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Home , Gene silencing

CURRICULUM VITAE

Andrey L. Karamyshev

Assistant Professor

Department of Cell Biology and Biochemistry Texas Tech University Health Sciences Center 3601 4th Street, Mail Stop 6540 Lubbock, TX 79430

Phone: (806) 743-4102 Fax: (806) 743-2990 e-mail: [email protected]

EDUCATION:

Postdoctoral Studies: Department of Tumor Biology, Institute of Medical Science, University of Tokyo, Tokyo, Japan (Advisor: Dr. Yoshikazu Nakamura). Department of Medical Biochemistry and Genetics, College of Medicine, Texas A&M University, College Station, TX (Advisor: Dr. Arthur E. Johnson). Ph.D. in Biochemistry, Russian Academy of Sciences, Pushchino, Moscow Region, Russia. M.S., Biology, Kuban State University, Krasnodar, Russia.

FIELDS OF SPECIALIZATION: Biochemistry, Molecular and Cellular Biology.

RESEARCH INTERESTS Molecular mechanisms of human diseases. Post-transcriptional regulation of expression. Gene silencing and translational repression. mRNA and quality control. RNA stability and degradation. siRNAs/miRNAs. Prolactin, CFTR, secretory and membrane . Protein , folding and transport. Protein-protein interactions.

SCIENTIFIC PUBLICATIONS (see list below) 31 publications (total), including 25 full-length peer-reviewed papers in scientific journals, 5 articles in the Encyclopedia of Molecular Biology (Publisher: John Wiley & Sons, Inc., N.Y.), and chapter in a book.

PRESENTATIONS (90 total, see lists below) Results were presented at various international and national meetings, conferences and symposia (58 presentations), as well as during invited or selected talks (32 talks) at different universities and meetings around the world.

Andrey L. Karamyshev, Ph.D.

RESEARCH EXPERIENCE AND POSITIONS

2016-present Assistant Professor (Tenure track), Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX. 2009-2016 Assistant Professor (Research track), Department of Physiology, UT Southwestern Medical Center at Dallas, Dallas, TX. 2006-2009 Senior Research Scientist, Department of Physiology, UT Southwestern Medical Center at Dallas, Dallas, TX. 2002-2006 Assistant Research Scientist, Department of Medical Biochemistry and Genetics, College of Medicine, Texas A&M University System Health Sciences Center, College Station, TX. 2000-2002 Postdoctoral Research Associate, Department of Medical Biochemistry and Genetics, College of Medicine, Texas A&M University System Health Sciences Center, College Station, TX. Advisor: Professor Arthur E. Johnson, Ph.D. 1996-1999 Postdoctoral Fellow: Japan Society for the Promotion of Science (JSPS) Postdoctoral Fellow (1996-1998), then IMSUT Postdoctoral Fellow (1998-1999), Department of Tumor Biology, Institute of Medical Science, University of Tokyo, Tokyo, Japan. Advisor: Professor Yoshikazu Nakamura, Ph.D.

HONORS, AWARDS AND FELLOWSHIPS: • 2015 Alzheimer’s Disease Research Award. UT Southwestern Medical Center and The Friends of the Alzheimer’s Disease Center. • 2014 Featured in Nature Reviews Genetics: Research highlights: Novel mRNA quality control mechanism, vol. 15 (3), p. 144. • 2014 Featured in Trends in Biochemical Sciences: Popp, M. W.-L. and Maquat L. E. Defective secretory-protein mRNAs take the RAPP, vol. 39, No. 4, p. 154-156. • Selected speaker at the Gordon Research Conference on Translation Machinery in Health & Disease (2015), the Gordon Research Conference on Protein Transport Across Cell Membranes (2014), 26th North American Conference (2012), FASEB Scientific Research Conference (2012), 21st Res. Symposium Mol. Biophys. Graduate Program, UTSW Medical Center (2012), 20th Texas Protein Folders Meeting (2012), 19th Texas Protein Folders Meeting (2011), European Cystic Fibrosis Society Conference, Portugal (2008), 16th Texas Protein Folders Meeting (2008), 21st North American Cystic Fibrosis Conference (2007), MBTP Retreat (2005), Center for Advanced Biomolecular Research (CABR) Retreat (2003). • Selected speaker of the Department of Physiology Junior Scientist Seminar series (selection on the base of significance of work and excellent achievement) (2014). • Award for Best Poster at the 2008 European Cystic Fibrosis Society Conference: New Frontiers in Basic Science of Cystic Fibrosis, Regua, Douro, Portugal (2008). • Japan Society for the Promotion of Science (JSPS) Postdoctoral Fellowship (1996-1998). • International Science Foundation (ISF) Fellowship for participation in the Cold Spring Harbor Meeting Molecular genetics of and phages, USA (1995). • NATO travel and living grant for participation in summer school Molecular dynamics of biomembranes, Cargese (Corse), France, (1995). • State Scientific Research Grant for Young Scientists of Russia (1993). • G. K. Skryabin Premium in Molecular Biology, Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences (1992).

2 Andrey L. Karamyshev, Ph.D.

SUMMARY OF RESEARCH ACCOMPLISHMENTS

My major accomplishment is a discovery of a novel pathway of and protein quality control in which specific mRNA degradation preemptively regulates aberrant protein production (RAPP) (Karamyshev et al., 2014, Cell) [3, see references in my list of publications]1; the paper was highlighted in Nature Rev. Genet., in TIBS, and recommended by Faculty of 1000. Data indicate that RAPP is a general regulatory mechanisms controlling at the . This pathway monitors the status of nascent chains interactions during translation and transfers the signal to mRNA degradation machinery to prevent synthesis of proteins that lost these natural interactions. The data demonstrate that many human diseases may be a result of deregulation of RAPP. I also developed a new methodology for identification of proteins interacting with nascent chains, iPINCH, that is a powerful tool for identification of transient, short-lived interactions during translation. Recently I conducted detail analysis of interaction of SRP with altered signal sequences and deciphered the code for directing proteins for translocation across ER membrane (J. Mol. Biol., 2016) [2]. I am a co-corresponding author on the Cell paper, and corresponding author of the J. Mol. Biol. paper. We also discovered that a cystic fibrosis causing mutation in CFTR changes its interaction partners during translation, that influences mutant protein expression [1]. During my work in Arthur E. Johnson lab I discovered targeting function of SecA protein and proposed mechanism for protein sorting in bacteria [6, the paper has been recommended by Faculty of 1000]. I also conducted mapping the interactions of the STT3 subunit of the oligosaccharyl transferase complex with nascent chains in [5]. I was awarded JSPS (Japan Society for the Promotion of Science) Postdoctoral Fellowship for Foreign Researchers and worked in Japan in Dr. Yoshikazu Nakamura laboratory at the Department of Tumor Biology, Institute of Medical Science, University of Tokyo for three years. I was involved in the projects that were focused on the elucidation of molecular mechanisms of translation termination, reinitiation, and frameshifting [7-11, 17]. We found that reinitiation of protein synthesis is quantitatively regulated by the distance between stop and initiation codons [7]. As a major result of my work at the University of Tokyo a new release factor gene from Tetrahymena was cloned and studied [11, 17]. It was the first release factor cloned from ciliates. It was the first release factor with naturally restricted specificity, and it can recognize only one stop codon (UGA). In contrast to the most other organisms, Tetrahymena uses only one stop codon UGA and the other two codons, UAA and UAG, are decoded as glutamine codons. We have found that Tetrahymena release factor has unique alterations in its structure and proposed that its decoding specificity resides in the domain 1 of the protein. Later we showed that interactions within domain 1 modulate the decoding specificity of Tetrahymena release factor [9]. During my graduate school I was studying molecular mechanisms of protein and processing in bacteria. I developed amber-suppressor mutagenesis approach (as an alternative to classical site-directed mutagenesis) to elucidate role of specific amino acid residues in protein secretion and processing [19, 21]. The approach is based on amber-stop codon suppression in the cells expressing a gene of interest containing amber-stop mutation and an appropriate amber-suppressor tRNA. In addition to bacterial amber-suppressors we generated a set of phage T5 amber-suppressors [20]. I discovered that N-terminus of signal sequence of a secretory protein provides translocation efficiency [18, 21, 24, 26], while C- terminal part is important for signal sequence cleavage by a leader peptidase [19, 22, 26]. We also showed that alkaline phosphatase is secreted outside of the cells by a secretory vesicles mechanism [23, 26, 30- 31].

1 All reference numbers correspond to those in the List of Publications 3 Andrey L. Karamyshev, Ph.D.

INVITED AND SELECTED SEMINARS AND TALKS • Protein Quality Control During Translation in Health and Disease. Institute of Metabolic Disease, Baylor Research Institute. Dallas, TX, USA, June 20, 2016. Invited talk. Host: Dr. Jinsong Shen. • RAPP is a Pathway for Specific Degradation of mRNAs Encoding Aberrant Proteins. RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, MA, USA, February 2, 2016. Invited talk. Host: Dr. . • Modulation of Proteins Associated with Alzheimer’s Disease by a Novel Pathway of Translational Regulation. Presentation at the Friends of the Alzheimer’s Disease Center Reception and Tour. UT Southwestern Medical Center at Dallas, Dallas, TX, USA, November 12, 2015. • Molecular Mechanism of Regulation of Aberrant Protein Production (RAPP) and Human Diseases. Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, USA, August 18, 2015. • Lost in Translation: Regulation of Aberrant Protein Production (RAPP) in Health and Disease. Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, USA, June 23, 2015. • Lost in Translation: mRNA and Protein Quality Control in Health and Disease. Department of Biological Sciences, Dedman College of Humanities and Sciences, Southern Methodist University (SMU), Dallas, TX, USA. Host: Dr. Steven B. Vik. Invited talk, April 17, 2015. • How to Train Your Protein: Translational Silencing by Specific mRNA Degradation in Health and Disease. Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA. Host: Dr. V. Panin. Invited talk, April 15, 2015. • Lost in Translation: Regulation of Aberrant Protein Production (RAPP) in Health and Disease. Gordon Research Conference on Translation Machinery in Health & Disease: Protein Synthesis and Beyond. Ventura, CA, USA (February 22-27, 2015). Selected talk. • Adventures in Science with Art. Arthur E. Johnson Symposia, Embassy Suites (Philadelphia Airport), Philadelphia, PA, USA, December 6, 2014. • Lost in Translation: Aberrant Protein Expression Silencing by Specific mRNA Degradation. Junior Scientist Seminar series of the Department of Physiology, UT Southwestern Medical Center at Dallas, Dallas, TX, USA (May 12, 2014). Host: Dr. Jiang Wu. Selected talk. • Defects in SRP-Nascent Chain Interaction Induce mRNA Degradation Pathway. Center for Biomembrane research, Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, Stockholm, Sweden. (April 3, 2014). Host Dr. IngMarie Nilsson. Invited talk. • Preemptive Protein/mRNA Quality Control on the Ribosome: Defects in SRP – Nascent Chain Interactions Induce Specific mRNA Degradation. Gordon Research Conference on Protein Transport Across Cell Membranes, Galveston, Texas, USA (March 10, 2014). Selected talk. • Quality Control of CFTR Nascent Chains During Translation. Cystic Fibrosis translational research meeting, UT Southwestern Medical Center at Dallas, Dallas, TX, USA (2013). • CFTR: Early, Cotranslational Quality Control. The 26th Annual North American Cystic Fibrosis Conference, Orange County Convention Center, Orlando, Florida, USA (2012). Selected talk. • Gene Silencing Induced by Synthesis of Aberrant Proteins. FASEB Scientific Research Conference Protein Folding in the Cell, Saxtons River, VT, USA (2012). Selected talk. • Novel Mechanism of Protein Quality Control: mRNA Degradation Triggered by Aberrant Protein Translation, University of Ljubljana, Ljubljana, Slovenia (2012). Invited talk. Host Dr. Klementina Fon Tacer. • Silencing of Aberrant Protein Expression by Specific, Translation-Dependent mRNA Degradation. 21st Annual Research Symposium Molecular Biophysics Graduate Program, UT Southwestern 4 Andrey L. Karamyshev, Ph.D.

Medical Center, Dallas Arboretum and Botanical Garden Rosine Hall, Dallas, TX, USA (2012). Selected talk. • Cotranslational protein quality control. The 20th Annual Texas Protein Folders Meeting, Camp Allen, Navasota, TX, USA (2012). Selected talk. • Nascent chain-induced gene silencing: Specific mRNA degradation of defective proteins. Department of Molecular Biology, Keio University School of Medicine, Tokyo, Japan (2012). Invited talk. Host Dr. Mikiko Siomi. • Novel Protein Quality Control of CFTR Nascent Chains During Translation. Department of Molecular Biology, Jikei University School of Medicine, Tokyo, Japan (2012). Invited talk. Host Dr. Senya Matsufuji. • Translation-induced gene silencing: The fate of a translated nascent chain and its mRNA template. Jikei University School of Medicine, Tokyo, Japan (2012). Invited talk. Host Dr. Senya Matsufuji. • Cotranslational protein quality control. Furano conference on Advanced bioregulation and RNA, Furano Hotel, Asahikawa City, Hokkaido, Japan (2012). Invited talk. • Identification of novel quality control systems utilizing mutant CFTRs. The 19th Annual Texas Protein Folders Meeting, Camp Allen, Navasota, TX, USA (2011). Selected talk. • The First Steps in CFTR Biogenesis: Cotranslational Interactions with Nascent CFTR as It Exits the Ribosome. 2008 ECFS Conference - New Frontiers in Basic Science of Cystic Fibrosis, Regua, Douro, Portugal (2008). Selected talk. • CFTR First Steps: Cotranslational Interactions of New Synthesized Nascent Chain. Instituto Nacional de Saude, University of Lisbon, Portugal, Host: Margarida D. Amaral (2008). Invited talk. • CFTR Interactions in the Process of its Biogenesis. The 16th Annual Texas Protein Folders Meeting, Camp Allen, Navasota, TX, USA (2008). Selected talk. • Interactions with Nascent CFTR as it Exits the Ribosome. The 21st Annual North American Cystic Fibrosis Conference, Anaheim Convention Center, Anaheim, California, USA (2007). Selected talk. • Nascent Chain Interactions at the Ribosome Exit Site: The Fate of a Newly Synthesized Protein. UT Southwestern Medical Center at Dallas Dallas, TX, USA. Host: Dr. Philip J. Thomas (2006). Invited talk. • Nascent Chain Interactions at the Ribosome Exit Site. MBTP Retreat at Camp Allen, TX, USA (2005). Selected talk. • A new role for SecA: Targeting of secretory proteins to the bacterial translocon. The Center for Advanced Biomolecular Research (CABR) Retreat at Camp Allen, TX, USA (2003). Selected talk. • Investigation of the Role of Signal Peptide Primary Structure in Alkaline Phosphatase Secretion. Institute for Research, Kyoto University, Kyoto, Japan (1999). Invited talk. Host: Dr. Koreaki Ito. • Polypeptide Release Factor eRF1 from Tetrahymena thermophila: cDNA Cloning, Purification and Complex Formation with Yeast eRF3. Institute for Virus Research, Kyoto University, Kyoto, Japan (1999). Invited talk. Host: Dr. Koreaki Ito.

JOURNAL REVIEWER AND OTHER ACTIVITIES

Biochemical Journal Biochimie to Cells

Moderator (Selected by organizers): Roundtable: Protein interactions during CFTR biogenesis. The 26th Annual North American Cystic Fibrosis Conference, Orange County Convention Center, Orlando, Florida, USA. (2012). 5 Andrey L. Karamyshev, Ph.D.

PERSONAL LAB EXPERIENCE: Biochemistry: Site-directed incorporation of modified (fluorescent or photoreactive) amino acids into a protein by translation using chemically-modified aa-tRNA, tRNA purification, fluorescence spectroscopy, FRET, site-specific photo-crosslinking, protein purification and analysis, liquid chromatography (low pressure chromatography and FPLC-Akta), SDS polyacrylamide gel electrophoresis, non-denaturing electrophoresis, pulse-chase analysis of protein processing, alkaline phosphatase assays, in vitro, translation in vitro (both, pro- and eukaryotic), purification of bacterial membrane vesicles and mammalian ER microsomes, translocation of proteins into mammalian microsomes and bacterial membrane vesicles, chemical crosslinking. Molecular Biology and Recombinant DNA technology: RNAi, miRNA assay, Gene cloning, DNA sequencing, -directed mutagenesis, amber-suppressor mutagenesis, real-time PCR (qPCR), PCR, 5’ and 3’ RACE (Rapid Amplification of cDNA Ends), gene library screening, Southern and Northern blottings, preparation of plasmid and bacteriophage DNA, isolation of RNA and genomic DNA, preparation of radiolabeled DNA and , ECL labelling and detection, transformation of E. coli and yeast, agarose and polyacrylamide gel electrophoresis. Gene expression: expression of cloned genes in E. coli, yeast and mammalian . Immunology methods: antibody preparation and purification, immunoprecipitation, Western blotting. Cell Biology: Mammalian cell culture handling, stem cells, transfection, immunofluorescence.

TEACHING

During my career I was working in multicultural environment and mentored students and researchers from different countries (USA, New Zealand, Turkey, Sweden, India, Russia), so I have ability to work with and instruct culturally diverse students and researchers. I have experience in the lecture presentations, as well as laboratory practice and in mentoring undergraduate, Ph.D. and M.D. students in their projects. In addition to training student and researchers affiliated with my working place, I was mentoring visitors from other colleges and universities. For example, Andrey Rybalchenko from Texas Christian University (Forth Worth, TX) was a recipient of Summer Undergraduate Research Fellowship Program (SURF), Dustin S. Griesemer from Washington University (St. Louis, MO) was a recipient of QP-SURF program, Karl Enquist was a visitor from Department of Biochemistry and Biophysics, Stockholm University (Sweden). I was directly supervising these students during their research programs. Results of many projects guided by me were incorporated in publications and presentations at multiple scientific conferences, and the participating students and researchers became coauthors. For example, trained by me three students and one researcher became coauthors of our recent paper in Cell. I also taught Theoretical and Practical Course “Sequencing of Nucleic Acids”. Currently I am teaching Gene Expression V: Translation (in the frame of Core III: Genes (GSBS 5373) at the Graduate School of Biomedical Sciences, Texas Tech University Health Sciences Center).

GENE SEQUENCES SUBMITTED TO THE DDBJ/EMBL/GENEBANK

• AB026195 Tetrahymena thermophila mRNA for eRF1. • AB029089 Oryctolagus cuniculus mRNA for eukaryotic polypeptide chain release factor 1 (eRF1). • AB035256 Oryctolagus cuniculus mRNA for eukaryotic polypeptide chain release factor 3 (eRF3). • NC_005859 Bacteriophage T5 virion, complete .

6 Andrey L. Karamyshev, Ph.D.

LIST OF PUBLICATIONS

1. Vetter,* A. J., Karamyshev,* A. L., Patrick, A. E., Hudson, H., Thomas, P. J. (2016) N-alpha- acetyltransferases and regulation of CFTR expression. PLoS ONE 11(5): e0155430. *These authors contributed equally to this work.

2. Nilsson, I., Lara, P., Hessa T., Johnson, A. E., von Heijne, G., Karamyshev,* A. L. (2015) The code for directing proteins for translocation across ER membrane: SRP cotranslationally recognizes specific features of a signal sequence. Journal of Molecular Biology, vol. 427, p.1191-1201. (* = corresponding author).

3. Karamyshev,* A. L., Patrick, A. E., Karamysheva, Z. N., Griesemer, D. S., Hudson, H., Tjon-Kon- Sang, S, Nilsson, I., Otto, H., Liu, Q., Rospert, S., von Heijne, G., Johnson, A. E., Thomas,* P. J. (2014) Inefficient SRP Interaction with a Nascent Chain Triggers a mRNA Quality Control Pathway. Cell, vol. 156, p. 146-157. (* = co-corresponding authors).

Spotlight about this paper was published in TIBS: Popp, M. W.-L. and Maquat L. E. (2014) Defective secretory-protein mRNAs take the RAPP, Trends in Biochemical Sciences, vol. 39, No. 4, p. 154-156.

Highlighted in Nature Reviews Genetics: Research highlights: Novel mRNA quality control mechanism. Nature Reviews Genetics (2014) vol. 15 (3), p. 144.

The article has been recommended by Faculty of 1000 - selected for F1000Prime (by Karin Romisch).

4. Patrick A. E., Karamyshev A. L., Millen L., Thomas P. J. (2011) Alteration of CFTR transmembrane span integration by disease-causing mutations. Molecular Biology of the Cell, vol. 22(23), p. 4461-4471.

5. Karamyshev, A. L., Kelleher, D. J., Gilmore, R., Johnson, A. E., von Heijne, G., Nilsson, I. (2005) Mapping the interaction of the STT3 subunit of the oligosaccharyl transferase complex with nascent polypeptide chains. Journal of Biological Chemistry, vol. 280, No 49, p. 40489-40493.

6. Karamyshev, A. L., Johnson, A. E. (2005) Selective SecA association with signal sequences in ribosome-bound nascent chains: A potential role for SecA in ribosome targeting to the bacterial membrane. Journal of Biological Chemistry, vol. 280, No. 45, p. 37930-37940.

The article has been recommended by Faculty of 1000 - selected for F1000Prime (by Koreaki Ito).

7. Karamyshev, A. L., Karamysheva, Z. N., Yamami, T., Ito, K., Nakamura, Y. (2004) Transient idling of posttermination ready to reinitiate protein synthesis. Biochimie, 86(12), p.933-938.

8. Karamysheva, Z. N., Karamyshev, A. L., Ito, K., Yokogawa, T., Nishikawa, K., Nakamura, Y., Matsufuji, S. (2003) Antizyme frameshifting as a functional probe of eukaryotic translational termination. Nucleic Acids Research, 31 (20), p.5949-5956.

The article has been recommended by Faculty of 1000 - selected for F1000Prime (by Eric Westhof).

9. Ito, K., Frolova, L., Seit-Nebi, A., Karamyshev, A., Kisselev, L., Nakamura, Y. (2002) Omnipotent decoding potential resides in termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within domain 1. Proceedings of the National Academy of Sciences of the USA, 99(13), p. 8494-8499.

10. Kervestin, S., Garnier, O. A., Karamyshev, A. L., Ito, K., Nakamura, Y., Meyer, E., Jean-Jean, O. (2002) Isolation and expression of two genes encoding eukaryotic release factor 1 from Paramecium tetraurelia. Journal of Eukaryotic Microbiology, 49 (5), p. 374-382. 7 Andrey L. Karamyshev, Ph.D.

11. Karamyshev, A. L., Ito, K., Nakamura, Y. (1999) Polypeptide release factor eRF1 from Tetrahymena thermophila: cDNA cloning, purification and complex formation with yeast eRF3. FEBS Letters, 457(3), p. 483-488.

12. Nakamura, Y., Karamyshev, A. (1999) fMet (N-formyl methionine). In: Encyclopedia of Molecular Biology (Creighton T.E. ed.), John Wiley & Sons, Inc., N.Y., p. 931-932.

13. Nakamura, Y., Karamyshev, A. (1999) Pre-protein, Pre-pro-protein. In: Encyclopedia of Molecular Biology (Creighton T.E. ed.), John Wiley & Sons, Inc., N.Y., 1946-1947.

14. Nakamura, Y., Karamyshev, A. (1999) Pro-protein. In: Encyclopedia of Molecular Biology (Creighton T.E. ed.), John Wiley & Sons, Inc., N.Y., p.1975.

15. Nakamura, Y., Karamyshev, A. (1999) Pro-sequence. In: Encyclopedia of Molecular Biology (Creighton T.E. ed.), John Wiley & Sons, Inc., N.Y., p.1975-1976.

16. Nakamura, Y., Karamyshev, A. (1999) Release factor. In: Encyclopedia of Molecular Biology (Creighton T.E. ed.), John Wiley & Sons, Inc., N.Y., p.2117-2119.

17. Karamyshev, A. L., Karamysheva, Z. N., Ito, K., Matsufuji, S., Nakamura, Y. (1999) Overexpression and purification of recombinant eRF1 proteins of rabbit and Tetrahymena thermophila. Biochemistry (Moscow), v. 64(12), p. 1391-1400.

18. Kalinin, A. E., Mikhaleva, N. I., Karamyshev, A. L., Karamysheva, Z. N., Nesmeyanova, M. A. (1999) Interaction of Mutant Alkaline Phosphatase Precursors with Membrane Phospholipids in vivo and in vitro. Biochemistry (Moscow), v. 64(9), p. 1021-1029.

19. Karamyshev, A. L., Karamysheva, Z. N., Kajava, A. V., Ksenzenko, V. N., Nesmeyanova, M. A. (1998) Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region. Journal of Molecular Biology, v. 277(4), 859-870.

20. Pan’kova, N. V., Karamyshev, A. L., Shlyapnikov, M. G., Presich, A. N., and Ksenzenko, V. N. (1998) Amber Suppressor tRNAs of phage T5: Gene constructs and suppression efficiency in vivo. Molecular Biology, v. 32 (6), p. 846-853.

21. Nesmeyanova, M. A., Karamyshev, A. L., Karamysheva, Z. N., Kalinin, A. E., Ksenzenko, V. N., Kajava A. V. (1997) Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphatase provides the secretion efficiency and is involved in the interaction with anionic phospholipids. FEBS Letters, v. 403, p. 203-207.

22. Karamysheva, Z. N., Karamyshev, A. L., Ksenzenko, V. N., Shlyapnikov, M. G., Kayava, A. V., Nesmeyanova, M. A. (1997) Biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. IV. Changes in the signal peptide C-proximal domain affect processing. Molecular Biology, v. 31(5). p. 768-774.

23. Nesmeyanova, M. A., Kalinin, A. E., Karamyshev, A. L., Mikhaleva, N. I., Krupyanko, V. I. (1997) Overproduction, secretion, isolation and properties of recombinant alkaline phosphatase encoded in Escherichia coli. Process Biochemistry, v. 32 (1), p.1-7.

8 Andrey L. Karamyshev, Ph.D.

24. Karamysheva, Z. N., Karamyshev, A. L., Ksenzenko, V. N., Nesmeyanova, M. A. (1996) Effect of Lys(-20) substitutions in alkaline phosphatase signal peptide on secretion of the enzyme. Biochemistry (Moscow), v. 61 (4), 541-548.

25. Kalinin, A. E., Karamyshev, A. L., Nesmeyanova, M. A. (1996) Block of alkaline phosphatase processing due to single amino acid substitutions affects phospholipid content and turnover in E. coli cells secreting the mutant proteins. Biochemistry (Moscow), v. 61, N1, p.73-80.

26. Nesmeyanova, M., Karamyshev, A., Kalinin, A., Tsfasman, I., Badyakina, A., Khmelnitsky, M., Shlyapnikov, M., Ksenzenko, V. (1994) Escherichia coli alkaline phosphatase biogenesis: Influence of overproduction and amino acid substitutions. In: Phoshate in Microorganisms: Cellular and Molecular Biology (A.Torriani-Gorini, E.Yagil, S.Silver, Eds), American Society for Microbiology, Washington, D.C., p.264-269.

27. Karamyshev, A. L., Kalinin, A. E., Khmel'nitskii, M. I., Shlyapnikov, M. G., Ksenzenko, V. N., Nesmeyanova, M. A. (1994) Study of biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. III. Substitutions of alkaline phosphatase N-terminal amino acid affect enzyme biogenesis. Molecular Biology, v.28, No. 2, part 2, p.253- 258.

28. Karamyshev, A. L., Kalinin, A. E., Tsfasman, I. M., Ksenzenko, V. N., Nesmeyanova, M. A. (1994) Study of biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. II. Effect of amino acid substitutions in the processing site and in N terminus of mature polypeptide chain on its biogenesis. Molecular Biology, v. 28, No. 2, part 2, p.245-252.

29. Karamyshev, A. L., Shlyapnikov, M. G., Khmel'nitskii, M. I., Nesmeyanova, M. A., Ksenzenko, V. N. (1994) Biogenesis and secretion of alkaline phosphatase and its mutated forms in Escherichia coli. I. Site-directed mutations in the alkaline phosphatase gene. Molecular Biology, v.28, No. 1, part 2, p.99- 104.

30. Nesmeyanova, M. A., Karamyshev, A. L., Tsfasman, I. M., Fedotikova, E. T. (1991) Transformation of various Escherichia coli strains by multicopy plasmids with phoA gene results in secretion of periplasmic alkaline phosphatase into the medium and accumulation of its precursor. Molecular Biology, v. 25 (3), p.770-778.

31. Nesmeyanova, M. A., Tsfasman, I. M., Karamyshev, A. L., Suzina, N. E. (1991) Secretion of the overproduced periplasmic PhoA protein into the medium and accumulation of its precursor in phoA- transformed Escherichia coli strains: involvement of outer membrane vesicles. World Journal of Microbiology and Biotechnology, v. 7, p.394-406.

Manuscripts or in preparation

Enquist, K., Remenshchikov, Valeriy, Johnson, A. E., von Heijne G., Nilsson, I, Karamyshev, A. L. Mapping the influence of proline residues on the interaction of the STT3 subunit with the nascent chain. In preparation.

Karamyshev, A. L., Karamysheva, Z. N., Hudson, H., Thomas, P. J. Lost in Translation: mRNA and Protein Quality Control. Review. In preparation.

Karamyshev, A. L., Johnson, A. E., Thomas, P. J. mRNA and protein quality control of CFTR during translation in health and disease. In preparation. 9 Andrey L. Karamyshev, Ph.D.

MEETINGS, CONFERENCES, SYMPOSIA AND OTHER PRESENTATIONS

1. Pinarbasi, E., Karamyshev, A., Thomas, P. The quality control pathway RAPP disrupts GRN secretion in Frontotemporal Lobar Degeneration (FTLD). February 16, 2016. UT Southwestern Medical Center 2016 GSO Poster Presentation, Dallas, Texas, USA. 2. Gough, S. M., Karamysheva, Z., Pinarbasi, E., Thomas, P. J., Kimmo Hatanpaa, Karamyshev, A. What Causes Alzheimer's Disease and other Neurodegenerative Diseases? Examining Malfunctioning Protein Production and Quality Control Pathways. August 6, 2015. Summer Undergraduate Research Fellowship (SURF) Program, UT Southwestern Medical Center, Dallas, Texas, USA. 3. Karamyshev, A. L., Karamysheva, Z. N., Hudson, H., Pinarbasi, E., Vetter A., Wu, I-H., Johnson, A. E., Thomas, P. J. Lost in Translation: Regulation of Aberrant Protein Production (RAPP) in Health and Disease. Gordon Research Conference on Translation Machinery in Health & Disease: Protein Synthesis and Beyond. February 22-27, 2015. Four Points Sheraton / Holiday Inn Express, Ventura, CA, USA. 4. Karamyshev, A. L. Adventures in Science with Art. Arthur E. Johnson Symposia, Embassy Suites (Philadelphia Airport), Philadelphia, PA, USA, December 6, 2014. 5. Karamyshev, A. L., Karamysheva, Z. N., Patrick, A. E., Griesemer, D. S., Hudson, H., Tjon-Kon- Sang, S, Nilsson, I., Otto, H., Liu, Q., Rospert, S., von Heijne, G., Johnson, A. E., Thomas, P. J. Preemptive Protein/mRNA Quality Control on the Ribosome: Defects in SRP – Nascent Chain Interactions Induce Specific mRNA Degradation. Gordon Research Conference on Protein Transport Across Cell Membranes, March 9-14, 2014, Galveston, Texas, USA. 6. Vetter A. J., Karamyshev A. L., Thomas, P. J. A Potential Role For N-terminal Acetylation in CFTR Biogenesis. The 28th Annual North American Cystic Fibrosis Conference, Georgia World Congress Center, Atlanta, Georgia, USA. Pediatric Pulmonology, 2014, vol. 49, S38, Abstract 73, p. 241. 7. Vetter A. J., Karamyshev A. L., Thomas, P. J. NatA and Degradation of CFTR. UT Southwestern Graduate Student Poster Session, February 18, 2014: Dallas, TX. Poster Presentation. 8. Vetter A. J., Karamyshev A. L., Thomas, P. J. NatA and degradation of CFTR. Abstract of the 22nd Annual Texas Protein Folding and Function Meeting (2014), Artesian Lakes, Cleveland, TX, p. 36. 9. Vetter A. J., Karamyshev A. L., Thomas, P. J. NatA and degradation of CFTR. Midwest Conference on Protein Folding, Assembly and Molecular Motions. Notre Dame Conference Center – McKenna Hall, University of Notre Dame (May 4, 2013), Notre Dame, Indiana, USA. 10. Karamyshev A. L., Johnson A. E., Thomas P. J. CFTR: Early, Cotranslational Quality Control. The 26th Annual North American Cystic Fibrosis Conference (October 11-13, 2012), Orange County Convention Center, Orlando, Florida, USA. Pediatric Pulmonology, Supplement 35, 2012, Abstract 1, p. 223. 11. Thomas P. J., Schmidt A., Mendoza J. L., Millen L., Richardson J., Fuller M., Patrick A., Vetter A., Karamysheva Z., Karamyshev A. L. Mechanism of Action & Molecular Pathology: Matching Drugs & Mutants. The 26th Annual North American Cystic Fibrosis Conference (October 11-13, 2012), Orange County Convention Center, Orlando, Florida, USA. Pediatric Pulmonology, Supplement 35, 2012, Abstract S8.2, p. 143. 12. Karamyshev A. Gene Silencing Induced by Synthesis of Aberrant Proteins. FASEB Scientific Research Conference Protein Folding in the Cell (July 29 – August 3, 2012), Saxtons River, VT, USA. 13. Karamyshev A. Silencing of Aberrant Protein Expression by Specific, Translation-Dependent mRNA Degradation. 21st Annual Research Symposium Molecular Biophysics Graduate Program, UT Southwestern Medical Center (May 18, 2012), Dallas Arboretum and Botanical Garden, Rosine Hall, Dallas, TX. 14. Karamyshev A. L., Patrick A. E., Karamysheva Z. N., Griesemer D. S., Tjon-Kon-Sang S., Nilsson I., Otto H., Liu Q., Rospert S., von Heijne G., Johnson A. E., Thomas P. J. Cotranslational protein quality

10 Andrey L. Karamyshev, Ph.D. control. Abstract of the 20th Annual Texas Protein Folders Meeting (April 13 - 15, 2012), Camp Allen, Navasota, TX, p. 11. 15. Karamyshev A. Cotranslational protein quality control. Furano conference on Advanced bioregulation and RNA (March 4-8, 2012), Furano Hotel, Asahikawa City, Hokkaido, Japan. Invited talk. 16. Karamyshev A. L., Patrick A. E., Johnson A. E., Thomas P. J. CFTR is Synthesized in the Vicinity of SRP, NAT and 65, 70, 80, and 90 kDa Proteins. Abstract of the 19th Annual Texas Protein Folders Meeting (March 25-27, 2011), Camp Allen, Navasota, TX, p. 5. 17. Patrick A. E., Karamyshev A. L., Johnson A. E., Thomas P. J. In Vitro Translation of CFTR TMD1 and NBD1. Abstract of the 19th Annual Texas Protein Folders Meeting (March 25-27, 2011), Camp Allen, Navasota, TX, p. 6. 18. Patrick A. E., Karamyshev A. L., Johnson A. E., Thomas P. J. In vitro translation of CFTR TMD1 and NBD1. Abstract of The 24th Annual North American Cystic Fibrosis Conference, Baltimore Convention Center, Baltimore, Maryland, October 21-23, 2010. Pediatric Pulmonology, Supplement 33, 2010, Abstract 29, p. 229. 19. Patrick A. E., Karamyshev A. L., Thomas P. J. G85E and G91R Mutations Alter CFTR Transmembrane Span 1 Structure in the ER. FASEB Protein Folding in the Cell Conference, July 25-30, 2010. Saxtons River, Vermont, Abstract 61. 20. Patrick A. E., Karamyshev A. L., Thomas P. J. CF-causing mutations in the first transmembrane span of CFTR shift its positioning in the ER membrane. Abstract of the 18th Annual Texas Protein Folders Meeting (April 9-11, 2010), Camp Allen, Navasota, TX, p. 16. 21. Karamyshev A. L., Patrick A. E., Johnson A. E., Thomas P. J. Proteins that interact with CFTR during translation. Abstract of The 23rd Annual North American Cystic Fibrosis Conference, Minneapolis Convention Center, Minneapolis, Minnesota, October 15-17, 2009. Pediatric Pulmonology, Supplement 32, 2009, Abstract 55, p. 230. 22. Karamyshev A. L., Patrick A. E., Johnson A. E., Thomas P. J. Identification of Proteins Involved in Interactions with the CFTR Nascent Chain. Abstract of the 17th Annual Texas Protein Folders Meeting (April 24-26 2009), Camp Allen, Navasota, TX, p. 33. 23. Patrick A. E., Karamyshev A. L., Thomas P. J. Introduction of charge into the first transmembrane span of CFTR alters its integration profile in the ER membrane. Abstract of the 17th Annual Texas Protein Folders Meeting (April 24-26 2009), Camp Allen, Navasota, TX, p. 30. 24. Patrick A. E., Karamyshev A. L., Thomas P. J. The CF-causing mutation G85E alters the register of the first transmembrane span within the membrane. Abstract of The 22nd Annual North American Cystic Fibrosis Conference, Orlando World Center Marriott, Orlando, Florida, October 23-25, 2008. Pediatric Pulmonology, Supplement 31, 2008, Abstract 72, p. 225. 25. Patrick A. E., Karamyshev A. L., Thomas P.J. CF-causing mutations in the first transmembrane of CFTR alter its integration profile within the membrane. UT Southwestern Medical Student Training Program Retreat, September 2008: Dallas, TX. Poster Presentation. 26. Karamyshev A. L., Patrick A. E., Johnson A. E., Thomas P. J. The First Steps in CFTR Biogenesis: Cotranslational Interactions with Nascent CFTR as It Exits the Ribosome. 2008 European Cystic Fibrosis Society Conference - New Frontiers in Basic Science of Cystic Fibrosis (April 9 – 13, 2008) Regua, Douro (Portugal), p. 70. 27. Karamyshev A. L., Patrick A. E., Johnson A. E., Thomas P. J. CFTR Interactions in the Process of its Biogenesis. Abstract of the 16th Annual Texas Protein Folders Meeting (March 14-16 2008), Camp Allen, Navasota, TX, p. 16. 28. Karamyshev A. L., Patrick A. E., Johnson A. E., Thomas P. J. Interactions with Nascent CFTR as it Exits the Ribosome. Abstract of The 21st Annual North American Cystic Fibrosis Conference, Anaheim Convention Center, Anaheim, California, October 3-6, 2007. Pediatric Pulmonology, Supplement 30, 2007, Abstract 10, p. 205. 11 Andrey L. Karamyshev, Ph.D.

29. Karamyshev A., Patrick A., Johnson A., Thomas P. Interactions with CFTR During the Earliest Step(s) in Biogenesis. Abstract of The 21st Symposium of The Protein Society, Boston, Massachusetts, July 21-25, 2007. Protein Science, Vol. 16, Suppl. 1, 2007, abstract 302, p. 168. 30. Karamyshev A. L., Nilsson I., Hessa T., von Heijne G., Johnson A. E. Mapping the Interaction of Mammalian SRP with Ribosome-Bound Nascent Chains. Abstract of the 45th Annual Meeting of the American Society for Cellular Biology, San Francisco, CA, December 10-14, 2005. Molecular Biology of the Cell, Supplement, vol. 16, 2005, abstract 449, p. 124a-125a. 31. Karamyshev A. L., Johnson A. E. Protein Targeting to the Bacterial Translocon: Role of SecA and SRP. Abstract of the 44th Annual Meeting of the American Society for Cellular Biology, Washington, DC, December 4-8, 2004. Molecular Biology of the Cell, Supplement, vol. 15, 2004, abstract 1124, p. 203a. 32. Karamyshev A. L., Johnson A. E. A potential role for SecA in ribosome targeting to the bacterial membrane. Abstr. of the 43rd Annual Meeting of the American Society for Cellular Biology, San Francisco, CA, December 13-17, 2003. Molecular Biology of the Cell, Supplement, vol. 14, 2003, abstract 493, p. 89a. 33. Karamyshev A. L. A new role for SecA: Targeting of secretory proteins to the bacterial translocon. The Center for Advanced Biomolecular Research (CABR) Retreat at Camp Allen. USA. October 25-26, 2003. 34. Karamyshev A. L., Ito K., Johnson A. E. Translocation of NBD- and BODIPY-labeled proteins into Escherichia coli inverted membrane vesicles in vitro. - Meeting on Experimental Biology, New Orleans, Louisiana, USA, April 20–24, 2002, FASEB Journal, 2002, vol. 16 (5), Abstracts, Part II, abstract 886.6, p. A1192. 35. Karamysheva Z., Karamyshev A., Ito K., Nakamura Y., Matsufuji S. Translational release factors affect the efficiency of the frameshifting and readthrough at the recoding sites. - Abstr. of the 72 Meeting of the Japanese Biochemical Society, Yokohama, Japan, October 6-9, 1999, p. 1084 (abstr. 4P-637). 36. Karamyshev A., Ito K., Nakamura Y. New polypeptide release factor from Tetrahymena thermophila. - Abstr. of the conference The Ribosome: Structure, Function, and Cellular Interactions, HelsingØr Conference, Denmark, June 13th-17th, 1999, p. 48. 37. Karamyshev A., Ito K., Nakamura Y. Overexpression and purification of polypeptide release factor eRF1 of Tetrahymena thermophila. - Abstr. of the 21 Annual Meeting of Molecular Biology Society of Japan, Yokohama, Japan, December 16-19 , 1998, p. 439 (abstr. 2P-556). 38. Karamysheva Z., Karamyshev A., Ito K., Nakamura Y., Matsufuji S. cDNA cloning and overexpression of rabbit translational release factors eRF1 and eRF3. - Abstr. of the 21 Annual Meeting of Molecular Biology Society of Japan, Yokohama, Japan, December 16-19 , 1998, p. 439 (abstr. 2P-557). 39. Karamyshev A., Ito K., Nakamura Y. Cloning and characterization of the Tetrahymena thermophila gene encoding the polypeptide release factor. - Abstr. of the 20th Annual Meeting of the Molecular Biology Society of Japan, Kyoto, Japan, December 16-19, 1997, p.352 (abstr. 1-554-P-710). 40. Nesmeyanova, M. A., Karamyshev, A. L., Karamysheva, Z. N., Kalinin, A. E., Ksenzenko, V. N., Kajava, A. V. Structure-function analysis of the signal peptide of the Esherichia coli alkaline phosphatase. European Research conference Protein targeting: Protein Translocation across Cellular Membranes. Albufeira, Portugal, October 22-27, 1997. 41. Kajava A. V., Karamyshev A. L., Karamysheva Z. N., Ksenzenko V. N., Kalinin A., Nesmeyanova M. A. Effect of amino acid substitutions in the signal peptide cleavage region on the processing of E. coli alkaline phosphatase. - Abstr. of 17th International Congress of Biochemistry and Molecular Biology, San Francisco, USA, August 24-29, 1997, B-124; FASEB Journal, 1997, vol. 11 (9), Abstracts, A930, 430. 42. Nesmeianova, M.A., Badyakina, A.O., Zolov, S.N., Mikhaleva, N.I., Karamyshev A. L. and Suzina N.E. (1997) Biogenesis and secretion of alkaline phosphatase under its increased synthesis by Escherichia

12 Andrey L. Karamyshev, Ph.D. coli: possible ways of regulating the process. 2nd Congress of the Biochemical Society of the Russian Academy of Sciences. Moscow, May 19-23, p. 341-342 43. Pan’kova N., Vinokurov L., Karamyshev A., Shlyapnikov M., Ksenzenko V. Construction and characterization of the complete collection of phage T5 amber suppressors. - Abstr. of 17th International tRNA Workshop, Kazusa Akademia Center, Japan, May 10-15, 1997, p.5-4. 44. Nesmeyanova M. A., Karamyshev A. L., Karamysheva Z. N., Kalinin A. E., Suzina N. E., Kajava A. V. Role of primary structure of protein N-terminal domains and membrane anionic phospholipids in E. coli alkaline phosphatase (PhoA) secretion. - Abstr. of 1st Cell Biology Symposium of the MDC on "Protein transport and stability ", Berlin, September 26-29, 1996, p.92. 45. Kalinin A. E., Karamyshev A. L., Suzina N. E., Nesmeyanova M. A. Anchoring of E. coli alkaline phosphatase precursor in the cytoplasmic membrane leads to changes in the membrane phospholipid composition and turnover, - Abstr. of Cold Spring Harbor Meeting Molecular genetics of bacteria and phages, Cold Spring Harbor, New York, August 20-25, 1996, p.14. 46. Kalinin A. E., Karamysheva Z. N., Karamyshev A. L., Krupyanko V. I., Nesmeyanova M. A. Biogenesis and some catalytical properties of mutant alkaline phosphatases of E. coli. - Abstr. of Bayev memorial conference, Moscow, 1996, p.263. 47. Karamysheva Z. N., Karamyshev A. L., Ksenzenko V. N., Nesmeyanova M. A. Introduction of amino acid substitutions into E. coli alkaline phosphatase by amber-suppressor tRNAs and study of mutant proteins processing. - Abstr. of Bayev memorial conference, Moscow, 1996, p.264. 48. Karamyshev A. L., Karamysheva Z. N., Kalinin A. E., Ksenzenko V. N., Nesmeyanova M. A. Amber-suppressor mutagenesis of Escherichia coli alkaline phosphatase and protein processing analysis. - Abstr. of Cold Spring Harbor Meeting Molecular genetics of bacteria and phages, Cold Spring Harbor, New York, August 22-27, 1995, p.131. 49. Kalinin A. E., Karamyshev A. L., Krupyanko B. I., Nesmeyanova M. A. Site-directed mutagenesis of Escherichia coli alkaline phosphatase: analysis of secretion and function. Abstr. of Cold Spring Harbor Meeting Molecular genetics of bacteria and phages, Cold Spring Harbor, New York, August 22-27, 1995, p.127. 50. Karamysheva Z. N., Karamyshev A. L., Kalinin A. E., Ksenzenko V. N., Nesmeyanova M. A. Amino acid substitutions in the signal peptide cleavage site of Escherichia coli alkaline phosphatase: influence on processing. - Abstr. of 23rd Meeting of the Federation of European Biochemical Societies, Basel, Switzerland, August 13-18, 1995, P55.8. 51. Karamyshev A. L., Kalinin A. E., Karamysheva Z. N., Krupyanko B. I., Nesmeyanova M. A. Secretion and function of mutant alkaline phosphatases in E.coli. - Abstr. of 23rd Meeting of the Federation of European Biochemical Societies, Basel, Switzerland, August 13-18, 1995, P55.6. 52. Kalinin A. E., Karamyshev A. L., Nesmeyanova M. A. The block of E.coli alkaline phosphatase processing results in the change of membrane phospholipid turnover. In: Molecular Dynamics of Biomembranes, NATO Advanced Study Institute, FEBS Advanced Course, Cargese (Corse), France, June 19 - July 1, 1995. 53. Karamyshev A. L., Karamysheva Z. N., Kalinin A. E., Ksenzenko V. N., Nesmeyanova M. A. Effect of amino acid substitutions in the processing site of alkaline phosphatase on maturation of this protein. In: Molecular Dynamics of Biomembranes, NATO Advanced Study Institute, FEBS Advanced Course, Cargese (Corse), France, June 19 - July 1, 1995. 54. Kalinin A. E., Karamyshev A. L., Nesmeyanova M. A. The block of Escherichia coli alkaline phosphatase processing due to a single amino acid substitution result in the change of membrane phospholipid turnover. - Abstract of Symposium on lipid biochemistry, St.-Peterburg, 1994, p.40. 55. Ksenzenko V. N., Pan'kova N. V., Karamyshev A. L., Kanapin A. A., Khmelnitsky M. I., Wilkens K., Rueger W., Shlyapnikov M. G. Bacteriophage T5 transfer and their genes. - Abstract of X Russian-German Symposium Structure and function of genome, Suzdal, August 25-28, 1993. 13 Andrey L. Karamyshev, Ph.D.

56. Karamyshev A. L., Kalinin A. E., Tsfasman I. M., Khmelnitsky M. I., Shlyapnikov M. G., Ksenzenko V. N., Nesmeyanova M. A. Effect of amino acid substitutions in E.coli alkaline phosphatase on its biogenesis. - Abstract of X Russian-German Symposium Structure and function of genome, Suzdal, August 25-28, 1993. 57. Karamyshev A. L., Kalinin A. E., Tsfasman I. M., Ksenzenko V. N., Nesmeyanova M. A. Amino acid substitutions in PhoA affect its biogenesis and secretion in E.coli. - Abstr. of International symposium on cellular and molecular biology of phosphate and phosphorylated compounds in microorganisms, Woods Hole, Massachusetts, September 12-17, 1993, p.104. 58. Karamyshev A. L., Ksenzenko V. N., Nesmeyanova M.A. Mutations of alkaline phosphatase gene by site-directed mutagenesis influence the secretion of this protein.- Abstr. of Cold Spring Harbor Meeting Molecular genetics of bacteria and phages, Cold Spring Harbor, New York, August 20-25, 1991, p.62.

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