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THE FASS LAB
DEPARTMENT OF STRUCTURAL BIOLOGY
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Publications

published in 2012 ...
  • Hakim, M., Ezerina, D., Alon, A., Vonshak, O. & Fass, D. Exploring ORFan domains in giant viruses: structure of mimivirus sulfhydryl oxidase R596. PLoS One 7(11):e50649 (2012). PubMed

  • Limor-Waisberg, K., Alon, A., Mehlman, T. & Fass, D. Phylogenetics and enzymology of plant quiescin sulfhydryl oxidase. FEBS Lett 586, 4119-4125 (2012). PubMed

  • Alon, A., Grossman, I., Gat, Y., Kodali, V. K., DiMaio, F., Mehlman, T., Haran, G., Baker, D., Thorpe, C. & Fass, D. The dynamic disulphide relay of quiescin sulphydryl oxidase. Nature 488, 414-418 (2012). PubMed

  • Fass, D. Disulfide bonding in protein biophysics. Annu Rev Biophys 41, 63-79 (2012). PubMed

published in 2011 ...
  • DiMaio, F., Terwilliger, T. C., Read, R. J., Wlodawer, A., Oberdorfer, G., Wagner, U., Valkov, E., Alon, A., Fass, D., Axelrod, H. L., Das, D., Vorobiev, S. M., Iwai, H., Pokkuluri, P. R. & Baker, D. Improved molecular replacement by density- and energy-guided protein structure optimization. Nature 473, 540-543 (2011). PubMed

  • Hakim, M., Mandelbaum, A. & Fass, D. Structure of a baculovirus sulfhydryl oxidase, a highly divergent member of the erv flavoenzyme family. J Virol 85, 9406-9413 (2011). PubMed

published in 2010 ...
  • Fass, D. Hunting for alternative disulfide bond formation pathways: endoplasmic reticulum janitor turns professor and teaches a lesson. Mol Cell 40, 685-686 (2010). PubMed

  • Heldman, N., Vonshak, O., Sevier, C. S., Vitu, E., Mehlman, T. & Fass, D. Steps in reductive activation of the disulfide-generating enzyme Ero1p. Protein Sci 19, 1863-1876 (2010). PubMed

  • Kogan, K., Spear, E. D., Kaiser, C. A. & Fass, D. Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals. J Mol Biol 402, 388-398 (2010). PubMed

  • Blais, J. D., Chin, K. T., Zito, E., Zhang, Y., Heldman, N., Harding, H. P., Fass, D., Thorpe, C. & Ron, D. A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity. The Journal of biological chemistry (2010). PubMed

  • Alon, A., Heckler, E. J., Thorpe, C. & Fass, D. QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains. FEBS Lett 584, 1521-1525 (2010). PubMed

  • Hakim, M. & Fass, D. Cytosolic Disulfide Bond Formation in Cells Infected With Large Nucleocytoplasmic DNA Viruses. Antioxidants & redox signaling (2010). PubMed

  • Vitu, E., Kim, S., Sevier, C. S., Lutzky, O., Heldman, N., Bentzur, M., Unger, T., Yona, M., Kaiser, C. A. & Fass, D. Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum. The Journal of biological chemistry (2010). PubMed

published in 2009 ...
  • Hakim, M. & Fass, D. Dimer interface migration in a viral sulfhydryl oxidase. Journal of Molecular Biology 391, 758-768 (2009). PubMed

  • Erez, E., Fass, D. & Bibi, E. How intramembrane proteases bury hydrolytic reactions in the membrane. Nature 459, 371-378 (2009). PubMed

  • Farver, O., Vitu, E., Wherland, S., Fass, D. & Pecht, I. Electron transfer reactivity of the Arabidopsis thaliana sulfhydryl oxidase AtErv1. J Biol Chem 284, 2098-2105 (2009). PubMed

published in 2008 ...
  • Fass, D. The Erv family of sulfhydryl oxidases. Biochim Biophys Acta 1783, 557-566 (2008). PubMed

  • Vitu, E., Gross, E., Greenblatt, H. M., Sevier, C., Kaiser, C. & Fass, D. Yeast Mpd1p reveals the structural diversity of the protein disulfide isomerase family. Journal of Molecular Biology 384, 631-640 (2008). PubMed

  • Bar, M., Celik, Y., Fass, D. & Braslavsky, I. Interactions of β-Helical Antifreeze Protein Mutants with Ice. Cryst. Growth Des., 8 (8), 2954-63 (2008).

  • Heckler, E.J., Alon, A., Fass, D. & Thorpe, C. Human Quiescin-Sulfhydryl Oxidase, QSOX1: Probing Internal Redox Steps by Mutagenesis. Biochemistry, 47 (17), 4955–63 (2008). PubMed

  • Bar, M., Scherf, T. & Fass, D. Two-dimensional surface display of functional groups on a {beta}-helical antifreeze protein scaffold. Protein Eng Des Sel 21, 107-14 (2008). PubMed
published in 2007 ...
  • Sevier, C.S., Qu, H., Heldman, N., Gross, E., Fass, D. & Kaiser CA.. Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 129, 333-44 (2007).  PubMed

  • Magidovich, E., Orr, I., Fass, D., Abdu, U. & Yifrach, O. Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins. Proc Natl Acad Sci U S A 104, 13022-7 (2007). PubMed

  • Frenkiel-Krispin, D. et al. Plant transformation by Agrobacterium tumefaciens: modulation of single-stranded DNA-VirE2 complex assembly by VirE1. J Biol Chem 282, 3458-64 (2007). PubMed

  • Fass, D. The Erv family of sulfhydryl oxidases. Biochim Biophys Acta (2007). PubMed

  • Ben-Shem, A., Fass, D. & Bibi, E. Structural basis for intramembrane proteolysis by rhomboid serine proteases. Proc Natl Acad Sci U S A 104, 462-6 (2007). PubMed

published in 2006 ...

  • Vitu, E., Bentzur, M., Lisowsky, T., Kaiser, C.A. & Fass, D. Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. J Mol Biol 362, 89-101 (2006). PubMed

  • Sirkis, R., Gerst, J.E. & Fass, D. Ddi1, a eukaryotic protein with the retroviral protease fold. J Mol Biol 364, 376-87 (2006). PubMed

  • Gross, E. Sevier, C.S., Heldman, N., Vitu, E., Bentzur, M., Kaiser, C.A., Thorpe, C. & Fass D. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc Natl Acad Sci U S A 103, 299-304 (2006). PubMed

  • Bar, M., Bar-Ziv, R., Scherf, T. & Fass, D. Efficient production of a folded and functional, highly disulfide-bonded beta-helix antifreeze protein in bacteria. Protein Expr Purif 48, 243-52 (2006). PubMed

published in 2005 ...

  • Sevier, C.S., Kadokura, H., Tam, V.C., Beckwith, J., Fass, D. & Kaiser, C.A. The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases. Protein Sci 14, 1630-42 (2005). PubMed

  • Forster, F., Medalia, O., Zauberman, N., Baumeister, W. & Fass, D. Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography. Proc Natl Acad Sci U S A 102, 4729-34 (2005). PubMed

published in 2003-2004 ...

  • Gross, E., Kastner, D.B., Kaiser, C.A. & Fass, D. Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117, 601-10 (2004). PubMed

  • Fass, D. Conformational changes in enveloped virus surface proteins during cell entry. Adv Protein Chem 64, 325-62 (2003).

  • Barnett, A.L., Wensel, D.L., Li, W., Fass, D. & Cunningham, J.M. Structure and mechanism of a coreceptor for infection by a pathogenic feline retrovirus. J Virol 77, 2717-29 (2003). PubMed

published in 2000-2002 ...

  • Gross, E., Sevier, C.S., Vala, A., Kaiser, C.A. & Fass, D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat Struct Biol 9, 61-7 (2002). PubMed

  • Paz, Y., Elazar, Z. & Fass, D. Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p. J Biol Chem 275, 25445-50 (2000). PubMed

published in 1997-1999 ...

  • Fass, D., Bogden, C.E. & Berger, J.M. Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. Nat Struct Biol 6, 322-6 (1999). PubMed

  • Fass, D., Bogden, C.E. & Berger, J.M. Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure 7, 691-8 (1999). PubMed

  • Bogden, C.E., Fass, D., Bergman, N., Nichols, M.D. & Berger, J.M. The structural basis for terminator recognition by the Rho transcription termination factor. Mol Cell 3, 487-93 (1999). PubMed

  • Babor, S.M. & Fass, D. Crystal structure of the Sec18p N-terminal domain. Proc Natl Acad Sci U S A 96, 14759-64 (1999). PubMed

  • Berger, J.M., Fass, D., Wang, J.C. & Harrison, S.C. Structural similarities between topoisomerases that cleave one or both DNA strands. Proc Natl Acad Sci U S A 95, 7876-81 (1998). PubMed

  • Fass, D. et al. Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution. Science 277, 1662-6 (1997). PubMed

  • Fass, D., Blacklow, S., Kim, P.S. & Berger, J.M. Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module. Nature 388, 691-3 (1997). PubMed

  • Chan, D.C., Fass, D., Berger, J.M. & Kim, P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-73 (1997). PubMed

published in 1993-1996 ...

  • Fass, D., Harrison, S.C. & Kim, P.S. Retrovirus envelope domain at 1.7 angstrom resolution. Nat Struct Biol 3, 465-9 (1996). PubMed

  • Fass, D. & Kim, P.S. Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin. Curr Biol 5, 1377-83 (1995). PubMed

  • Ellenberger, T., Fass, D., Arnaud, M. & Harrison, S.C. Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes Dev 8, 970-80 (1994). PubMed

  • Ponath, P.D., Fass, D., Liou, H.C., Glimcher, L.H. & Strominger, J.L. The regulatory gene, hXBP-1, and its target, HLA-DRA, utilize both common and distinct regulatory elements and protein complexes. J Biol Chem 268, 17074-82 (1993). PubMed
 
 


 

Contact the Fass Lab
deborah.fass@weizmann.ac.il
Weizmann Institute of Science
Department of Structural Biology
Rehovot, Israel
Phone: 972-8-934-3214
Fax: 972-8-934-4136