SA, Budzynski AZ, Doolittle RF, Cottrell BA, Greene TC. Structure of fragment E species from human cross-linked fibrin. Biochemistry. 20: 6139-45. PMID 6458323 DOI: 10.1021/Bi00524A035 |
0.325 |
|
| 1981 |
Van Beveren C, Galleshaw JA, Jonas V, Berns AJ, Doolittle RF, Donoghue DJ, Verma IM. Nucleotide sequence and formation of the transforming gene of a mouse sarcoma virus. Nature. 289: 258-62. PMID 6256659 DOI: 10.1038/289258A0 |
0.355 |
|
| 1980 |
Jue RA, Woodbury NW, Doolittle RF. Sequence homologies among E. coli ribosomal proteins: Evidence for evolutionarily related groupings and internal duplications Journal of Molecular Evolution. 15: 129-148. PMID 6995620 DOI: 10.1007/Bf01732666 |
0.365 |
|
| 1980 |
Walter G, Scheidtmann KH, Carbone A, Laudano AP, Doolittle RF. Antibodies specific for the carboxy- and amino-terminal regions of simian virus 40 large tumor antigen Proceedings of the National Academy of Sciences of the United States of America. 77: 5197-5200. PMID 6254066 DOI: 10.1073/Pnas.77.9.5197 |
0.334 |
|
| 1979 |
Watt KWK, Cottrell BA, Strong DD, Doolittle RF. Amino acid sequence studies on the α chain of human fibrinogen. Overlapping sequences providing the complete sequence Biochemistry. 18: 5410-5416. PMID 518846 DOI: 10.1021/Bi00591A024 |
0.44 |
|
| 1979 |
Cottrell BA, Strong DD, Watt KWK, Doolittle RF. Amino acid sequence studies on the α chain of human fibrinogen. exact location of cross-linking acceptor sites Biochemistry. 18: 5405-5410. PMID 518845 DOI: 10.1021/Bi00591A023 |
0.353 |
|
| 1979 |
Strong DD, Watt KWK, Cottrell BA, Doolittle RF. Amino acid sequence studies on the α chain of human fibrinogen. complete sequence of the largest cyanogen bromide fragment Biochemistry. 18: 5399-5404. PMID 518844 DOI: 10.1021/Bi00591A022 |
0.447 |
|
| 1979 |
Doolittle RF, Watt KWK, Cottrell BA, Strong DD, Riley M. The amino acid sequence of the α-chain of human fibrinogen Nature. 280: 464-468. PMID 460425 DOI: 10.1038/280464A0 |
0.42 |
|
| 1979 |
Doolittle RF, Cottrell BA, Strong D, Watt KW. Preliminary report on the amino acid sequence of the alpha-chain of human fibrinogen. Thrombosis Research. 14: 787-92. PMID 158235 DOI: 10.1016/0049-3848(79)90133-6 |
0.401 |
|
| 1979 |
Doolittle RF, Cottrell BA, Strong D, Watt KW. Sequence of amino acids comprising the single intra-chain disulfide loop in the alpha-chain of human fibrinogen. Biochemical and Biophysical Research Communications. 84: 495-500. PMID 152630 DOI: 10.1016/0006-291X(78)90196-1 |
0.424 |
|
| 1978 |
Cottrell BA, Doolittle RF. The amino acid sequence of the carboxy-terminal 142 amino acids of the alpha-chain of human fibrinogen. Thrombosis Research. 12: 1135-46. PMID 694821 DOI: 10.1016/0049-3848(78)90068-3 |
0.433 |
|
| 1978 |
Doolittle RF, Goldbaum DM, Doolittle LR. Designation of sequences involved in the "coiled-coil" interdomainal connections in fibrinogen: constructions of an atomic scale model. Journal of Molecular Biology. 120: 311-25. PMID 642011 DOI: 10.1016/0022-2836(78)90070-0 |
0.375 |
|
| 1978 |
Watt KW, Takagi T, Doolittle RF. Amino acid sequence of the beta chain of human fibrinogen: homology with the gamma chain. Proceedings of the National Academy of Sciences of the United States of America. 75: 1731-5. PMID 273904 DOI: 10.1073/Pnas.75.4.1731 |
0.39 |
|
| 1978 |
Friedmann T, Doolittle RF, Walter G. Amino acid sequence homology between polyoma and SV40 tumour antigens deduced from nucleotide sequences. Nature. 274: 291-3. PMID 210390 DOI: 10.1038/274291A0 |
0.394 |
|
| 1977 |
Cottrell BA, Doolittle RF. Amino acid sequences of lamprey fibrinopeptides A and B and characterizations of the junctions split by lamprey and mammalian thrombins. Biochimica Et Biophysica Acta. 453: 426-38. PMID 999898 DOI: 10.1016/0005-2795(76)90138-0 |
0.426 |
|
| 1977 |
Doolittle RF, Cassman KG, Cottrell BA, Friezner SJ, Hucko JT, Takagi T. Amino acid sequence studies on the alpha chain of human fibrinogen. Characterization of 11 cyanogen bromide fragments. Biochemistry. 16: 1703-9. PMID 856257 DOI: 10.1021/Bi00627A028 |
0.453 |
|
| 1977 |
Doolittle RF, Cassman KG, Cottrell BA, Friezner SJ. Amino acid sequence studies on the alpha chain of human fibrinogen. Isolation and characterization of two linked alpha-chained cyanogen bromide fragments from fully cross-linked fibrin. Biochemistry. 16: 1715-9. PMID 851527 DOI: 10.1021/Bi00627A030 |
0.392 |
|
| 1977 |
Doolittle LR, Mross GA, Fothergill LA, Doolittle RF. A simple solid-phase amino acid sequencer employing a thioacetylation stepwise degradation procedure Analytical Biochemistry. 78: 491-505. PMID 851221 DOI: 10.1016/0003-2697(77)90109-9 |
0.335 |
|
| 1977 |
Doolittle RF, Cottrell BA, Riley M. Amino acid compositions of the subunit chains of lamprey fibrinogen. Evolutionary significance of some structural anomalies. Biochimica Et Biophysica Acta. 453: 439-52. PMID 826275 DOI: 10.1016/0005-2795(76)90139-2 |
0.397 |
|
| 1977 |
Doolittle RF, Cassman KG, Cottrell BA, Friezner SJ, Takagi T. Amino acid sequence studies on the alpha chain of human fibrinogen. Covalent structure of the alpha-chain portion of fragment D. Biochemistry. 16: 1710-5. PMID 139916 DOI: 10.1021/Bi00627A029 |
0.428 |
|
| 1976 |
Cottrell BA, Doolittle RF. The amino acid sequence of a 27-residue peptide released from the alpha-chain carboxy-terminus during the plasmic digestion of human fibrinogen. Biochemical and Biophysical Research Communications. 71: 754-61. PMID 134710 DOI: 10.1016/0006-291X(76)90895-0 |
0.417 |
|
| 1976 |
Takagi T, Doolittle RF. Amino acid sequence studies on the alpha chain of human fibrinogen. Location of four plasmin attack points and a covalent cross-linking site. Biochemistry. 14: 5149-56. PMID 127612 DOI: 10.1021/Bi00694A020 |
0.415 |
|
| 1976 |
Takagi T, Doolittle RF. The amino acid sequences of those portions of human fibrinogen fragment E which are not included in the amino-terminal disulfide knot. Thrombosis Research. 7: 813-8. PMID 54947 DOI: 10.1016/0049-3848(75)90206-6 |
0.408 |
|
| 1975 |
Doolittle RF, Wooding GL, Lin Y, Riley M. Hominoid evolution as judged by fibrinopeptide structures. Journal of Molecular Evolution. 1: 74-83. PMID 5006251 DOI: 10.1007/Bf01659395 |
0.401 |
|
| 1975 |
Doolittle RF, Wooding GL. The subunit structure of lamprey fibrinogen and fibrin. Biochimica Et Biophysica Acta. 371: 277-82. PMID 4474019 DOI: 10.1016/0005-2795(74)90024-5 |
0.338 |
|
| 1975 |
Doolittle RF, Cottrell BA. Lamprey fibrinopeptide B is a glycopeptide. Biochemical and Biophysical Research Communications. 60: 1090-6. PMID 4429563 DOI: 10.1016/0006-291X(74)90424-0 |
0.328 |
|
| 1975 |
Gaulton GN, Doolittle RF. Amino-terminal analysis of human fibrinogen treated with estrogenic steroids: Failure to support a thrombin-mimetic proteolytic effect Thrombosis Research. 7: 789-795. PMID 1209562 DOI: 10.1016/0049-3848(75)90203-0 |
0.309 |
|
| 1975 |
Takagi T, Doolittle RF. Amino acid sequence of the carboxy-terminal cyanogen bromide peptide of the human fibrinogen beta-chain: homology with the corresponding gamma-chain peptide and presence in fragment D. Biochimica Et Biophysica Acta. 386: 617-22. PMID 124585 DOI: 10.1016/0005-2795(75)90306-2 |
0.403 |
|
| 1975 |
Takagi T, Doolittle RF. Amino acid sequence studies on plasmin-derived fragments of human fibrinogen: amino-terminal sequences of intermediate and terminal fragments. Biochemistry. 14: 940-6. PMID 123758 DOI: 10.1021/Bi00676A010 |
0.409 |
|
| 1974 |
Takagi T, Doolittle RF. Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin. Biochemistry. 13: 750-6. PMID 4811064 DOI: 10.1021/Bi00701A018 |
0.375 |
|
| 1974 |
Doolittle RF. Structural aspects of the fibrinogen to fibrin conversion. Advances in Protein Chemistry. 27: 1-109. PMID 4589664 DOI: 10.1016/S0065-3233(08)60446-5 |
0.344 |
|
| 1972 |
Sharp J, Cassman K, Doolittle R. Amino acid sequence of the carboxy-terminal cyanogen bromide fragment from bovine and human fibrinogen γ-chains Febs Letters. 25: 334-336. DOI: 10.1016/0014-5793(72)80517-9 |
0.428 |
|
| 1971 |
Fuller GM, Doolittle RF. Studies of invertebrate fibrinogen. II. Transformation of lobster fibrinogen into fibrin Biochemistry. 10: 1311-1315. PMID 5580652 DOI: 10.1021/Bi00784A006 |
0.321 |
|
| 1971 |
Fuller GM, Doolittle RF. Studies of invertebrate fibrinogen. I. Purification and characterization of fibrinogen from the spiny lobster Biochemistry. 10: 135-1311. PMID 5580651 DOI: 10.1021/Bi00784A005 |
0.318 |
|
| 1971 |
Currie BL, Sievertsson H, Bogentoft C, Chang JK, Folkers K, Bowers CY, Doolittle RF. Data on structure of bovine LRH by inactivation. Biochemical and Biophysical Research Communications. 42: 1180-4. PMID 4994511 DOI: 10.1016/0006-291X(71)90030-1 |
0.321 |
|
| 1970 |
Doolittle RF, Mross GA. Identity of chimpanzee with human fibrinopeptides. Nature. 225: 643-644. PMID 5461008 DOI: 10.1038/225643A0 |
0.385 |
|
| 1970 |
Chen R, Doolittle RF. Isolation, characterization, and location of a donor-acceptor unit from cross-linked fibrin. Proceedings of the National Academy of Sciences of the United States of America. 66: 472-9. PMID 5271175 DOI: 10.1073/Pnas.66.2.472 |
0.358 |
|
| 1970 |
Doolittle RF, Chen R, Glasgow C, Mross G, Weinstein M. The molecular constancy of fibrinopeptides A and B from 125 individual humans. Humangenetik. 10: 15-29. PMID 4988845 DOI: 10.1007/Bf00297636 |
0.34 |
|
| 1969 |
Doolittle RF, Astrin KH. Light chains of rabbit immunoglobulin: assignment to the kappa class. Science (New York, N.Y.). 156: 1755-7. PMID 4180574 DOI: 10.1126/Science.156.3783.1755 |
0.342 |
|
| 1969 |
Chen R, Doolittle RF. IDENTIFICATION OF THE POLYPEPTIDE CHAINS INVOLVED IN THE CROSS-LINKING OF FIBRIN Proceedings of the National Academy of Sciences. 63: 420-427. DOI: 10.1073/Pnas.63.2.420 |
0.309 |
|
| 1968 |
Doolittle RF, Armentrout RW. Pyrrolidonyl peptidase. An enzyme for selective removal of pyrrolidonecarboxylic acid residues from polypeptides. Biochemistry. 7: 516-21. PMID 5644127 DOI: 10.1021/Bi00842A005 |
0.309 |
|
| 1967 |
Doolittle RF, Fuller GM. Quantitative determination of amino-terminal amino acids in crosslinked and non-crosslinked fibrin Biochemical and Biophysical Research Communications. 26: 327-333. PMID 6034356 DOI: 10.1016/0006-291X(67)90126-X |
0.354 |
|
| 1967 |
Doolittle RF, Schubert D, Schwartz SA. Amino acid sequence studies on artiodactyl fibrinopeptides. I. Dromedary camel, mule deer, and cape buffalo Archives of Biochemistry and Biophysics. 118: 456-467. PMID 6033721 DOI: 10.1016/0003-9861(67)90374-8 |
0.383 |
|
| 1967 |
Doolittle RF. The amino-terminal amino acid sequences of rabbit immunoglobulin light chains. Proceedings of the National Academy of Sciences of the United States of America. 55: 1195-201. PMID 4163205 DOI: 10.1073/Pnas.55.5.1195 |
0.401 |
|
| 1967 |
Mross G, Doolittle R. Amino acid sequence studies on artiodactyl fibrinopeptides Archives of Biochemistry and Biophysics. 122: 674-684. DOI: 10.1016/0003-9861(67)90177-4 |
0.393 |
|
| 1966 |
Doolittle RF, Singer SJ, Metzger H. Evolution of immunoglobulin polypeptide chains: carboxy-terminal of an IgM heavy chain. Science (New York, N.Y.). 154: 1561-2. PMID 4162777 DOI: 10.1126/Science.154.3756.1561 |
0.39 |
|
| 1966 |
Singer SJ, Doolittle RF. Antibody active sites and immunoglobulin molecules. Science (New York, N.Y.). 153: 13-25. PMID 4160942 DOI: 10.1126/Science.153.3731.13 |
0.346 |
|
| 1966 |
Fuller G, Doolittle R. The formation of crosslinked fibrins: Evidence for the involvement of lysine ε-amino groups Biochemical and Biophysical Research Communications. 25: 694-700. DOI: 10.1016/0006-291X(66)90511-0 |
0.306 |
|
| 1964 |
Doolittle RF, Blombäck B. Amino-Acid Sequence Investigations Of Fibrinopeptides From Various Mammals: Evolutionary Implications. Nature. 202: 147-152. PMID 14156289 DOI: 10.1038/202147A0 |
0.394 |
|
| 1963 |
Blomback B, Doolittle RF. Amino acid sequence studies on fibrinopeptides from several species. Acta Chemica Scandinavica. 17: 1819-22. PMID 22132445 DOI: 10.3891/Acta.Chem.Scand.17-1819 |
0.608 |
|
| 1963 |
Blomback B, Doolittle RF. The sequence of amino acids at the N-terminal end of bovine fibrinopeptide B. Acta Chemica Scandinavica. 17: 1816-9. PMID 22132444 DOI: 10.3891/Acta.Chem.Scand.17-1816 |
0.609 |
|
| 1962 |
Doolittle RF, Oncley JL, Surgenor DM. Species differences in the interaction of thrombin and fibrinogen. The Journal of Biological Chemistry. 237: 3123-7. PMID 22103031 |
0.576 |
|
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