Chen, Shun-Jia; Kim, Leehyeon et al. (2021) Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway Proceedings of the National Academy of Sciences of the United States of America; Vol. 118; No. 43;

Vu, Tri T. M.; Mitchell, Dylan C. et al. (2020) The Arg/N-degron pathway targets transcription factors and regulates specific genes Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 49;

Vu, Tri T. M.; Varshavsky, Alexander (2020) The ATF3 Transcription Factor Is a Short-Lived Substrate of the Arg/N-Degron Pathway Biochemistry; Vol. 59; No. 30;

Dong, Cheng; Chen, Shun-Jia et al. (2020) Recognition of nonproline N-terminal residues by the Pro/N-degron pathway Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 25;

Oh, Jang-Hyun; Hyun, Ju-Yeon et al. (2020) Five enzymes of the Arg/N-degron pathway form a targeting complex: The concept of superchanneling Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 20;

Chen, Shun-Jia; Melnykov, Artem et al. (2020) Evolution of Substrates and Components of the Pro/N-Degron Pathway Biochemistry; Vol. 59; No. 4;

Melnykov, Artem; Chen, Shun-Jia et al. (2019) Gid10 as an alternative N-recognin of the Pro/N-degron pathway Proceedings of the National Academy of Sciences of the United States of America; Vol. 116; No. 32;

Varshavsky, Alexander (2019) On the cause of sleep: Protein fragments, the concept of sentinels, and links to epilepsy Proceedings of the National Academy of Sciences of the United States of America; Vol. 116; No. 22;

Varshavsky, Alexander (2019) N-degron and C-degron pathways of protein degradation Proceedings of the National Academy of Sciences of the United States of America; Vol. 116; No. 2;

Kim, Jeong-Mok; Seok, Ok-Hee et al. (2018) Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway Science; Vol. 362; No. 6418;

Dougan, David A.; Varshavsky, Alexander (2018) Understanding the Pro/N-end rule pathway Nature Chemical Biology; Vol. 14; No. 5;

Oh, Jang-Hyun; Chen, Shun-Jia et al. (2017) A reference-based protein degradation assay without global translation inhibitors Journal of Biological Chemistry; Vol. 292; No. 52;

Varshavsky, Alexander (2017) The Ubiquitin System, Autophagy, and Regulated Protein Degradation Annual Review of Biochemistry; Vol. 86;

Oh, Jang-Hyun; Hyun, Ju-Yeon et al. (2017) Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway Proceedings of the National Academy of Sciences of the United States of America; Vol. 114; No. 22;

Chen, Shun-Jia; Wu, Xia et al. (2017) An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes Science; Vol. 355; No. 6323;

Wadas, Brandon; Piatkov, Konstantin et al. (2016) Analyzing N-terminal Arginylation Through the Use of Peptide Arrays and Degradation Assays Journal of Biological Chemistry; Vol. 291; No. 40;

Wadas, Brandon; Borjigin, Jimo et al. (2016) Degradation of Serotonin N-Acetyltransferase, a Circadian Regulator, by the N-end Rule Pathway Journal of Biological Chemistry; Vol. 291; No. 33;

Liu, Yu-Jiao; Liu, Chao et al. (2016) Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway Journal of Biological Chemistry; Vol. 291; No. 14;

Piatkov, Konstantin; Vu, Tri et al. (2015) Formyl-methionine as a degradation signal at the N-termini of bacterial proteins Microbial Cell; Vol. 2; No. 10;

Park, Sang-Eun; Kim, Jeong-Mok et al. (2015) Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway Science; Vol. 347; No. 6227;

Brower, Christopher S.; Rosen, Connor E. et al. (2014) Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats Proceedings of the National Academy of Sciences of the United States of America; Vol. 111; No. 46;

Varshavsky, Alexander (2014) Discovery of the Biology of the Ubiquitin System JAMA : the journal of the American Medical Association; Vol. 311; No. 19;

Piatkov, Konstantin I.; Oh, Jang-Hyun et al. (2014) Calpain-generated natural protein fragments as short-lived substrates of the N-end rule pathway Proceedings of the National Academy of Sciences of the United States of America; Vol. 111; No. 9;

Kim, Heon-Ki; Kim, Ryu-Ryun et al. (2014) The N-Terminal Methionine of Cellular Proteins as a Degradation Signal Cell; Vol. 156; No. 1;

Piatkov, Konstantin; Graciet, Emmanuelle et al. (2013) Ubiquitin Reference Technique and Its Use in Ubiquitin-Lacking Prokaryotes PLoS ONE; Vol. 8; No. 6;

Shemorry, Anna; Hwang, Cheol-Sang et al. (2013) Control of Protein Quality and Stoichiometries by N-Terminal Acetylation and the N-End Rule Pathway Molecular Cell; Vol. 50; No. 4;

Brower, Christopher S.; Piatkov, Konstantin I. et al. (2013) Neurodegeneration-Associated Protein Fragments as Short-Lived Substrates of the N-End Rule Pathway Molecular Cell; Vol. 50; No. 2;

Piatkov, Konstantin I.; Colnaghi, Luca et al. (2012) The Auto-Generated Fragment of the Usp1 Deubiquitylase Is a Physiological Substrate of the N-End Rule Pathway Molecular Cell; Vol. 48; No. 6;

Varshavsky, Alexander (2012) Augmented generation of protein fragments during wakefulness as the molecular cause of sleep: A hypothesis Protein Science; Vol. 21; No. 11;

Piatkov, Konstantin I.; Brower, Christopher S. et al. (2012) The N-end rule pathway counteracts cell death by destroying proapoptotic protein fragments Proceedings of the National Academy of Sciences of the United States of America; Vol. 109; No. 27;

Varshavsky, Alexander (2012) The Ubiquitin System, an Immense Realm Annual Review of Biochemistry; Vol. 81;

Hwang, Cheol-Sang; Sukalo, Maja et al. (2011) Ubiquitin Ligases of the N-End Rule Pathway: Assessment of Mutations in UBR1 That Cause the Johanson-Blizzard Syndrome PLoS ONE; Vol. 6; No. 9;

Varshavsky, Alexander (2011) The N-end rule pathway and regulation by proteolysis Protein Science; Vol. 20; No. 8;

Hwang, Cheol-Sang; Shemorry, Anna et al. (2010) The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases Nature Cell Biology; Vol. 12; No. 12;

Brower, Christopher S.; Veiga, Lucia et al. (2010) Mouse Dfa Is a Repressor of TATA-box Promoters and Interacts with the Abt1 Activator of Basal Transcription Journal of Biological Chemistry; Vol. 285; No. 22;

Hwang, Cheol-Sang; Shemorry, Anna et al. (2010) N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals Science; Vol. 327; No. 5968;

Brower, Christopher S.; Varshavsky, Alexander (2009) Ablation of Arginylation in the Mouse N-End Rule Pathway: Loss of Fat, Higher Metabolic Rate, Damaged Spermatogenesis, and Neurological Perturbations PLoS ONE; Vol. 4; No. 11;

Graciet, Emmanuelle; Walter, Franziska et al. (2009) The N-end rule pathway controls multiple functions during Arabidopsis shoot and leaf development Proceedings of the National Academy of Sciences of the United States of America; Vol. 106; No. 32;

Wang, Haiqing; Piatkov, Konstantin I. et al. (2009) Glutamine-Specific N-Terminal Amidase, a Component of the N-End Rule Pathway Molecular Cell; Vol. 34; No. 6;

Hwang, Cheol-Sang; Shemorry, Anna et al. (2009) Two proteolytic pathways regulate DNA repair by cotargeting the Mgt1 alkylguanine transferase Proceedings of the National Academy of Sciences of the United States of America; Vol. 106; No. 7;

Varshavsky, Alexander (2008) Discovery of cellular regulation by protein degradation Journal of Biological Chemistry; Vol. 283; No. 50;

Hwang, Cheol-Sang; Varshavsky, Alexander (2008) Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway Proceedings of the National Academy of Sciences of the United States of America; Vol. 105; No. 49;

Varshavsky, Alexander (2008) The N-end rule at atomic resolution Nature Structural & Molecular Biology; Vol. 15; No. 12;

Xia, Zanxian; Turner, Glenn C. et al. (2008) Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter Journal of Biological Chemistry; Vol. 283; No. 43;

Xia, Zanxian; Webster, Ailsa et al. (2008) Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway Journal of Biological Chemistry; Vol. 283; No. 35;

Connor, Rebecca E.; Piatkov, Konstantin et al. (2008) Enzymatic N-terminal Addition of Noncanonical Amino Acids to Peptides and Proteins ChemBioChem; Vol. 9; No. 3;

Hu, Rong-Gui; Wang, Haiqing et al. (2008) The N-end rule pathway is a sensor of heme Proceedings of the National Academy of Sciences of the United States of America; Vol. 105; No. 1;

Schnupf, Pamela; Zhou, Jianmin et al. (2007) Listeriolysin O Secreted by Listeria monocytogenes into the Host Cell Cytosol Is Degraded by the N-End Rule Pathway Infection and Immunity; Vol. 75; No. 11;

Varshavsky, Alexander (2007) Targeting the absence: Homozygous DNA deletions as immutable signposts for cancer therapy Proceedings of the National Academy of Sciences of the United States of America; Vol. 104; No. 38;

Tasaki, Takafumi; Sohr, Reinhard et al. (2007) Biochemical and Genetic Studies of UBR3, a Ubiquitin Ligase with a Function in Olfactory and Other Sensory Systems Journal of Biological Chemistry; Vol. 282; No. 25;

Hu, Rong-Gui; Brower, Christopher S. et al. (2006) Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms Journal of Biological Chemistry; Vol. 281; No. 43;

An, Jee Young; Seo, Jai Wha et al. (2006) Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway Proceedings of the National Academy of Sciences of the United States of America; Vol. 103; No. 16;

Graciet, Emmanuelle; Hu, Rong-Gui et al. (2006) Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen Proceedings of the National Academy of Sciences of the United States of America; Vol. 103; No. 9;

Zenker, Martin; Varshavsky, Alexander (2005) Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome) Nature Genetics; Vol. 37; No. 12;

Hu, Rong-Gui; Sheng, Jun et al. (2005) The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators Nature; Vol. 437; No. 7061;

Tasaki, Takafumi; Mulder, Lubbertus C. F. et al. (2005) A Family of Mammalian E3 Ubiquitin Ligases That Contain the UBR Box Motif and Recognize N-Degrons Molecular and Cellular Biology; Vol. 25; No. 16;

Yin, Jinhu; Kwon, Yong Tae et al. (2004) RECQL4, mutated in the Rothmund–Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway Human Molecular Genetics; Vol. 13; No. 20;

Kwon, Yong Tae; Xia, Zanxian et al. (2003) Female Lethality and Apoptosis of Spermatocytes in Mice Lacking the UBR2 Ubiquitin Ligase of the N-End Rule Pathway Molecular and Cellular Biology; Vol. 23; No. 22;

Varshavsky, Alexander (2003) The N-end rule and regulation of apoptosis Nature Cell Biology; Vol. 5; No. 5;

Xie, Youming; Varshavsky, Alexander (2002) UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis Nature Cell Biology; Vol. 4; No. 12;

Du, Fangyong; Navarro-Garcia, Federico et al. (2002) Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain Proceedings of the National Academy of Sciences of the United States of America; Vol. 99; No. 22;

Kwon, Yong Tae; Kashina, Anna S. et al. (2002) An Essential Role of N-Terminal Arginylation in Cardiovascular Development Science; Vol. 297; No. 5578;

Kwon, Yong Tae; Xia, Zanxian et al. (2001) Construction and Analysis of Mouse Strains Lacking the Ubiquitin Ligase UBR1 (E3α) of the N-End Rule Pathway Molecular and Cellular Biology; Vol. 21; No. 23;

Rao, Hai; Uhlmann, Frank et al. (2001) Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability Nature; Vol. 410; No. 6831;

Xie, Youming; Varshavsky, Alexander (2001) RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: A negative feedback circuit Proceedings of the National Academy of Sciences of the United States of America; Vol. 98; No. 6;

Hershko, Avram; Ciechanover, Aaron et al. (2000) The ubiquitin system Nature Medicine; Vol. 6; No. 10;

Turner, Glenn C.; Varshavsky, Alexander (2000) Detecting and Measuring Cotranslational Protein Degradation in Vivo Science; Vol. 289; No. 5487;

Varshavsky, Alexander; Turner, Glenn et al. (2000) The Ubiquitin System and the N-End Rule Pathway Biological Chemistry; Vol. 381; No. 9-10;

Kwon, Yong Tae; Balogh, Seth A. et al. (2000) Altered Activity, Social Behavior, and Spatial Memory in Mice Lacking the NTAN1p Amidase and the Asparagine Branch of the N-End Rule Pathway Molecular and Cellular Biology; Vol. 20; No. 11;

Turner, Glenn C.; Du, Fangyong et al. (2000) Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway Nature; Vol. 405; No. 6786;

Davydov, Ilia V.; Varshavsky, Alexander (2000) RGS4 is arginylated and degraded by the N-end rule pathway in vitro Journal of Biological Chemistry; Vol. 275; No. 30;

Xie, Youming; Varshavsky, Alexander (2000) Physical association of ubiquitin ligases and the 26S proteasome Proceedings of the National Academy of Sciences of the United States of America; Vol. 97; No. 6;

Kwon, Yong Tae; Lévy, Frédéric et al. (1999) Bivalent Inhibitor of the N-end Rule Pathway Journal of Biological Chemistry; Vol. 274; No. 25;

Dünnwald, Martin; Varshavsky, Alexander et al. (1999) Detection of Transient In Vivo Interactions between Substrate and Transporter during Protein Translocation into the Endoplasmic Reticulum Molecular Biology of the Cell; Vol. 10; No. 2;

Kwon, Yong Tae; Kashina, Anna S. et al. (1999) Alternative Splicing Results in Differential Expression, Activity, and Localization of the Two Forms of Arginyl-tRNA-Protein Transferase, a Component of the N-End Rule Pathway Molecular and Cellular Biology; Vol. 19; No. 1;

Varshavsky, Alexander (1999) Recent studies of the ubiquitin system and the N-end rule pathway Harvey lectures; Vol. 96;

Kwon, Yong Tae; Reiss, Yuval et al. (1998) The mouse and human genes encoding the recognition component of the N-end rule pathway Proceedings of the National Academy of Sciences of the United States of America; Vol. 95; No. 14;

Varshavsky, Alexander (1998) Codominant interference, antieffectors, and multitarget drugs Proceedings of the National Academy of Sciences of the United States of America; Vol. 95; No. 5;

Ramos, Paula C.; Höckendorff, Jörg et al. (1998) Ump1p Is Required for Proper Maturation of the 20S Proteasome and Becomes Its Substrate upon Completion of the Assembly Cell; Vol. 92; No. 4;

Byrd, Christopher; Turner, Glenn C. et al. (1998) The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor EMBO Journal; Vol. 17; No. 1;

Varshavsky, Alexander (1997) The ubiquitin system Trends in Biochemical Sciences; Vol. 22; No. 10;

Varshavsky, Alexander (1997) The N-end rule pathway of protein degradation Genes to Cells; Vol. 2; No. 1;

Grigoryev, Sergei; Stewart, Albert E. et al. (1996) A Mouse Amidase Specific for N-terminal Asparagine: the gene, the enzyme, and their function in the N-end rule pathway Journal of Biological Chemistry; Vol. 271; No. 45;

Varshavsky, Alexander (1996) The N-end rule: Functions, mysteries, uses Proceedings of the National Academy of Sciences of the United States of America; Vol. 93; No. 22;

Ghislain, Michel; Dohmen, R. Jürgen et al. (1996) Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae EMBO Journal; Vol. 15; No. 18;

Lévy, Frédéric; Johnsson, Nils et al. (1996) Using ubiquitin to follow the metabolic fate of a protein Proceedings of the National Academy of Sciences of the United States of America; Vol. 93; No. 10;

Dohmen, R. Jürgen; Stappen, Reiner et al. (1995) An Essential Yeast Gene Encoding a Homolog of Ubiquitin-activating Enzyme Journal of Biological Chemistry; Vol. 270; No. 30;

Baker, Rohan T.; Varshavsky, Alexander (1995) Yeast N-terminal Amidase: a new enzyme and component of the N-end rule pathway Journal of Biological Chemistry; Vol. 270; No. 20;

Varshavsky, Alexander (1995) Codominance and toxins: A path to drugs of nearly unlimited selectivity Proceedings of the National Academy of Sciences of the United States of America; Vol. 92; No. 9;

Johnston, Jennifer A.; Johnson, Erica S. et al. (1995) Methotrexate Inhibits Proteolysis of Dihydrofolate Reductase by the N-end Rule Pathway Journal of Biological Chemistry; Vol. 270; No. 14;

Varshavsky, A. J. (1995) The N-end Rule Cold Spring Harbor Symposia on Quantitative Biology; Vol. 60;

Johnsson, Nils; Varshavsky, Alexander (1994) Split ubiquitin as a sensor of protein interactions in vivo Proceedings of the National Academy of Sciences of the United States of America; Vol. 91; No. 22;

Madura, Kiran; Varshavsky, Alexander (1994) Degradation of Gα by the N-End Rule Pathway Science; Vol. 265; No. 5177;

Johnsson, Nils; Varshavsky, Alexander (1994) Ubiquitin-assisted dissection of protein transport across membranes EMBO Journal; Vol. 13; No. 11;

Dohmen, R. Jürgen; Wu, Peipei et al. (1994) Heat-Inducible Degron: A Method for Constructing Temperature-Sensitive Mutants Science; Vol. 263; No. 5151;

Ota, Irene M.; Varshavsky, Alexander (1993) A yeast protein similar to bacterial two-component regulators Science; Vol. 262; No. 5133;

Shrader, Thomas E.; Tobias, John W. et al. (1993) The N-End Rule in Escherichia coli: Cloning and Analysis of the Leucyl, Phenylalanyl-tRNA-Protein Transferase Gene aat Journal of Bacteriology; Vol. 175; No. 14;

Madura, Kiran; Dohmen, R. Jürgen et al. (1993) N-recognin/Ubc2 interactions in the N-end rule pathway Journal of Biological Chemistry; Vol. 268; No. 16;

Baker, Rohan T.; Tobias, John W. et al. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family Journal of Biological Chemistry; Vol. 267; No. 32;

Varshavsky, Alexander (1992) The N-end rule Cell; Vol. 69; No. 5;

Ota, Irene M.; Varshavsky, Alexander (1992) A gene encoding a putative tyrosine phosphatase suppresses lethality of an N-end rule-dependent mutant Proceedings of the National Academy of Sciences of the United States of America; Vol. 89; No. 6;

Johnson, Erica S.; Bartel, Bonnie et al. (1992) Ubiquitin as a degradation signal EMBO Journal; Vol. 11; No. 2;

Tobias, John W.; Shrader, Thomas E. et al. (1991) The N-end rule in bacteria Science; Vol. 254; No. 5036;

Dohmen, R. Jürgen; Madura, Kiran et al. (1991) The N-End Rule is Mediated by the UBC2(RAD6) Ubiquitin-Conjugating Enzyme Proceedings of the National Academy of Sciences of the United States of America; Vol. 88; No. 16;

Tobias, John W.; Varshavsky, Alexander (1991) Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae Journal of Biological Chemistry; Vol. 266; No. 18;

Hochstrasser, Mark; Ellison, Michael J. et al. (1991) The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo Proceedings of the National Academy of Sciences of the United States of America; Vol. 88; No. 11;

Baker, Rohan T.; Varshavsky, Alexander (1991) Inhibition of the N-end rule pathway in living cells Proceedings of the National Academy of Sciences of the United States of America; Vol. 88; No. 4;

Varshavsky, Alexander (1991) Naming a targeting signal Cell; Vol. 64; No. 1;

McGrath, John P.; Jentsch, Stefan et al. (1991) UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme EMBO Journal; Vol. 10; No. 1;

Johnson, Erica S.; Gonda, David K. et al. (1990) Cis-trans recognition and subunit-specific degradation of short-lived proteins Nature; Vol. 346; No. 6281;

Hochstrasser, Mark; Varshavsky, Alexander (1990) In vivo degradation of a transcriptional regulator: The yeast α2 repressor Cell; Vol. 61; No. 4;

Balzi, Elisabetta; Choder, Mordechai et al. (1990) Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae Journal of Biological Chemistry; Vol. 265; No. 13;

Gonda, David K.; Bachmair, Andreas et al. (1989) Universality and Structure of the N-end Rule Journal of Biological Chemistry; Vol. 264; No. 28;

McGrath, John P.; Varshavsky, Alexander (1989) The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein Nature; Vol. 340; No. 6232;

Winter, Edward; Varshavsky, Alexander (1989) A DNA binding protein that recognizes oligo(dA)•oligo(dT) tracts EMBO Journal; Vol. 8; No. 6;

Finley, Daniel; Bartel, Bonnie et al. (1989) The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis Nature; Vol. 338; No. 6214;

Chau, Vincent; Tobias, John W. et al. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein Science; Vol. 243; No. 4898;

Bachmair, Andreas; Varshavsky, Alexander (1989) The degradation signal in a short-lived protein Cell; Vol. 56; No. 6;

Varshavsky, A.; Bachmair, A. et al. (1989) Targeting of proteins for degradation Biotechnology (Reading, Mass.); Vol. 13;

Goebl, Mark G.; Yochem, John et al. (1988) The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme Science; Vol. 241; No. 4871;

Solomon, Mark J.; Larsen, Pamela L. et al. (1988) Mapping protein-DNA interactions in vivo with formaldehyde: Evidence that histone H4 is retained on a highly transcribed gene Cell; Vol. 53; No. 6;

Bartel, Bonnie; Varshavsky, Alexander (1988) Hypersensitivity to heavy water: A new conditional phenotype Cell; Vol. 52; No. 6;

Varshavsky, Alexander; Bachmair, Andreas et al. (1987) N-end rule of selective protein turnover: mechanistic aspects and functional implications Biochemical Society Transactions; Vol. 15; No. 5;

Solomon, Mark J.; Varshavsky, Alexander (1987) A nuclease-hypersensitive region forms de novo after chromosome replication Molecular and Cellular Biology; Vol. 7; No. 10;

Peck, Lawrence J.; Millstein, Larry et al. (1987) Transcriptionally inactive oocyte-type 5S RNA genes of Xenopus laevis are complexed with TFIIIA in vitro Molecular and Cellular Biology; Vol. 7; No. 10;

Jentsch, Stefan; McGrath, John P. et al. (1987) The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme Nature; Vol. 329; No. 6135;

Özkaynak, Engin; Finley, Daniel et al. (1987) The yeast ubiquitin genes: a family of natural gene fusions EMBO Journal; Vol. 6; No. 5;

Finley, Daniel; Özkaynak, Engin et al. (1987) The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses Cell; Vol. 48; No. 6;

Snapka, Robert M.; Kwok, Kwan et al. (1986) Post-separation detection of nucleic acids and proteins by neutron activation Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 23;

Bachmair, Andreas; Finley, Daniel et al. (1986) In vivo half-life of a protein is a function of its amino-terminal residue Science; Vol. 234; No. 4773;

Swerdlow, Paul S.; Finley, Daniel et al. (1986) Enhancement of immunoblot sensitivity by heating of hydrated filters Analytical Biochemistry; Vol. 156; No. 1;

Solomon, Mark J.; Strauss, Francois et al. (1986) A mammalian high mobility group protein recognizes any stretch of six A·T base pairs in duplex DNA Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 5;

Gros, Philippe; Croop, James et al. (1986) Isolation and characterization of DNA sequences amplified in multidrug-resistant hamster cells Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 2;

Ciccarelli, Richard B.; Solomon, Mark J. et al. (1985) In vivo effects of cis- and trans-diamminedichloroplatinum(II) on SV40 chromosomes: differential repair, DNA-protein crosslinking, and inhibition of replication Biochemistry; Vol. 24; No. 26;

Solomon, Mark J.; Varshavsky, Alexander (1985) Formaldehyde-mediated DNA-protein crosslinking: A probe for in vivo chromatin structures Proceedings of the National Academy of Sciences of the United States of America; Vol. 82; No. 19;

Barsoum, James; Varshavsky, Alexander (1985) Preferential localization of variant nucleosomes near the 5'-end of the mouse dihydrofolate reductase gene Journal of Biological Chemistry; Vol. 260; No. 12;

Ciechanover, A.; Finley, D. et al. (1985) Mammalian cell cycle mutant defective in intracellular protein degradation and ubiquitin-protein conjugation Progress in clinical and biological research; Vol. 180;

Özkaynak, Engin; Finley, Daniel et al. (1984) The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein Nature; Vol. 312; No. 5995;

Strauss, François; Varshavsky, Alexander (1984) A protein binds to a satellite DNA repeat at three specific sites that would be brought into mutual proximity by DNA folding in the nucleosome Cell; Vol. 37; No. 3;

Roninson, Igor B.; Abelson, Herbert T. et al. (1984) Amplification of specific DNA sequences correlates with multi-drug resistance in Chinese hamster cells Nature; Vol. 309; No. 5969;

Finley, Daniel; Ciechanover, Aaron et al. (1984) Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85 Cell; Vol. 37; No. 1;

Ciechanover, Aaron; Finley, Daniel et al. (1984) Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85 Cell; Vol. 37; No. 1;

Ciechanover, Aaron; Finley, Daniel et al. (1984) The ubiquitin-mediated proteolytic pathway and mechanisms of energy‐dependent intracellular protein degradation Journal of Cellular Biochemistry; Vol. 24; No. 1;

Varshavsky, Alexander (1983) Do stalled replication forks synthesize a specific alarmone? Journal of Theoretical Biology; Vol. 105; No. 4;

Snapka, Robert M.; Varshavsky, Alexander (1983) Loss of unstably amplified dihydrofolate reductase genes from mouse cells is greatly accelerated by hydroxyurea Proceedings of the National Academy of Sciences of the United States of America; Vol. 80; No. 24;

Wu, Kun Chi; Strauss, François et al. (1983) Nucleosome arrangement in green monkey α-satellite chromatin: Superimposition of non-random and apparently random patterns Journal of Molecular Biology; Vol. 170; No. 1;

Varshavsky, Alexander (1983) Diadenosine 5′, 5′′′-P¹, P⁴-tetraphosphate: a pleiotropically acting alarmone? Cell; Vol. 34; No. 3;

Barsoum, James; Varshavsky, Alexander (1983) Mitogenic hormones and tumor promoters greatly increase the incidence of colony-forming cells bearing amplified dihydrofolate reductase genes Proceedings of the National Academy of Sciences of the United States of America; Vol. 80; No. 17;

Swerdlow, Paul S.; Varshavsky, Alexander (1983) Affinity of HMG17 for a mononucleosome is not influenced by the presence of ubiquitin-H2A semihistone but strongly depends on DNA fragment size Nucleic Acids Research; Vol. 11; No. 2;

Varshavsky, A.; Barsoum, J. et al. (1983) Acquisition and loss of amplified genes: dramatic effects of hormones, tumor promoters and cytotoxic drugs Princess Takamatsu symposia; Vol. 14;

Varshavsky, A.; Levinger, L. et al. (1983) Cellular and SV40 Chromatin: Replication, Segregation, Ubiqiritination, Nuclease-hypersensitive Sites, HMG-containing Nueleosomes, and Heterochromatin-specific Protein Cold Spring Harbor Symposia on Quantitative Biology; Vol. 47;

Levinger, Louis; Varshavsky, Alexander (1982) Protein D1 preferentially binds A+T-rich DNA in vitro and is a component of Drosophila melanogaster nucleosomes containing A+T-rich satellite DNA Proceedings of the National Academy of Sciences of the United States of America; Vol. 79; No. 23;

Barsoum, James; Levinger, Louis et al. (1982) On the chromatin structure of the amplified, transcriptionally active gene for dihydrofolate reductase in mouse cells Journal of Biological Chemistry; Vol. 257; No. 9;

Boyce, Frederick M.; Sundin, Olof et al. (1982) New way to isolate simian virus 40 nucleoprotein complexes from infected cells: use of a thiol-specific reagent Journal of Virology; Vol. 42; No. 1;

Levinger, Louis; Varshavsky, Alexander (1982) Selective arrangement of ubiquitinated and D1 protein-containing nucleosomes within the drosophila genome Cell; Vol. 28; No. 2;

Sundin, Olof; Varshavsky, Alexander (1981) Arrest of segregation leads to accumulation of highly intertwined catenated dimers: Dissection of the final stages of SV40 DNA replication Cell; Vol. 25; No. 3;

Levinger, Louis; Varshavsky, Alexander (1981) Heat-shock proteins of Drosophila are associated with nuclease-resistant, high-salt-resistant nuclear structures Journal of Cell Biology; Vol. 90; No. 3;

Varshavsky, Alexander (1981) On the possibility of metabolic control of replicon "misfiring": Relationship to emergence of malignant phenotypes in mammalian cell lineages Proceedings of the National Academy of Sciences of the United States of America; Vol. 78; No. 6;

Levinger, Louis; Barsoum, James et al. (1981) Two-dimensional hybridization mapping of nucleosomes: Comparison of DNA and protein patterns Journal of Molecular Biology; Vol. 146; No. 3;

Sundin, Olof; Varshavsky, Alexander (1980) Terminal stages of SV40 DNA replication proceed via multiply intertwined catenated dimers Cell; Vol. 21; No. 1;

Levinger, Louis; Varshavsky, Alexander (1980) High-resolution fractionation of nucleosomes: minor particles, "whiskers," and separation of mononucleosomes containing and lacking A24 semihistone Proceedings of the National Academy of Sciences of the United States of America; Vol. 77; No. 6;

Sundin, Olof; Varshavsky, Alexander (1979) Staphylococcal nuclease makes a single non-random cut in the simian virus 40 viral minichromosome Journal of Molecular Biology; Vol. 132; No. 3;

Varshavsky, Alexander J.; Sundin, Olof et al. (1979) A stretch of “late” SV40 viral DNA about 400 bp long which includes the origin of replication is specifically exposed in SV40 minichromosomes Cell; Vol. 16; No. 2;

Varshavsky, A. J.; Sundin, O. H. et al. (1978) SV40 viral minichromosome: preferential exposure of the origin of replication as probed by restriction endonucleases Nucleic Acids Research; Vol. 5; No. 10;

Varshavsky, A. J.; Bakayev, V. V. et al. (1978) On the structure of cellular and viral chromatin Philosophical Transactions of the Royal Society of London. B, Biological Sciences; Vol. 283; No. 997;

Shmatchenko, V. V.; Varshavsky, A. J. (1978) A technique of low-pH gel electrophoresis of chromosomal proteins which does not require preliminary removal of DNA Analytical Biochemistry; Vol. 85; No. 1;

Varshavsky, A. J.; Bakayev, V. V. et al. (1978) On the Structure of Eukaryotic, Prokaryotic, and Viral Chromatin Cold Spring Harbor Symposia on Quantitative Biology; Vol. 42; No. 1;

Varshavsky, A. J.; Nedospasov, S. A. et al. (1977) Compact form of SV40 viral minichromosome is resistant to nuclease: possible implications for chromatin structure Nucleic Acids Research; Vol. 4; No. 10;

Varshavsky, A. J.; Nedospasov, S. A. et al. (1977) Histone-like proteins in the purified Escherichia coli deoxyribonucleoprotein Nucleic Acids Research; Vol. 4; No. 8;

Bakayev, V. V.; Bakayeva, T. G. et al. (1977) Nucleosomes and subnucleosomes: heterogeneity and composition Cell; Vol. 11; No. 3;

Varshavsky, A. J.; Georgiev, G. P. (1976) Free DNA stretches in histone H1-depleted chromatin and their possible relation to chromomere structure Molecular Biology Reports; Vol. 3; No. 1;

Varshavsky, A. J.; Bakayev, V. V. et al. (1976) Minichromosome of simian virus 40: presence of histone HI Nucleic Acids Research; Vol. 3; No. 8;

Varshavsky, Alexander J.; Bakayev, Valery V. et al. (1976) Studies on Chromatin. Free DNA in Sheared Chromatin European Journal of Biochemistry; Vol. 66; No. 2;

Varshavsky, A. J.; Bakayev, V. V. et al. (1976) Heterogeneity of chromatin subunits in vitro and location of histone H1 Nucleic Acids Research; Vol. 3; No. 2;

Varshavsky, A. J.; Bakayev, V. V. (1975) Studies on chromatin. III. v-Bodies and Free DNA in Chromatin Lacking Histone H1 Molecular Biology Reports; Vol. 2; No. 3;

Varshavsky, A. J.; Bakayev, V. V. (1975) Studies on chromatin. IV. Evidence for a toroidal shape of chromatin subunits Molecular Biology Reports; Vol. 2; No. 3;

Varshavsky, A. J.; Georgiev, G. P. (1975) Studies on chromatin. V. A model for the structure of chromatin subunit Molecular Biology Reports; Vol. 2; No. 3;

Varshavsky, A. J.; Ilyin, Yu. V. et al. (1974) Very long stretches of free DNA in chromatin Nature; Vol. 250; No. 5467;

Ilyin, Yu. V.; Bayev, A. A., Jr. et al. (1974) Histone-histone proximity in chromatin as seen by imidoester cross-linking Molecular Biology Reports; Vol. 1; No. 6;

Georgiev, Georgiy P.; Varshavsky, Alexandr Ja. et al. (1974) On the Structural Organization of the Transcriptional Unit in Animal Chromosomes Cold Spring Harbor Symposia on Quantitative Biology; Vol. 38;

Varshavsky, A. J.; Ilyin, Yu. V. et al. (1973) Long molecules of free DNA in the sheared chromatin preparation Molecular Biology Reports; Vol. 1; No. 4;

Varshavsky, Alexander J.; Georgiev, Georgii P. (1973) Redistribution of histones during unfolding of chromosomal DNA Molecular Biology Reports; Vol. 1; No. 3;

Varshavsky, A. J.; Georgiev, G. P. (1973) Arrangement of histones along DNA in chromosomal deoxyribonucleoprotein lacking histone F1 Molecular Biology Reports; Vol. 1; No. 2;

Varshavsky, A. J.; Georgiev, G. P. (1972) Clustered arrangement of histones F2a1 and F3 along DNA in chromosomal deoxyribonucleoproteins Biochimica et Biophysica Acta; Vol. 281; No. 4;

Varshavsky, A. Ya.; Ilyin, Yu. V. et al. (1971) Collapse of extended deoxyribonucleoprotein molecules upon increase of the ionic strength of solution Biochimica et Biophysica Acta; Vol. 246; No. 3;