Source: https://medicine.uiowa.edu/biochemistry/profile/peter-rubenstein
Timestamp: 2019-04-21 23:05:49+00:00

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Our laboratory investigates the biochemistry of actin and the actin binding proteins that modulate its function within the cell. In particular, we are interested in the conformational changes in actin necessary for its polymerization, the forces that stabilize actin monomers within the actin filament, and the manner in which actin filament modulating proteins such as cofilin, Arp2/3 complex and profilin carry out their roles. Our approach is to use yeast actin and the yeast actin cytoskeleton as a model system. Based on hypotheses concerning actin function and actin dynamics, we make mutant actin constructs using site-directed mutagenesis, express the actin in yeast as the only actin in the cell, and determine phenotypes associated with the actin mutation such as altered growth rate, altered endocytosis, and altered actin deposition. We then purify the actin and determine its in vitro behavior using a series of biochemical and biophysical approaches such as electron microscopy and fluorescence spectroscopy. We then try to correlate the effects of the mutations we observe in vitro with the phenotypes associated with these mutations in vivo. With this basic system, we are currently focusing on two projects. We have shown that although the proteins are 90% identical, muscle and yeast actins display distinct differences in their kinetics and ability to interact with different actin binding proteins that can have a substantial effect on actin filament dynamics. To investigate the basis for these differences, we have made a set of yeast/muscle hybrid actins with one yeast half and one muscle half to try to determine which part of the actin is responsible for the behavioral differences seen between the two parent actins. Second, it has been found that six different actin mutations cause autosomal dominant hearing loss in humans. We have cloned each of these into yeast actin and are assessing the effects of these mutations in vivo and in vitro with the goal of gaining insight into altered actin interactions that might result in deafness.
Niederhoffer, E. C., Cline, S. D., Osheroff, N., Simmons, J. M., Diekman, A. B., Franklin, D. S., Abali, E. E., Bateman, Jr, R. C., Fontes, J. D., Lindsley, J. E., Pearson, D., Rubenstein, P. A., Slaughter, C. A., Bernstein, J. A., Hyland, K. M., Park, V. M., Sobering, A. K., Weiler, T. A. & Dasgupta, S. (2017). Teaching Biochemistry and Genetics to Students of Dentistry, Medicine, and Pharmacy 6th International Conference of the Association of Biochemistry Educators (ABE) Clearwater Beach, FL, USA, May 7-11, 2017. Medical science educator, 27(4), 855-859. PMID: 29291139.
Lee, C. Y., Lou, J., Wen, K. K., McKane, M., Eskin, S. G., Rubenstein, P. A., Chien, S., Ono, S., Zhu, C. & McIntire, L. V. (2016). Regulation of actin catch-slip bonds with a RhoA-formin module. Scientific reports, 6, 35058. PMID: 27731359.
Jepsen, L., Kruth, K. A., Rubenstein, P. A. & Sept, D. (2016). Two Deafness-Causing Actin Mutations (DFNA20/26) Have Allosteric Effects on the Actin Structure. Biophysical journal, 111(2), 323-32. PMID: 27463135.
Jepsen, L., Kruth, K. A. & Rubenstein, P. A. (2016). Molecular Effects of Deafness Mutations in Actin. Biophys J, 1110(2), 354a. DOI: 10.1016/j.bpj.2015.11.1909.
Rubenstein, P. A., Wen, K. K. (2015). Mutant vascular actin is a TAAD misbehaving. Proceedings of the National Academy of Sciences of the United States of America, 112(31), 9500-1. PMID: 26204915.
Rubenstein, P. A., Wen, K. K. (2014). Insights into the effects of disease-causing mutations in human actins. Cytoskeleton (Hoboken). PMID: 24574087.
Yamashiro, S., Gokhin, D., Sui, Z., Bergeron, S., Rubenstein, P. & Fowler, V. (2014). Differential actin-regulatory activities of Tropomodulin1 and Tropomodulin3 with diverse tropomyosin and actin isoforms. J Biol Chem, 289(17), 11616-29. PMID: 24644292.
Bai, F., Caster, H., Rubenstein, P., Dawson, J. & Kawai, M. (2014). Using baculovirus/insect cell expressed recombinant actin to study the molecular pathogenesis of HCM caused by actin mutation A331P. J Mol Cell Cardiol, 74, 64-75. PMID: 24793351.
Wen, K. K., McKane, M. & Rubenstein, P. A. (2013). Importance of a Lys113-Glu195 Intermonomer Ionic Bond in F-actin Stabilization and Regulation by Yeast Formins Bni1p and Bnr1p. The Journal of Biological Chemistry, 288(26), 19140-53. PMID: 23653364.
Johnston, J. J., Wen, K. K., Keppler-Noreuil, K., McKane, M., Maiers, J. L., Greiner, A. & Sapp, J. C. (2013). Functional Analysis of a De Novo ACTB Mutation in a Patient with Atypical Baraitser-Winter Syndrome. Human Mutation, doi: 10.1002/humu.22350. PMID: 23649928.
Lee, C. Y., Lou, J., Wen, K. K., McKane, M., Eskin, S. G., Ono, S., Chien, S., Rubenstein, P. A., Zhu, C. & McIntire, L. V. (2013). Actin depolymerization under force is governed by lysine 113:glutamic acid 195-mediated catch-slip bonds. Proceedings of the National Academy of Sciences of the United States of America, 110(13), 5022-7. PMID: 23460697.
Rubenstein, P. A., Mayer, E. A. (2012). Familial visceral myopathies: From symptom-based syndromes to actin-related diseases. Gastroenterology, 143(6). PMID: 23085350.
Glenn, N. O., McKane, M., Kohli, V., Wen, K. K., Rubenstein, P. A., Bartman, T. & Sumanas, S. (2012). The W-loop of alpha-cardiac actin is critical for heart function and endocardial cushion morphogenesis in zebrafish. Molecular and Cellular Biology, 32(17), 3527-40. PMID: 22751927.
Malloy, L. E., Wen, K. K., Pierick, A. R., Wedemeyer, E. W., Bergeron, S. E., Vanderpool, N. D., McKane, M., Rubenstein, P. A. & Bartlett, H. L. (2012). Thoracic aortic aneurysm (TAAD)-causing mutation in actin affects formin regulation of polymerization. The Journal of Biological Chemistry, 287(34), 28398-408. PMID: 22753406.
Kruth, K. A., Rubenstein, P. A. (2012). Two deafness-causing (DFNA20/26) actin mutations affect Arp2/3-dependent actin regulation. The Journal of Biological Chemistry, 287(32), 27217-26. PMID: 22718764.
Wen, K. K., McKane, M., Stokasimov, E. & Rubenstein, P. A. (2011). Mutant profilin suppresses mutant actin-dependent mitochondrial phenotype in Saccharomyces cerevisiae. The Journal of Biological Chemistry, 286(48), 41745-57. PMID: 21956104.
Stark, B. C., Wen, K. K., Allingham, J. S., Rubenstein, P. A. & Lord, M. (2011). Functional adaptation between yeast actin and its cognate myosin motors. The Journal of Biological Chemistry, 286(35), 30384-92. PMID: 21757693.
Bergeron, S. E., Wedemeyer, E. W., Lee, R., Wen, K. K., McKane, M., Pierick, A. R., Berger, A. P., Rubenstein, P. A. & Bartlett, H. L. (2011). Allele-specific effects of thoracic aortic aneurysm and dissection alpha-smooth muscle actin mutations on actin function. The Journal of Biological Chemistry, 286(13), 11356-69. PMID: 21288906.
Kudryashov, D. S., Grintsevich, E. E., Rubenstein, P. A. & Reisler, E. (2010). A nucleotide state-sensing region on actin. The Journal of Biological Chemistry, 285(33), 25591-601. PMID: 20530485.
Wen, K. K., McKane, M., Stokasimov, E., Fields, J. & Rubenstein, P. A. (2010). A potential yeast actin allosteric conduit dependent on hydrophobic core residues val-76 and trp-79. The Journal of Biological Chemistry, 285(27), 21185-94. PMID: 20442407.
Bergeron, S. E., Zhu, M., Thiem, S. M., Friderici, K. H. & Rubenstein, P. A. (2010). Ion-dependent polymerization differences between mammalian beta- and gamma-nonmuscle actin isoforms. The Journal of Biological Chemistry, 285(21), 16087-95. PMID: 20308063.
Wen, K. K., Rubenstein, P. A. & DeMali, K. A. (2009). Vinculin nucleates actin polymerization and modifies actin filament structure. The Journal of Biological Chemistry, 284(44), 30463-73. PMID: 19736312.
Stokasimov, E., Rubenstein, P. A. (2009). Actin isoform-specific conformational differences observed with hydrogen/deuterium exchange and mass spectrometry. The Journal of Biological Chemistry, 284(37), 25421-30. PMID: 19605362.
MorÃ­n, M., Bryan, K. E., Mayo-Merino, F., Goodyear, R., MencÃ­a, A., Modamio-HÃ¸ybjÃ¸r, S., del Castillo, I., Cabalka, J. M., Richardson, G., Moreno, F. & Rubenstein, P. A. (2009). In vivo and in vitro effects of two novel gamma-actin (ACTG1) mutations that cause DFNA20/26 hearing impairment. Human Molecular Genetics, 18(16), 3075-89. PMID: 19477959.
Bryan, K. E., Rubenstein, P. A. (2009). Allele-specific effects of human deafness gamma-actin mutations (DFNA20/26) on the actin/cofilin interaction. The Journal of Biological Chemistry, 284(27), 18260-9. PMID: 19419963.
Wen, K. K., Rubenstein, P. A. (2009). Differential regulation of actin polymerization and structure by yeast formin isoforms. The Journal of Biological Chemistry, 284(25), 16776-83. PMID: 19386598.
Scoville, D., Stamm, J. D., Altenbach, C., Shvetsov, A., Kokabi, K., Rubenstein, P. A., Hubbell, W. L. & Reisler, E. (2009). Effects of binding factors on structural elements in F-actin. Biochemistry, 48(2), 370-8. PMID: 19113841.
Stokasimov, E., McKane, M. & Rubenstein, P. A. (2008). Role of intermonomer ionic bridges in the stabilization of the actin filament. The Journal of Biological Chemistry, 283(50), 34844-54. PMID: 18945676.
Wen, K. K., McKane, M., Houtman, J. C. & Rubenstein, P. A. (2008). Control of the ability of profilin to bind and facilitate nucleotide exchange from G-actin. The Journal of Biological Chemistry, 283(14), 9444-53. PMID: 18223293.
Shvetsov, A., Galkin, V. E., Orlova, A., Phillips, M., Bergeron, S. E., Rubenstein, P. A., Egelman, E. H. & Reisler, E. (2008). Actin hydrophobic loop 262-274 and filament nucleation and elongation. Journal of Molecular Biology, 375(3), 793-801. PMID: 18037437.
Scoville, D., Stamm, J. D., Toledo-Warshaviak, D., Altenbach, C., Phillips, M., Shvetsov, A., Rubenstein, P. A., Hubbell, W. L. & Reisler, E. (2006). Hydrophobic loop dynamics and actin filament stability. Biochemistry, 45(45), 13576-84. PMID: 17087511.
McKane, M., Wen, K. K., Meyer, A. & Rubenstein, P. A. (2006). Effect of the substitution of muscle actin-specific subdomain 1 and 2 residues in yeast actin on actin function. The Journal of Biological Chemistry, 281(40), 29916-28. PMID: 16882670.
Bryan, K. E., Wen, K. K., Zhu, M., Rendtorff, N. D., Feldkamp, M., Tranebjaerg, L., Friderici, K. H. & Rubenstein, P. A. (2006). Effects of human deafness gamma-actin mutations (DFNA20/26) on actin function. The Journal of Biological Chemistry, 281(29), 20129-39. PMID: 16690605.
Shvetsov, A., Stamm, J. D., Phillips, M., Warshaviak, D., Altenbach, C., Rubenstein, P. A., Hideg, K., Hubbell, W. L. & Reisler, E. (2006). Conformational dynamics of loop 262-274 in G- and F-actin. Biochemistry, 45(20), 6541-9. PMID: 16700564.
Chen, W., Wen, K. K., Sens, A. E. & Rubenstein, P. A. (2006). Differential interaction of cardiac, skeletal muscle, and yeast tropomyosins with fluorescent (pyrene235) yeast actin. Biophysical Journal, 90(4), 1308-18. PMID: 16326906.
McKane, M., Wen, K. K., Boldogh, I. R., Ramcharan, S., Pon, L. A. & Rubenstein, P. A. (2005). A mammalian actin substitution in yeast actin (H372R) causes a suppressible mitochondria/vacuole phenotype. (43), pp. 36494-501. The Journal of Biological Chemistry. PMID: 16118223.
Rubenstein, P. A., Wen, K. K. (2005). Lights, camera, actin. (10), pp. 683-7. IUBMB life. PMID: 16223708.
Wen, K. K., Rubenstein, P. A. (2005). Acceleration of yeast actin polymerization by yeast Arp2/3 complex does not require an Arp2/3-activating protein. The Journal of Biological Chemistry, 280(25), 24168-74. PMID: 15857833.
Lu, X., Bryant, M. K., Bryan, K. E., Rubenstein, P. A. & Kawai, M. (2005). Role of the N-terminal negative charges of actin in force generation and cross-bridge kinetics in reconstituted bovine cardiac muscle fibres. The Journal of Physiology, 564(Pt 1), 65-82. PMID: 15649975.
Bryan, K. E., Rubenstein, P. A. (2005). An intermediate form of ADP-F-actin. The Journal of Biological Chemistry, 280(2), 1696-703. PMID: 15536092.
Orlova, A., Shvetsov, A., Galkin, V. E., Kudryashov, D. S., Rubenstein, P. A., Egelman, E. H. & Reisler, E. (2004). Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization. Proceedings of the National Academy of Sciences of the United States of America, 101(51), 17664-8. PMID: 15591338.
Bartman, T., Walsh, E. C., Wen, K. K., McKane, M., Ren, J., Alexander, J., Rubenstein, P. A. & Stainier, D. Y. (2004). Early myocardial function affects endocardial cushion development in zebrafish. PLoS Biology, 2(5), E129. PMID: 15138499.
Rubenstein, P. A. (2004). Alcohol metabolism (sung to the tune of amazing grace). (Vols. 32). (2), pp. 30. Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology. PMID: 21706696.
Wen, K. K., Blake, M. S. & Rubenstein, P. A. (2004). Neisseria gonorrhoeae porin, P.IB, causes release of ATP from yeast actin. Journal of Muscle Research and Cell Motility, 25, 343-50. PMID: 15548863.
Wen, K. K., Rubenstein, P. A. (2003). Biochemical consequences of the cardiofunk (R177H) mutation in yeast actin. The Journal of Biological Chemistry, 278(48), 48386-94. PMID: 13129918.
Vorobiev, S., Strokopytov, B., Drubin, D. G., Frieden, C., Ono, S., Condeelis, J., Rubenstein, P. A. & Almo, S. C. (2003). The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism. Proceedings of the National Academy of Sciences of the United States of America, 100(10), 5760-5. PMID: 12732734.
Kusner, D. J., Barton, J. A., Wen, K. K., Wang, X., Rubenstein, P. A. & Iyer, S. S. (2002). Regulation of phospholipase D activity by actin. Actin exerts bidirectional modulation of Mammalian phospholipase D activity in a polymerization-dependent, isoform-specific manner. The Journal of Biological Chemistry, 277(52), 50683-92. PMID: 12388543.
Wong, W. W., Gerson, J. H., Rubenstein, P. A. & Reisler, E. (2002). Thin filament regulation and ionic interactions between the N-terminal region in actin and troponin. Biophysical Journal, 83(5), 2726-32. PMID: 12414705.
Wen, K. K., Yao, X. & Rubenstein, P. A. (2002). GTP-yeast actin. The Journal of Biological Chemistry, 277(43), 41101-9. PMID: 12191996.
Shvetsov, A., Musib, R., Phillips, M., Rubenstein, P. A. & Reisler, E. (2002). Locking the hydrophobic loop 262-274 to G-actin surface by a disulfide bridge prevents filament formation. Biochemistry, 41(35), 10787-93. PMID: 12196017.
Musib, R., Wang, G., Geng, L. & Rubenstein, P. A. (2002). Effect of polymerization on the subdomain 3/4 loop of yeast actin. The Journal of Biological Chemistry, 277(25), 22699-709. PMID: 11959868.
Yao, X., Nguyen, V., Wriggers, W. & Rubenstein, P. A. (2002). Regulation of yeast actin behavior by interaction of charged residues across the interdomain cleft. The Journal of Biological Chemistry, 277(25), 22875-82. PMID: 11940592.
Yao, X., Rubenstein, P. A. (2001). F-actin-like ATPase activity in a polymerization-defective mutant yeast actin (V266G/L267G). The Journal of Biological Chemistry, 276(27), 25598-604. PMID: 11328808.
Wen, K. K., Kuang, B. & Rubenstein, P. A. (2000). Tropomyosin-dependent filament formation by a polymerization-defective mutant yeast actin (V266G,L267G). The Journal of Biological Chemistry, 275(51), 40594-600. PMID: 10998421.
Wen, K. K., Giardina, P. C., Blake, M. S., Edwards, J., Apicella, M. A. & Rubenstein, P. A. (2000). Interaction of the gonococcal porin P.IB with G- and F-actin. Biochemistry, 39(29), 8638-47. PMID: 10913272.
Kim, E., Wriggers, W., Phillips, M., Kokabi, K., Rubenstein, P. A. & Reisler, E. (2000). Cross-linking constraints on F-actin structure. Journal of Molecular Biology, 299(2), 421-9. PMID: 10860749.
Hansen, J. E., Marner, J., Pavlov, D., Rubenstein, P. A. & Reisler, E. (2000). Structural transition at actin's N-terminus in the actomyosin cross-bridge cycle. Biochemistry, 39(7), 1792-9. PMID: 10677229.
Yao, X., Grade, S., Wriggers, W. & Rubenstein, P. A. (1999). His(73), often methylated, is an important structural determinant for actin. A mutagenic analysis of HIS(73) of yeast actin. The Journal of Biological Chemistry, 274(52), 37443-9. PMID: 10601317.
Cheng, D., Marner, J. & Rubenstein, P. A. (1999). Interaction in vivo and in vitro between the yeast fimbrin, SAC6P, and a polymerization-defective yeast actin (V266G and L267G). The Journal of Biological Chemistry, 274(50), 35873-80. PMID: 10585472.
Kalhor, H. R., Niewmierzycka, A., Faull, K. F., Yao, X., Grade, S., Clarke, S. & Rubenstein, P. A. (1999). A highly conserved 3-methylhistidine modification is absent in yeast actin. Archives of Biochemistry and Biophysics, 370(1), 105-11. PMID: 10496983.
Eads, J. C., Mahoney, N. M., Vorobiev, S., Bresnick, A. R., Wen, K. K., Rubenstein, P. A., Haarer, B. K. & Almo, S. C. (1998). Structure determination and characterization of Saccharomyces cerevisiae profilin. Biochemistry, 37(32), 11171-81. PMID: 9698363.
Rubenstein, P. A., Tobacman, L. S. (1998). Highlights of the Molecular Interactions of Actin meeting, Hawaii, 1-5 April 1997. (3), pp. 271-6. Journal of Muscle Research and Cell Motility. PMID: 9583367.
Orlova, A., Chen, X., Rubenstein, P. A. & Egelman, E. H. (1997). Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft. Journal of Molecular Biology, 271(2), 235-43. PMID: 9268655.
Feng, L., Kim, E., Lee, W. L., Miller, C. J., Kuang, B., Reisler, E. & Rubenstein, P. A. (1997). Fluorescence probing of yeast actin subdomain 3/4 hydrophobic loop 262-274. Actin-actin and actin-myosin interactions in actin filaments. The Journal of Biological Chemistry, 272(27), 16829-37. PMID: 9201989.
Kuang, B., Rubenstein, P. A. (1997). The effects of severely decreased hydrophobicity in a subdomain 3/4 loop on the dynamics and stability of yeast G-actin. The Journal of Biological Chemistry, 272(7), 4412-8. PMID: 9020164.
Kuang, B., Rubenstein, P. A. (1997). Beryllium fluoride and phalloidin restore polymerizability of a mutant yeast actin (V266G,L267G) with severely decreased hydrophobicity in a subdomain 3/4 loop. The Journal of Biological Chemistry, 272(2), 1237-47. PMID: 8995427.
Miller, C. J., Wong, W. W., Bobkova, E., Rubenstein, P. A. & Reisler, E. (1996). Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle. Biochemistry, 35(51), 16557-65. PMID: 8987990.
Chen, X., Rubenstein, P. A. (1995). A mutation in an ATP-binding loop of Saccharomyces cerevisiae actin (S14A) causes a temperature-sensitive phenotype in vivo and in vitro. The Journal of Biological Chemistry, 270(19), 11406-14. PMID: 7744777.
Chen, X., Peng, J., Pedram, M., Swenson, C. A. & Rubenstein, P. A. (1995). The effect of the S14A mutation on the conformation and thermostability of Saccharomyces cerevisiae G-actin and its interaction with adenine nucleotides. The Journal of Biological Chemistry, 270(19), 11415-23. PMID: 7744778.
Crosbie, R. H., Miller, C., Chalovich, J. M., Rubenstein, P. A. & Reisler, E. (1994). Caldesmon, N-terminal yeast actin mutants, and the regulation of actomyosin interactions. Biochemistry, 33(11), 3210-6. PMID: 8136356.
Chen, X., Cook, R. K. & Rubenstein, P. A. (1993). Yeast actin with a mutation in the "hydrophobic plug" between subdomains 3 and 4 (L266D) displays a cold-sensitive polymerization defect. The Journal of Cell Biology, 123(5), 1185-95. PMID: 8245125.
Cook, R. K., Root, D., Miller, C., Reisler, E. & Rubenstein, P. A. (1993). Enhanced stimulation of myosin subfragment 1 ATPase activity by addition of negatively charged residues to the yeast actin NH2 terminus. The Journal of Biological Chemistry, 268(4), 2410-5. PMID: 8428914.
Babcock, G., Rubenstein, P. A. (1993). Control of profilin and actin expression in muscle and nonmuscle cells. Cell Motility and the Cytoskeleton, 24(3), 179-88. PMID: 8385578.
Cook, R., Rubenstein, P. (1993). An actin mutation rescues a tropomyosin deletion in yeast. (Vols. 4:S). (36a) Mol. Biol. Cell.
Chen, X., Rubenstein, P. (1993). Yeast S14A actin has a lower thermostability and a higher Kd for etheno ATP than yeast wild-type actin in vitro. (Vols. 4:S). (36a) Mol. Biol. Cell.
Al-Alami, J., Miller, C., Reisler, E. & Rubenstein, P. (1993). The functional significance of actin ala7. (Vols. 4:S). (36a) Mol. Biol. Cell.
Sheff, D. R., Rubenstein, P. A. (1992). Isolation and characterization of the rat liver actin N-acetylaminopeptidase. The Journal of Biological Chemistry, 267(28), 20217-24. PMID: 1400339.
Cao, L. G., Babcock, G. G., Rubenstein, P. A. & Wang, Y. L. (1992). Effects of profilin and profilactin on actin structure and function in living cells. The Journal of Cell Biology, 117(5), 1023-9. PMID: 1577865.
Wang, Y. C., Rubenstein, P. A. (1992). Splicing of two alternative exon pairs in beta-tropomyosin pre-mRNA is independently controlled during myogenesis. The Journal of Biological Chemistry, 267(17), 12004-10. PMID: 1601870.
Cook, R. K., Blake, W. T. & Rubenstein, P. A. (1992). Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo. The Journal of Biological Chemistry, 267(13), 9430-6. PMID: 1349604.
Sheff, D. R., Rubenstein, P. A. (1992). Amino-terminal processing of actins mutagenized at the Cys-1 residue. The Journal of Biological Chemistry, 267(4), 2671-8. PMID: 1733964.
Wang, Y. C., Rubenstein, P. A. (1992). Choice of 3' cleavage/polyadenylation site in beta-tropomyosin RNA processing is differentiation-dependent in mouse BC3H1 muscle cells. The Journal of Biological Chemistry, 267(4), 2728-36. PMID: 1733968.
Cook, R. K., Rubenstein, P. A. (1992). The genertion and isolation of mutant actins in practical approaches in cell biology. K. Carraway , Carraway (Eds.) pp. 99-122. IRL Press.
Cook, R. K., Sheff, D. R. & Rubenstein, P. A. (1991). Unusual metabolism of the yeast actin amino terminus. The Journal of Biological Chemistry, 266(25), 16825-33. PMID: 1885608.
Cook, R., Blake, W. & Rubenstein, P. (1991). A negatively charged actin amino-terminus is not essential in yeast. (Vols. 115). (159a) J. Cell Biol..
Sheff, D., Rubenstein, P. (1991). Isolation and characterization of the actin N-Acetyl aminopeptidase. (Vols. 115). (159a) J. Cell Biol..
Rubenstein, P., Cook, R. & Babcock, G. (1991). Do residues 265-268 in yeast actin stabilize the F-actin helix. (Vols. 115). (160a) J. Cell Biol..
Cao, L., Babcock, G., Rubenstein, P. & Wang, Y. (1991). Effects of profiling and profilactin on actin structure and function in living cells. (Vols. 115). (375a) J. Cell Biol..
Wang, Y., Rubenstein, P. (1991). A novel hybrid tropomyosin isoform is expressed from the beta-tropomyosin gene in mouse muscle cells through alternative RNA splicing. (Vols. 115). (378a) J. Cell Biol..
Rubenstein, P. A. (1990). The functional importance of multiple actin isoforms. (7), pp. 309-15. BioEssays : news and reviews in molecular, cellular and developmental biology. PMID: 2203335.
Cook, R., Sheff, D. & Rubenstein, P. (1990). Metabolism of the actin amino terminus. (Vols. 111). (31a) J. Cell Biol..
Babcock, G., Rubenstein, P. (1990). Profilin and actin gene expression are not co-regulated. (Vols. 111). (160a) J. Cell Biol..
Wang, Y., Strauch, A. & Rubenstein, P. (1990). Aberrant 3'-processing of skeletal muscle B-Tropmyosin. (Vols. 111). (327a) J. Cell Biol..
Sheff, D. R., Rubenstein, P. A. (1989). Identification of N-acetylmethionine as the product released during the NH2-terminal processing of a pseudo-class I actin. The Journal of Biological Chemistry, 264(19), 11491-6. PMID: 2738074.
Rubenstein, P. A., Solomon, L. R., Solomon, T. & Gay, L. (1989). Actin structure-function relationships in vitro using oligodeoxynucleotide-directed site-specific mutagenesis. (1), pp. 35-9. Cell Motility and the Cytoskeleton. PMID: 2684425.
Shires, A. K., Rubenstein, P. A. (1989). Nonuniform behavior of multiple isoactins in the same cell is a cell-dependent phenomenon. Cell Motility and the Cytoskeleton, 14(2), 263-70. PMID: 2611893.
Babcock, G., Rubenstein, P. A. (1989). Synthesis of mammalian profilin in Escherichia coli and its characterization. Cell Motility and the Cytoskeleton, 14(2), 230-6. PMID: 2692842.
Cook, R., Rubenstein, P. (1989). The effects of actin asp10 mutations on yeast motility. (Vols. 109). (271a) J. Cell Biol..
Solomon, T. L., Solomon, L. R., Gay, L. S. & Rubenstein, P. A. (1988). Studies on the role of actin's aspartic acid 3 and aspartic acid 11 using oligodeoxynucleotide-directed site-specific mutagenesis. The Journal of Biological Chemistry, 263(36), 19662-9. PMID: 3198644.
Wang, Y. C., Rubenstein, P. A. (1988). Epidermal growth factor controls smooth muscle alpha-isoactin expression in BC3H1 cells. The Journal of Cell Biology, 106(3), 797-803. PMID: 3279054.
Rubenstein, P. A., Solomon, L. R. & Martin, D. J. (1988). Specificity of the actin amino terminal processing protease. R. A. Bradshaw , L. McAlister-Henn & M. G. Douglas (Eds.) pp. 99-104. in Molecular Bology of Intracellular Protein Sorting and Organelle Assembly., Alan R. Liss, Inc. (New York).
Babcock, G., Rubenstein, P. (1988). Bacterial synthesis of mouse spleen profiling and its characterization. (Vols. 2). (A1538) FASEB J..
Solomon, L. R., Rubenstein, P. A. (1987). Studies on the role of actin's N tau-methylhistidine using oligodeoxynucleotide-directed site-specific mutagenesis. The Journal of Biological Chemistry, 262(23), 11382-8. PMID: 3301854.
Martin, D. J., Rubenstein, P. A. (1987). Alternate pathways for removal of the class II actin initiator methionine. The Journal of Biological Chemistry, 262(13), 6350-6. PMID: 3571262.
Rubenstein, P. A., Redman, K. L., Solomon, L. R. & Martin, D. J. (1987). Amino-terminal processing of Dictyostelium discoideum actin. pp. 231-43. Methods in Cell Biology. PMID: 3600408.
Solomon, L., Rubenstein, P. (1987). Studies on the role of actin's aspartic acid 11 using oligodeoxynucleotide directed site specific mutagenesis. (Vols. 25a). J. Cell Biol..
Miller, T., Rubenstein, P. (1987). Studies on the role of actin's aspartic acid 3 residue using oligodeoxynucleotide site directed mutgenesis. (Vols. 105). (24a) J. Cell Biol..
Shires, A., Rubenstein, P. (1987). Nonuniform behavior of isoactins in differentiated BC3H1 cells. (Vols. 105). (25a) J. Cell Biol..
Rubenstein, P. A., Redman, K. L. & Solomon, L. R. (1986). Amino terminal processing of actin. Microbiology.
Strauch, A. R., Offord, J. D., Chalkley, R. & Rubenstein, P. A. (1986). Characterization of actin mRNA levels during BC3H1 cell differentiation. The Journal of Biological Chemistry, 261(2), 849-55. PMID: 3941103.
Solomon, L., Rubenstein, P. (1986). In Vitro mutagenesis of human skeletal muscle actin: Methylhistidine 73 is not required for amino terminal post-translational processing or polymerization in Vivo. (Vols. 45). (1491) Fed. Proc..
Wang, Y., Gordon, E. & Rubenstein, P. (1986). EGF and PDGF effects on the differentiation of BC3 cells. (Vols. 103). (121a) J. Cell Biol..
Redman, K. L., Martin, D. J., Korn, E. D. & Rubenstein, P. A. (1985). Lack of NH2-terminal processing of actin from Acanthamoeba castellanii. The Journal of Biological Chemistry, 260(27), 14857-61. PMID: 4055803.
Solomon, L. R., Rubenstein, P. A. (1985). Correct NH2-terminal processing of cardiac muscle alpha-isoactin (class II) in a nonmuscle mouse cell. The Journal of Biological Chemistry, 260(12), 7659-64. PMID: 3997892.
Khurana, G., Bocuzzi, L., Stoll, L., Spector, A. & Rubenstein, P. (1985). Developmental regulation of prostaglandin synthesis in BC3H1 smooth muscle cells. (Vols. 44). (488) Fed. Proc..
Martin, D., Rubenstein, P. (1985). Alternate pathways for removal of the class II actin initiator methionine. (Vols. 101). (1060a) J. Cell Biol..
Strauch, A. R., Rubenstein, P. A. (1984). A vascular smooth muscle alpha-isoactin biosynthetic intermediate in BC3H1 cells. Identification of acetylcysteine at the NH2 terminus. The Journal of Biological Chemistry, 259(11), 7224-9. PMID: 6725286.
Moore, S. A., Strauch, A. R., Yoder, E. J., Rubenstein, P. A. & Hart, M. N. (1984). Cerebral microvascular smooth muscle in tissue culture. In Vitro, 20(6), 512-20. PMID: 6235174.
Strauch, A. R., Rubenstein, P. A. (1984). Induction of vascular smooth muscle alpha-isoactin expression in BC3H1 cells. The Journal of Biological Chemistry, 259(5), 3152-9. PMID: 6699010.
Redman, K. L., Rubenstein, P. A. (1984). Actin amino-terminal acetylation and processing in a rabbit reticulocyte lysate. pp. 179-92. Methods in Enzymology. PMID: 6493055.
Solomon, L., Rubenstein, P. (1984). Correct processing of cardiac muscle actin by a nonmuscle cell. (Vols. 43). (1850) Fed. Proc..
Strauch, A., Offord, J., Chalkley, R. & Rubenstein, P. (1984). Characterization of steady state actin mRNA levels during BC3H1 cell differentiation. (Vols. 99). (440a) J. Cell Biol..
Strauch, A., Lessard, J. & Rubenstein, P. (1984). Utilization of smooth muscle a-Isoactin in differentiated BC3H1 cells. (Vols. 99). (199a) J. Cell Biol..
Redman, K., Korn, E. & Rubenstein, P. (1984). Acanthamoeba actin is not a substrate for amino terminal processing. (Vols. 99). (30a) J. Cell Biol..
Cass, K. A., Clark, E. B. & Rubenstein, P. A. (1983). Is the onset of actin histidine methylation under development control in the chick embryo. Archives of Biochemistry and Biophysics, 225(2), 731-9. PMID: 6625608.
Rubenstein, P. A., Martin, D. J. (1983). NH2-terminal processing of Drosophila melanogaster actin. Sequential removal of two amino acids. The Journal of Biological Chemistry, 258(18), 11354-60. PMID: 6411730.
Rubenstein, P. A., Martin, D. J. (1983). NH2-terminal processing of actin in mouse L-cells in vivo. The Journal of Biological Chemistry, 258(6), 3961-6. PMID: 6833238.
Rubenstein, P. A. (1983). Applications of polyacrylamide gel electrofocusing and electrophoresis to contractile and cytoskeletal protein research. Z. Deyl. (Eds.) pp. 172-6. Electrophoresis, Elsevier Pub. (Amsterdam).
Ionasescu, V., Searby, C., Rubenstein, P., Sandra, A., Cancilla, P. & Robillard, J. (1983). Giant Axonal Neuropathy: Normal Protein Composition of Neurofilaments. J. Neurol., Neurosurg., and Psych, 46, 551-554.
Rubenstein, P., Martin, D. (1983). NH2-terminal processing of drosophila actin. (Vols. 42). (2217) Fed. Proc..
Strauch, A., Rubenstein, P. (1983). Induction of vascular smooth muscle a-isoactin expression in differentiated BC3H1 cells. (Vols. 46a). J. Cell Biol..
Rubenstein, P. A., Ruppert, T. & Sandra, A. (1982). Selective isoactin release from cultured embryonic quail breast muscle cells. The Journal of Biological Chemistry, 92, 164-9.
Rubenstein, P., Martin, D. (1982). NH2-terminal actin processing In Vivo goes through a 43,000 M.W. polypeptide intermediate with an amino terminal acetyl methionine. (Vols. 14). (1421) Fed. Proc..
Strauch, A., Rubenstein, P. (1982). Expression of a variant form of y-non-muscle actin by a transformed smooth muscle cell line. (Vols. 95). (280a) J. Cell Biol..
Redman, K., Rubenstein, P. A. (1981). NH2-terminal processing of Dictyostelium discoideum actin in vitro. The Journal of Biological Chemistry, 256(24), 13226-9. PMID: 7309760.
Rubenstein, P. A. (1981). Differential behavior of gizzard isoactins. Archives of Biochemistry and Biophysics, 210(2), 598-608. PMID: 7305348.
Ionasescu, V., Braga, S., Kaeding, L., Rubenstein, P. A., Kalnitsky, G. & Chatterjee, R. (1981). Muscle ribosome detachment factor - A role in the pathogenesis of Duchenne muscular dystrophy?. Acta Neurology Scand?, 64, 108-21.
Rubenstein, P. A., Deuchler, J., Redman, K. & Smith, P. (1981). NH2-Therminal acetylation of D. discoideum actin in a cell-free protein synthesizing system. The Journal of Biological Chemistry, 256, 8149-8155.
Redman, K., Smith, P. & Rubenstein, P. (1981). Amino terminal processing of D. discoideum Actin In Vitro. (Vols. 40). (1741) Fed. Proc..
Sandra, A., Ruppert, T. & Rubenstein, P. (1981). Selective release of actin isomers during muscle development In Vitro. (Vols. 91). (356a) J. Cell Biol..
Rubenstein, P. A., Dryer, R. (1980). S-Acetonyl-CoA: A nonreactive analog of acetyl-CoA. The Journal of Biological Chemistry, 255, 7858-62.
Rubenstein, P., Deuchler, J. (1980). Acetylation of actin In Vitro. (Vols. 39). (1660) Fed. Proc..
Sheff, D., Rubenstein, P. (1980). Specificity of the actin N-acetyl aminopeptidase. (Vols. 111). (31a) J. Cell Biol..
Rubenstein, P. A., Ivarie, R. D. (1979). Isolation of two different molecular weight polypeptides copurifying with rat liver tyrosine aminotransferase. Archives of Biochemistry and Biophysics, 194(1), 299-311. PMID: 36036.
Rubenstein, P. A., Deuchler, J. (1979). Acetylated and nonacetylated actins in Dictyostelium discoideum. The Journal of Biological Chemistry, 254, 11142-47.
Rubenstein, P. A., Sealy, L., Marshall, S. & Chalkley, R. (1979). Cellular protein synthesis and inhibition of cell division appear to be independent of butyrate induced histone hyperacetylation. Nature, 280, 692-693.
Ionasescu, V., Stern, L., Ionasescu, R. & Rubenstein, P. A. (1979). Stimulatory effects of drugs for protein synthesis on muscle cell cultures in Duchenne dystrophy. Annals of Neurology, 5, 107-111.
Levinson, W., Oppermann, H., Rubenstein, P. A. & Jackson, J. (1978). Host range restriction of vesicular stomatitis virus on duck embryo cells. Journal of Virology, 85, 612-7.
Rubenstein, P., Ionasescu, R. & Ionasescu, V. (1978). Two dimensional gel analysis of cultured normal and dystrophic chick muscle cells. Montreal, Canada: IVth International Congress on Neuromuscular Diseases.
Rubenstein, P., Ionesescu, R. & Ionesescu, V. (1978). Specific differences in the proteins synthesized by cultured chick normal and dystrophic cells. Atlanta, Georgia: American Society Biol. Chemists.
Rubenstein, P. A., Spudich, J. A. (1977). Actin microheterogeneity in chick embryo fibroblasts. Proceedings of the National Academy of Sciences of the United States of America, 74(1), 120-3. PMID: 264664.
Spudich, J. A., Mockrin, S. C., Brown, S. S., Rubenstein, P. A. & Levinson, W. (1977). The organization and interaction of actin and myosin in nonmuscle cells. pp. 545-58. Progress in Clinical and Biological Research. PMID: 144920.
Rubenstein, P. A., Strominger, J. L. (1974). Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. 8. Mechanistic roles of enzyme E-1 and pyridoxamine 5'-phosphate in the formation of cytidine diphosphate-4-keto-3,6-dideoxy-D-glucose from cytidine diphosphate-4-keto-6-deoxy-D-glucose. The Journal of Biological Chemistry, 249(12), 3776-81. PMID: 4152100.
Rubenstein, P. A., Strominger, J. L. (1974). Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. 8. Studies of the properties of E3 and its role in the formation of cytidine diphosphate-4-keto-3,6-dideoxyglucose. The Journal of Biological Chemistry, 249(12), 3782-88. PMID: 4151947.
Rubenstein, P. A., Strominger, J. L. (1974). Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexosis. IX. Purification and properties of the cytidine diphosphate-D-glucose pyrophosphorylase from Pasteurella pseudotuberculosis. type V. The Journal of Biological Chemistry, 249(12), 3789-96. PMID: 4833746.
Wickus, G. G., Rubenstein, P. A., Warth, A. D. & Strominger, J. L. (1973). Partial purification and some properties of the uridine diphospho-N-acetylglucosamine-enolpyruvate reductase from Staphylococcus epidermidis. Journal of Bacteriology, 113(1), 291-4. PMID: 4143897.
Stevens, C. L., Schultze, K. W., Smith, D. J., Pillai, P. M., Rubenstein, P. A. & Strominger, J. L. (1973). Synthesis of 3,6-dideoxy-D-erythro-hexos-4-ulose and identification as the 3,6-dideoxy-4-ketohexose from Pasteurella pseudotuberculosis. Journal of American Chemical Society, 95, 5767-68.
Rubenstein, P. (1973). Biosynthesis of the UDP-3,6-Dideoxyhexoses. Harvard University.
Streitwieser A,, J. R., Hollyhead, W. B., Pudjaatmaka, A. H., Owens, P. H., Kruger, T. L., Rubenstein, P. A., MacQuarrie, R. A., Brokaw, M. L., Chu, W. & Niemeyer, H. M. (1971). The Bronsted correlation and hydrogen isotope exchange kinetics of fluorenes, benzfluorenes, and indene with methanolic sodium methoxide. Journal of American Chemical Society, 93, 5088-96.
Gibian, M. J., Rubenstein, P. A. & Ficklin, W. H. (1969). The formation and activities of substituted phenacylchymotrypsins. Biochimica et Biophysica Acta, 191(3), 677-85. PMID: 5363989.

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