| Year |
Citation |
Score |
| 2017 |
Yersak JM, Montie HL, Chevalier-Larsen ES, Liu Y, Huang L, Rechsteiner M, Merry DE. The 11S Proteasomal Activator REGγ Impacts Polyglutamine-Expanded Androgen Receptor Aggregation and Motor Neuron Viability through Distinct Mechanisms. Frontiers in Molecular Neuroscience. 10: 159. PMID 28596723 DOI: 10.3389/Fnmol.2017.00159 |
0.362 |
|
| 2013 |
Gorbea C, Rechsteiner M, Vallejo JG, Bowles NE. Depletion of the 26S proteasome adaptor Ecm29 increases Toll-like receptor 3 signaling. Science Signaling. 6: ra86. PMID 24084648 DOI: 10.1126/Scisignal.2004301 |
0.311 |
|
| 2010 |
Zhang H, Rajasekaran NS, Orosz A, Xiao X, Rechsteiner M, Benjamin IJ. Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways. Journal of Molecular and Cellular Cardiology. 49: 918-30. PMID 20863832 DOI: 10.1016/J.Yjmcc.2010.09.004 |
0.336 |
|
| 2010 |
Gorbea C, Pratt G, Ustrell V, Bell R, Sahasrabudhe S, Hughes RE, Rechsteiner M. A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components. The Journal of Biological Chemistry. 285: 31616-33. PMID 20682791 DOI: 10.1074/Jbc.M110.154120 |
0.391 |
|
| 2008 |
Pratt G, Rechsteiner M. Proteasomes cleave at multiple sites within polyglutamine tracts: activation by PA28gamma(K188E). The Journal of Biological Chemistry. 283: 12919-25. PMID 18343811 DOI: 10.1074/Jbc.M709347200 |
0.407 |
|
| 2006 |
Gonciarz-Swiatek M, Rechsteiner M. Proteasomes and antigen presentation: evidence that a KEKE motif does not promote presentation of the class I epitope SIINFEKL. Molecular Immunology. 43: 1993-2001. PMID 16423396 DOI: 10.1016/J.Molimm.2005.11.012 |
0.366 |
|
| 2006 |
Gorbea C, Kaufmann AG, Pratt G, Rechsteiner M, Rogers SW. Multiple Forms of the 26S Proteasome-Associated Protein Ecm29 in the Mouse Brain Israel Journal of Chemistry. 46: 207-217. DOI: 10.1560/742P-Et1J-8Rlc-2Jyv |
0.324 |
|
| 2005 |
Ustrell V, Pratt G, Gorbea C, Rechsteiner M. Purification and assay of proteasome activator PA200. Methods in Enzymology. 398: 321-9. PMID 16275339 DOI: 10.1016/S0076-6879(05)98026-9 |
0.389 |
|
| 2005 |
Ortega J, Heymann JB, Kajava AV, Ustrell V, Rechsteiner M, Steven AC. The axial channel of the 20S proteasome opens upon binding of the PA200 activator. Journal of Molecular Biology. 346: 1221-7. PMID 15713476 DOI: 10.1016/J.Jmb.2004.12.049 |
0.378 |
|
| 2005 |
Rechsteiner M, Hill CP. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends in Cell Biology. 15: 27-33. PMID 15653075 DOI: 10.1016/J.Tcb.2004.11.003 |
0.419 |
|
| 2004 |
Baumeister W, Bachmair A, Chau V, Cohen R, Coffino P, Demartino G, Deshaies R, Dohmen J, Emr S, Finley D, Hampton R, Hill C, Hochstrasser M, Huber R, Jackson P, ... ... Rechsteiner M, et al. Varshavsky's contributions. Science (New York, N.Y.). 306: 1290-2. PMID 15550643 DOI: 10.1126/Science.306.5700.1290 |
0.329 |
|
| 2004 |
Gorbea C, Goellner GM, Teter K, Holmes RK, Rechsteiner M. Characterization of mammalian Ecm29, a 26 S proteasome-associated protein that localizes to the nucleus and membrane vesicles. The Journal of Biological Chemistry. 279: 54849-61. PMID 15496406 DOI: 10.1074/Jbc.M410444200 |
0.457 |
|
| 2004 |
Gao X, Li J, Pratt G, Wilk S, Rechsteiner M. Purification procedures determine the proteasome activation properties of REG gamma (PA28 gamma). Archives of Biochemistry and Biophysics. 425: 158-64. PMID 15111123 DOI: 10.1016/J.Abb.2004.03.021 |
0.667 |
|
| 2004 |
Kajava AV, Gorbea C, Ortega J, Rechsteiner M, Steven AC. New HEAT-like repeat motifs in proteins regulating proteasome structure and function. Journal of Structural Biology. 146: 425-30. PMID 15099583 DOI: 10.1016/J.Jsb.2004.01.013 |
0.333 |
|
| 2003 |
Mahaffey DT, Gorbea C, Rechsteiner M. Evidence that DNA replication is not regulated by ubiquitin-dependent proteolysis in Xenopus egg extract. Experimental Cell Research. 288: 225-34. PMID 12915114 DOI: 10.1016/S0014-4827(03)00088-0 |
0.301 |
|
| 2003 |
Goellner GM, Rechsteiner M. Are Huntington's and polyglutamine-based ataxias proteasome storage diseases? The International Journal of Biochemistry & Cell Biology. 35: 562-71. PMID 12672449 DOI: 10.1016/S1357-2725(02)00388-6 |
0.375 |
|
| 2002 |
Ustrell V, Hoffman L, Pratt G, Rechsteiner M. PA200, a nuclear proteasome activator involved in DNA repair. The Embo Journal. 21: 3516-25. PMID 12093752 DOI: 10.1093/Emboj/Cdf333 |
0.368 |
|
| 2002 |
Schmidt T, Lindenberg KS, Krebs A, Schöls L, Laccone F, Herms J, Rechsteiner M, Riess O, Landwehrmeyer GB. Protein surveillance machinery in brains with spinocerebellar ataxia type 3: redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions. Annals of Neurology. 51: 302-10. PMID 11891825 DOI: 10.1002/Ana.10101 |
0.302 |
|
| 2001 |
Harris JL, Alper PB, Li J, Rechsteiner M, Backes BJ. Substrate specificity of the human proteasome. Chemistry & Biology. 8: 1131-41. PMID 11755392 DOI: 10.1016/S1074-5521(01)00080-1 |
0.334 |
|
| 2001 |
Li J, Gao X, Ortega J, Nazif T, Joss L, Bogyo M, Steven AC, Rechsteiner M. Lysine 188 substitutions convert the pattern of proteasome activation by REGgamma to that of REGs alpha and beta. The Embo Journal. 20: 3359-69. PMID 11432824 DOI: 10.1093/Emboj/20.13.3359 |
0.678 |
|
| 2001 |
Li J, Rechsteiner M. Molecular dissection of the 11S REG (PA28) proteasome activators. Biochimie. 83: 373-83. PMID 11295500 DOI: 10.1016/S0300-9084(01)01236-6 |
0.428 |
|
| 2000 |
Li J, Gao X, Joss L, Rechsteiner M. The proteasome activator 11 S REG or PA28: chimeras implicate carboxyl-terminal sequences in oligomerization and proteasome binding but not in the activation of specific proteasome catalytic subunits. Journal of Molecular Biology. 299: 641-54. PMID 10835274 DOI: 10.1006/Jmbi.2000.3800 |
0.679 |
|
| 2000 |
Gorbea C, Taillandier D, Rechsteiner M. Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7. The Journal of Biological Chemistry. 275: 875-82. PMID 10625621 DOI: 10.1074/Jbc.275.2.875 |
0.331 |
|
| 2000 |
Thrower JS, Hoffman L, Rechsteiner M, Pickart CM. Recognition of the polyubiquitin proteolytic signal Embo Journal. 19: 94-102. PMID 10619848 DOI: 10.1093/Emboj/19.1.94 |
0.33 |
|
| 1999 |
Gorbea C, Taillandier D, Rechsteiner M. Assembly of the regulatory complex of the 26S proteasome. Molecular Biology Reports. 26: 15-9. PMID 10363641 DOI: 10.1023/A:1006957802028 |
0.404 |
|
| 1999 |
Mahaffey D, Rechsteiner M. Discrimination between ubiquitin-dependent and ubiquitin-independent proteolytic pathways by the 26S proteasome subunit 5a. Febs Letters. 450: 123-5. PMID 10350069 DOI: 10.1016/S0014-5793(99)00456-1 |
0.404 |
|
| 1999 |
Hoffman L, Gorbea C, Rechsteiner M. Identification, molecular cloning, and characterization of subunit 11 of the human 26S proteasome. Febs Letters. 449: 88-92. PMID 10225435 DOI: 10.1016/S0014-5793(99)00403-2 |
0.435 |
|
| 1999 |
RECHSTEINER M, REALINI C, USTRELL V. The proteasome activator 11 S REG (PA28) and Class I antigen presentation Biochemical Journal. 345: 1-15. DOI: 10.1042/Bj3450001 |
0.39 |
|
| 1998 |
Zhang Z, Clawson A, Rechsteiner M. The proteasome activator 11 S regulator or PA28. Contribution By both alpha and beta subunits to proteasome activation. The Journal of Biological Chemistry. 273: 30660-8. PMID 9804839 DOI: 10.1074/Jbc.273.46.30660 |
0.441 |
|
| 1998 |
Zhang Z, Realini C, Clawson A, Endicott S, Rechsteiner M. Proteasome activation by REG molecules lacking homolog-specific inserts. The Journal of Biological Chemistry. 273: 9501-9. PMID 9545278 DOI: 10.1074/Jbc.273.16.9501 |
0.486 |
|
| 1998 |
Zhang Z, Clawson A, Realini C, Jensen CC, Knowlton JR, Hill CP, Rechsteiner M. Identification of an activation region in the proteasome activator REGalpha. Proceedings of the National Academy of Sciences of the United States of America. 95: 2807-11. PMID 9501171 DOI: 10.1073/Pnas.95.6.2807 |
0.485 |
|
| 1998 |
Young P, Deveraux Q, Beal RE, Pickart CM, Rechsteiner M. Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a Journal of Biological Chemistry. 273: 5461-5467. PMID 9488668 DOI: 10.1074/Jbc.273.10.5461 |
0.405 |
|
| 1998 |
Beal RE, Toscano-Cantaffa D, Young P, Rechsteiner M, Pickart CM. The hydrophobic effect contributes to polyubiquitin chain recognition Biochemistry. 37: 2925-2934. PMID 9485444 DOI: 10.1021/Bi972514P |
0.34 |
|
| 1998 |
Johnston SC, Whitby FG, Realini C, Rechsteiner M, Hill CP. The proteasome 11S regulator subunit REG alpha (PA28 alpha) is a heptamer. Protein Science : a Publication of the Protein Society. 6: 2469-73. PMID 9385652 DOI: 10.1002/Pro.5560061123 |
0.347 |
|
| 1998 |
Dubiel W, Rechsteiner M. The 19S Regulatory Complex of the 26S Proteasome Advances in Molecular and Cell Biology. 27: 129-163. DOI: 10.1016/S1569-2558(08)60460-9 |
0.419 |
|
| 1997 |
Knowlton JR, Johnston SC, Whitby FG, Realini C, Zhang Z, Rechsteiner M, Hill CP. Structure of the proteasome activator REGalpha (PA28alpha). Nature. 390: 639-43. PMID 9403698 DOI: 10.1038/37670 |
0.446 |
|
| 1997 |
Li Y, Gorbea C, Mahaffey D, Rechsteiner M, Benezra R. MAD2 associates with the cyclosome/anaphase-promoting complex and inhibits its activity. Proceedings of the National Academy of Sciences of the United States of America. 94: 12431-6. PMID 9356466 DOI: 10.1073/Pnas.94.23.12431 |
0.331 |
|
| 1997 |
Realini C, Jensen CC, Zhang Z, Johnston SC, Knowlton JR, Hill CP, Rechsteiner M. Characterization of recombinant REGalpha, REGbeta, and REGgamma proteasome activators. The Journal of Biological Chemistry. 272: 25483-92. PMID 9325261 DOI: 10.1074/Jbc.272.41.25483 |
0.446 |
|
| 1997 |
Hoffman L, Rechsteiner M. Effects of nucleotides on assembly of the 26S proteasome and degradation of ubiquitin conjugates. Molecular Biology Reports. 24: 13-6. PMID 9228275 DOI: 10.1023/A:1006892220996 |
0.349 |
|
| 1997 |
Richmond C, Gorbea C, Rechsteiner M. Specific interactions between ATPase subunits of the 26 S protease. The Journal of Biological Chemistry. 272: 13403-11. PMID 9148964 DOI: 10.1074/Jbc.272.20.13403 |
0.353 |
|
| 1997 |
Hoffman L, Rechsteiner M. Molecular cloning and expression of subunit 9 of the 26S proteasome. Febs Letters. 404: 179-84. PMID 9119060 DOI: 10.1016/S0014-5793(97)00126-9 |
0.428 |
|
| 1997 |
Hoffman L, Rechsteiner M. Nucleotidase activities of the 26 S proteasome and its regulatory complex. The Journal of Biological Chemistry. 271: 32538-45. PMID 8955078 DOI: 10.1074/Jbc.271.51.32538 |
0.381 |
|
| 1996 |
Hoffman L, Rechsteiner M. Regulatory features of multicatalytic and 26S proteases. Current Topics in Cellular Regulation. 34: 1-32. PMID 8646844 DOI: 10.1016/S0070-2137(96)80001-X |
0.319 |
|
| 1996 |
Ferrell K, Deveraux Q, van Nocker S, Rechsteiner M. Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease. Febs Letters. 381: 143-8. PMID 8641424 DOI: 10.1016/0014-5793(96)00101-9 |
0.422 |
|
| 1996 |
Li X, Stebbins B, Hoffman L, Pratt G, Rechsteiner M, Coffino P. The N terminus of antizyme promotes degradation of heterologous proteins Journal of Biological Chemistry. 271: 4441-4446. PMID 8626796 DOI: 10.1074/Jbc.271.8.4441 |
0.379 |
|
| 1996 |
Beal R, Deveraux Q, Xia G, Rechsteiner M, Pickart C. Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting Proceedings of the National Academy of Sciences of the United States of America. 93: 861-866. PMID 8570649 DOI: 10.1073/Pnas.93.2.861 |
0.351 |
|
| 1996 |
Van Nocker S, Deveraux Q, Rechsteiner M, Vierstra RD. Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome Proceedings of the National Academy of Sciences of the United States of America. 93: 856-860. PMID 8570648 DOI: 10.1073/Pnas.93.2.856 |
0.441 |
|
| 1996 |
Realini C, Rechsteiner M. A proteasome activator subunit binds calcium. The Journal of Biological Chemistry. 270: 29664-7. PMID 8530352 DOI: 10.1074/Jbc.270.50.29664 |
0.409 |
|
| 1996 |
Deveraux Q, van Nocker S, Mahaffey D, Vierstra R, Rechsteiner M. Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S protease subunit S5a. The Journal of Biological Chemistry. 270: 29660-3. PMID 8530351 DOI: 10.1074/Jbc.270.50.29660 |
0.447 |
|
| 1996 |
Ustrell V, Realini C, Pratt G, Rechsteiner M. Human lymphoblast and erythrocyte multicatalytic proteases: differential peptidase activities and responses to the 11S regulator. Febs Letters. 376: 155-8. PMID 7498531 DOI: 10.1016/0014-5793(95)01257-9 |
0.402 |
|
| 1996 |
Rechsteiner M, Rogers SW. PEST sequences and regulation by proteolysis Trends in Biochemical Sciences. 21: 267-271. DOI: 10.1016/S0968-0004(96)10031-1 |
0.336 |
|
| 1995 |
Ustrell V, Pratt G, Rechsteiner M. Effects of interferon gamma and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases. Proceedings of the National Academy of Sciences of the United States of America. 92: 584-8. PMID 7831334 DOI: 10.1073/Pnas.92.2.584 |
0.399 |
|
| 1995 |
Dubiel W, Ferrell K, Dumdey R, Standera S, Prehn S, Rechsteiner M. Molecular cloning and expression of subunit 12: a non-MCP and non-ATPase subunit of the 26 S protease. Febs Letters. 363: 97-100. PMID 7729561 DOI: 10.1016/0014-5793(95)00288-K |
0.405 |
|
| 1995 |
Mahaffey DT, Yoo Y, Rechsteiner M. Ubiquitination of full-length cyclin. Febs Letters. 370: 109-12. PMID 7649287 DOI: 10.1016/0014-5793(95)00799-F |
0.342 |
|
| 1995 |
Dubiel W, Ferrell K, Rechsteiner M. Subunits of the regulatory complex of the 26S protease. Molecular Biology Reports. 21: 27-34. PMID 7565660 DOI: 10.1007/Bf00990967 |
0.328 |
|
| 1995 |
Deveraux Q, Jensen C, Rechsteiner M. Molecular cloning and expression of a 26 S protease subunit enriched in dileucine repeats. The Journal of Biological Chemistry. 270: 23726-9. PMID 7559544 DOI: 10.1074/Jbc.270.40.23726 |
0.444 |
|
| 1994 |
Dubiel W, Ferrell K, Rechsteiner M. Tat-binding protein 7 is a subunit of the 26S protease. Biological Chemistry Hoppe-Seyler. 375: 237-40. PMID 8060531 DOI: 10.1515/Bchm3.1994.375.4.237 |
0.395 |
|
| 1994 |
Realini C, Rogers SW, Rechsteiner M. KEKE motifs. Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors. Febs Letters. 348: 109-13. PMID 8034024 DOI: 10.1016/0014-5793(94)00569-9 |
0.401 |
|
| 1993 |
Dubiel W, Ferrell K, Rechsteiner M. Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease. Febs Letters. 323: 276-8. PMID 8500623 DOI: 10.1016/0014-5793(93)81356-5 |
0.368 |
|
| 1992 |
Hiroi Y, Rechsteiner M. Ubiquitin metabolism in HeLa cells starved of amino acids. Febs Letters. 307: 156-61. PMID 1322828 DOI: 10.1016/0014-5793(92)80757-8 |
0.326 |
|
| 1992 |
Yoo Y, Watts S, Rechsteiner M. Ubiquitin-RAS peptide extensions as substrates for farnesyl-protein transferase and carboxymethyltransferase Biochemical Journal. 285: 55-60. PMID 1322127 DOI: 10.1042/Bj2850055 |
0.376 |
|
| 1991 |
Di Cola D, Pratt G, Rechsteiner M. Multicatalytic and 26 S ubiquitin/ATP-stimulated proteases in maturing rabbit red blood cells. Febs Letters. 280: 137-40. PMID 1849090 DOI: 10.1016/0014-5793(91)80222-O |
0.378 |
|
| 1991 |
Rechsteiner M. Natural substrates of the ubiquitin proteolytic pathway. Cell. 66: 615-8. PMID 1652366 DOI: 10.1016/0092-8674(91)90104-7 |
0.425 |
|
| 1990 |
Yoo Y, Rechsteiner M. The use of ubiquitin-peptide extensions as protein kinase substrates Analytical Biochemistry. 191: 35-40. PMID 1964025 DOI: 10.1016/0003-2697(90)90383-K |
0.357 |
|
| 1989 |
Rechsteiner M. Regulation of enzyme levels by proteolysis: the role of pest regions. Advances in Enzyme Regulation. 27: 135-51. PMID 2907964 DOI: 10.1016/0065-2571(88)90014-3 |
0.422 |
|
| 1989 |
Redman KL, Rechsteiner M. Identification of the long ubiquitin extension as ribosomal protein S27a. Nature. 338: 438-40. PMID 2538756 DOI: 10.1038/338438A0 |
0.415 |
|
| 1988 |
Rechsteiner M. Osmotic lysis of pinosomes. Methods in Enzymology. 149: 42-8. PMID 3695968 DOI: 10.1016/0076-6879(87)49042-3 |
0.306 |
|
| 1988 |
Rechsteiner M. Ubiquitin-mediated pathways for intracellular proteolysis. Annual Review of Cell Biology. 3: 1-30. PMID 2825735 DOI: 10.1146/Annurev.Cb.03.110187.000245 |
0.422 |
|
| 1987 |
Rechsteiner M. Do myc, fos and E1A function as protein phosphatase inhibitors? Biochemical and Biophysical Research Communications. 143: 194-8. PMID 3030314 DOI: 10.1016/0006-291X(87)90649-8 |
0.377 |
|
| 1987 |
Carlson N, Rogers S, Rechsteiner M. Microinjection of ubiquitin: changes in protein degradation in HeLa cells subjected to heat-shock. The Journal of Cell Biology. 104: 547-55. PMID 3029142 DOI: 10.1083/Jcb.104.3.547 |
0.329 |
|
| 1987 |
Carlson N, Rechsteiner M. Microinjection of ubiquitin: intracellular distribution and metabolism in HeLa cells maintained under normal physiological conditions. The Journal of Cell Biology. 104: 537-46. PMID 3029141 DOI: 10.1083/Jcb.104.3.537 |
0.387 |
|
| 1986 |
Rogers S, Wells R, Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science (New York, N.Y.). 234: 364-8. PMID 2876518 DOI: 10.1126/Science.2876518 |
0.4 |
|
| 1985 |
Rechsteiner M, Wu LH, Miller AO. RBC-mediated microinjection of chromatin components into cultured mammalian cells Bibliotheca Haematologica. 142-149. PMID 4004757 DOI: 10.1159/000410237 |
0.352 |
|
| 1984 |
Hough R, Rechsteiner M. Effects of temperature on the degradation of proteins in rabbit reticulocyte lysates after injection into HeLa cells Proceedings of the National Academy of Sciences of the United States of America. 81: 90-94. PMID 6364139 DOI: 10.1073/Pnas.81.1.90 |
0.384 |
|
| 1983 |
Rote KV, Rechsteiner M. Degradation of microinjected proteins: effects of lysosomotropic agents and inhibitors of autophagy. Journal of Cellular Physiology. 116: 103-10. PMID 6853609 DOI: 10.1002/Jcp.1041160116 |
0.385 |
|
| 1983 |
McGarry T, Hough R, Rogers S, Rechsteiner M. Intracellular distribution and degradation of immunoglobulin G and immunoglobulin G fragments injected into HeLa cells Journal of Cell Biology. 96: 338-346. PMID 6403551 DOI: 10.1083/Jcb.96.2.338 |
0.37 |
|
| 1982 |
Wu L, Rechsteiner M, Kuehl L. Comparative studies on microinjected high-mobility-group chromosomal proteins, HMG1 and HMG2. The Journal of Cell Biology. 91: 488-96. PMID 6458621 DOI: 10.1083/Jcb.91.2.488 |
0.388 |
|
| 1982 |
Chin DT, Kuehl L, Rechsteiner M. Conjugation of ubiquitin to denatured hemoglobin is proportional to the rate of hemoglobin degradation in HeLa cells. Proceedings of the National Academy of Sciences of the United States of America. 79: 5857-61. PMID 6310549 DOI: 10.1073/Pnas.79.19.5857 |
0.427 |
|
| 1981 |
Bigelow S, Hough R, Rechsteiner M. The selective degradation of injected proteins occurs principally in the cytosol rather than in lysosomes Cell. 25: 83-93. PMID 7273138 DOI: 10.1016/0092-8674(81)90233-6 |
0.32 |
|
| 1980 |
Manser T, Thacher T, Rechsteiner M. Arginine-rich histones do not exchange between human and mouse chromosomes in hybrid cells. Cell. 19: 993-1003. PMID 7379125 DOI: 10.1016/0092-8674(80)90090-2 |
0.356 |
|
| 1979 |
Rechsteiner M, Kuehl L. Microinjection of the nonhistone chromosomal protein HMG1 into bovine fibroblasts and HeLa cells. Cell. 16: 901-8. PMID 455454 DOI: 10.1016/0092-8674(79)90105-3 |
0.367 |
|
| 1979 |
Schlegel RA, Iversen P, Rechsteiner M. The turnover of tRNAs microinjected into animal cells. Nucleic Acids Research. 5: 3715-29. PMID 214762 DOI: 10.1093/Nar/5.10.3715 |
0.354 |
|
| 1979 |
Zavortink M, Thacher T, Rechsteiner M. Degradation of proteins microinjected into cultured mammalian cells. Journal of Cellular Physiology. 100: 175-85. PMID 112104 DOI: 10.1002/Jcp.1041000118 |
0.391 |
|
| 1976 |
Rechsteiner M, Parsons B. Studies on the intranuclear distribution of human and mouse genomes and formation of human-mouse hybrid cells. Journal of Cellular Physiology. 88: 167-79. PMID 944703 DOI: 10.1002/Jcp.1040880206 |
0.324 |
|
| 1976 |
Rechsteiner M, Hillyard D, Olivera BM. Turnover at nicotinamide adenine dinucleotide in cultures of human cells. Journal of Cellular Physiology. 88: 207-17. PMID 178671 DOI: 10.1002/Jcp.1040880210 |
0.311 |
|
| 1976 |
Rechsteiner M, Hillyard D, Olivera BM. Magnitude and significance of NAD turnover in human cell line D98/AH2. Nature. 259: 695-6. PMID 175293 DOI: 10.1038/259695A0 |
0.325 |
|
| 1976 |
Elliott G, Rechsteiner M. Pyridine nucleotide metabolism in mitotic cells. Journal of Cellular Physiology. 641-51. PMID 172520 DOI: 10.1002/Jcp.1040860509 |
0.331 |
|
| 1975 |
Rechsteiner M. The distribution of pyridine nucleotides between nucleus and cytoplasm. Journal of Cellular Physiology. 84: 481-6. PMID 4154947 DOI: 10.1002/Jcp.1040840316 |
0.302 |
|
| 1975 |
Rechsteiner M, Catanzarite V. The biosynthesis and turnover of nicotinamide adenine dinucleotide in enucleated culture cells. Journal of Cellular Physiology. 84: 409-22. PMID 4154946 DOI: 10.1002/Jcp.1040840309 |
0.321 |
|
| 1974 |
Rechsteiner M, Lund K, Hillyard D, Olivera B. Autoradiographic studies of pyridine nucleotide metabolism in human culture cells. Journal of Cellular Physiology. 83: 389-400. PMID 4151246 DOI: 10.1002/Jcp.1040830309 |
0.324 |
|
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