1. Shabat D., Hananya N., Press O., Das A., Scomparin A., Satchi-Fainaro R. & Sagi I. (2019). Persistent Chemiluminescent Glow of Phenoxy-Dioxetane Luminophore Enables Unique CRET-Based Detection of Proteases.  Chemistry (Weinheim an der Bergstrasse, Germany).  Abstract
  2. Mohan V., Das A. & Sagi I. (2019). Emerging roles of ECM remodeling processes in cancer.  Seminars in Cancer Biology.  Abstract
  3. Wichert R., Scharfenberg F., Colmorgen C., Koudelka T., Schwarz J., Wetzel S., Potempa B., Potempa J., Bartsch J. W., Sagi I., Tholey A., Saftig P., Rose-John S. & Becker-Pauly C. (2019). Meprin β induces activities of A disintegrin and metalloproteinases 9, 10, and 17 by specific prodomain cleavage.  FASEB Journal.  Abstract
  4. Krishnaswamy V. R., Benbenishty A., Blinder P. & Sagi I. (2019). Demystifying the extracellular matrix and its proteolytic remodeling in the brain: structural and functional insights.  Cellular and Molecular Life Sciences. 76:(16)3229-3248.  Abstract
  5. Saad M. I., McLeod L., Yu L., Ebi H., Ruwanpura S., Sagi I., Rose-John S. & Jenkins B. J. (2019). The ADAM17 Protease Promotes Tobacco Smoke Carcinogen-induced Lung Tumourigenesis.  Carcinogenesis.  Abstract
  6. Saad M. I., Alhayyani S., McLeod L., Yu L., Alanazi M., Deswaerte V., Tang K., Jarde T., Smith J. A., Prodanovic Z., Tate M. D., Balic J. J., Watkins D. N., Cain J. E., Bozinovski S., Algar E., Kohmoto T., Ebi H., Ferlin W., Garbers C., Ruwanpura S., Sagi I., Rose-John S. & Jenkins B. J. (2019). ADAM17 selectively activates the IL-6 trans-signaling/ERK MAPK axis in KRAS-addicted lung cancer.  EMBO Molecular Medicine. 11:(4)  Abstract
  7. Shimshoni E. & Sagi I. (2019). Sample Preparation of Extracellular Matrix of Murine Colons for Scanning Electron Microscopy.  . 1944:129-133.  Abstract
  8. Sapoznikov A., Gal Y., Falach R., Sagi I., Ehrlich S., Lerer E., Makovitzki A., Aloshin A., Kronman C. & Sabo T. (2019). Early disruption of the alveolar-capillary barrier in a ricin-induced ARDS mouse model: neutrophil-dependent and -independent impairment of junction proteins.  American Journal Of Physiology-Lung Cellular And Molecular Physiology. 316:(1)L255-L268.  Abstract
  9. Sagi I. & Afratis N. (2019). Collagen: Methods and protocols.  . 1944.  Abstract
  10. Afratis N. A. & Sagi I. (2019). Novel Approaches for Extracellular Matrix Targeting in Disease Treatment.  . 1952:261-275.  Abstract


  1. Golan K., Kumari A., Kollet O., Khatib-Massalha E., Subramaniam M. D., Ferreira Z. S., Avemaria F., Rzeszotek S., Garcia-Garcia A., Xie S., Flores-Figueroa E., Gur-Cohen S., Itkin T., Ludin-Tal A., Massalha H., Bernshtein B., Ciechanowicz A. K., Brandis A., Mehlman T., Bhattacharya S., Bertagna M., Cheng H., Petrovich-Kopitman E., Janus T., Kaushansky N., Cheng T., Sagi I., Ratajczak M. Z., Mendez-Ferrer S., Dick J. E., Markus R. P. & Lapidot T. (2018). Daily Onset of Light and Darkness Differentially Controls Hematopoietic Stem Cell Differentiation and Maintenance.  Cell Stem Cell. 23:(4)572+.  Abstract
  2. Afratis N. A., Klepfish M., Karamanos N. K. & Sagi I. (2018). The apparent competitive action of ECM proteases and cross-linking enzymes during fibrosis: Applications to drug discovery.  Advanced Drug Delivery Reviews. 129:4-15.  Abstract
  3. Varol C. & Sagi I. (2018). Phagocyte-extracellular matrix crosstalk empowers tumor development and dissemination.  The FEBS journal. 285:(4)734-751.  Abstract
  4. Afratis N. A., Selman M., Pardo A. & Sagi I. (2018). Emerging insights into the role of matrix metalloproteases as therapeutic targets in fibrosis.  Matrix Biology. 68-69:167-179.  Abstract


  1. Decaneto E., Vasilevskaya T., Kutin Y., Ogata H., Grossman M., Sagi I., Havenith M., Lubitz W., Thiel W. & Cox N. (2017). Solvent water interactions within the active site of the membrane type I matrix metalloproteinase.  Physical Chemistry Chemical Physics. 19:(45)30316-30331.  Abstract
  2. Levin M., Udi Y., Solomonov I. & Sagi I. (2017). Next generation matrix metalloproteinase inhibitors - Novel strategies bring new prospects.  Biochimica et Biophysica Acta - Molecular Cell Research. 1864:(11)1927-1939.  Abstract
  3. Krishnaswamy V. R., Mintz D. & Sagi I. (2017). Matrix metalloproteinases: The sculptors of chronic cutaneous wounds: The sculptors of chronic cutaneous wounds.  Biochimica et Biophysica Acta - Molecular Cell Research. 1864:(11)2220-2227.  Abstract
  4. Elad N., Bellapadrona G., Houben L., Sagi I. & Elbaum M. (2017). Detection of isolated protein-bound metal ions by single-particle cryo-STEM.  Proceedings Of The National Academy Of Sciences Of The United States Of America-Physical Sciences. 114:(42)11139-11144.  Abstract
  5. Weizman T., Levin I., Zaretsky M., Sagi I. & Aharoni A. (2017). Increased potency of a bi-specific TL1A-ADAM17 (TACE) inhibitor by cell surface targeting.  Frontiers in Molecular Biosciences. 4:(AUG)  Abstract
  6. Bassat E., Mutlak Y. E., Genzelinakh A., Shadrin I. Y., Umansky K., Yifa O., Kain D., Rajchman D., Leach J., Bassat D. R., Udi Y., Sarig R., Sagi I., Martin J. F., Bursac N., Cohen S. & Tzahor E. (2017). The extracellular matrix protein agrin promotes heart regeneration in mice.  Nature. 547:(7662)179-+.  Abstract
  7. Rachman-Tzemah C., Zaffryar-Eilot S., Grossman M., Ribero D., Timaner M., Maki J. M., Myllyharju J., Bertolini F., Hershkovitz D., Sagi I., Hasson P. & Shaked Y. (2017). Blocking Surgically Induced Lysyl Oxidase Activity Reduces the Risk of Lung Metastases.  Cell Reports. 19:(4)774-784.
  8. Arkadash V., Yosef G., Shirian J., Cohen I., Horev Y., Grossman M., Sagi I., Radisky E. S., Shifman J. M. & Papo N. (2017). Development of High Affinity and High Specificity Inhibitors of Matrix Metalloproteinase 14 through Computational Design and Directed Evolution.  Journal of Biological Chemistry. 292:(8)3481-3495.  Abstract
  9. Kurzweil-Segev Y., Popov I., Solomonov I., Sagi I. & Feldman Y. (2017). Dielectric Relaxation of Hydration Water in Native Collagen Fibrils.  Journal of Physical Chemistry B. 121:(21)5340-5346.  Abstract


  1. Wong E., Cohen T., Romi E., Levin M., Peleg Y., Arad U., Yaron A., Milla M. E. & Sagi I. (2016). Harnessing the natural inhibitory domain to control TNF alpha Converting Enzyme (TACE) activity in vivo.  Scientific Reports. 6.  Abstract
  2. Talmi-Frank D., Altboum Z., Solomonov I., Ziv T., Amit I. & Sagi I. (2016). Extracellular Matrix Proteolysis by MT1-MMP Contributes to InfluenzaInfluenza-Related Tissue Damage and Mortality.  Cell Host & Microbe. 20.  Abstract
  3. Afik R., Zigmond E., Vugman M., Klepfish M., Shimshoni E., Pasmanik-Chor M., Shenoy A., Bassat E., Halpern Z., Geiger T., Sagi I. & Varol C. (2016). Tumor macrophages are pivotal constructors of tumor collagenous matrix.  J. Exp. Med. 213:(11)  Abstract
  4. Solomonov I., Zehorai E., Talmi-Frank D., Wolf S. G., Shainskaya A., Zhuravlev A., Kartvelishvily E., Visse R., Levin Y., Kampf N., Jaitin D. A., David E., Amit I., Nagase H. & Sagi I. (2016). Distinct biological events generated by ECM proteolysis by two homologous collagenases.  Proceedings of the National Academy of Sciences of the United States of America. 113:(39)10884-10889.  Abstract
  5. Kefaloyianni E., Muthu M. L., Kaeppler J., Sun X., Sabbisetti V., Chalaris A., Rose-John S., Wong E., Sagi I., Waikar S. S., Rennke H., Humphreys B. D., Bonventre J. V. & Herrlich A. (2016). ADAM17 substrate release in proximal tubule drives kidney fibrosis.  Africa Insight. 1:(13)  Abstract
  6. Grossman M., Ben Chetrit C. N., Zhuravlev A., Afik R., Bassat E., Solomonov I., Yarden Y. & Sagi I. (2016). Tumor cell invasion can be blocked by modulators of collagen fibril alignment that control assembly of the extracellular matrix.  Cancer Res. 93:(5)  Abstract
  7. Mohan V., Talmi-Frank D., Arkadash V., Papo N. & Sagi I. (2016). Matrix metalloproteinase protein inhibitors: highlighting a new beginning for metalloproteinases in medicine.  Metalloproteinases In Medicine. 3:31-47.  Abstract


  1. Tsukerman P., Eisenstein E. M., Chavkin M., Schmiedel D., Wong E., Werner M., Yaacov B., Averbuch D., Molho-Pessach V., Stepensky P., Kaynan N., Bar-On Y., Seidel E., Yamin R., Sagi I., Elpeleg O. & Mandelboim O. (2015). Cytokine secretion and NK cell activity in human ADAM17 deficiency.  Oncotarget. 6:(42)44151-44160.  Abstract
  2. Cohen S. G., Itkin T., Chakrabarty S., Graf C., Kollet O., Ludin A., Golan K., Kalinkovich A., Ledergor G., Wong E., Niemeyer E., Porat Z., Erez A., Sagi I., Esmon C. T., Ruf W. & Lapidot T. (2015). PAR1 signaling regulates the retention and recruitment of EPCR-expressing bone marrow hematopoietic stem cells.  Nature Medicine. 21:(11)1307-17.  Abstract
  3. Kutchuk L., Laitala A., Soueid-Bomgarten S., Shentzer P., Rosendahl A., Eilot S., Grossman M., Sagi I., Sormunen R., Myllyharju J., Maki J. M. & Hasson P. (2015). Muscle composition is regulated by a Lox-TGF beta feedback loop.  Development. 142:(5)983-993.  Abstract
  4. Shimshoni E., Yablecovitch D., Baram L., Dotan I. & Sagi I. (2015). ECM remodelling in IBD: innocent bystander or partner in crime? The emerging role of extracellular molecular events in sustaining intestinal inflammation.  Gut. 64:(3)367-372.
  5. Vandooren J., Born B., Solomonov I., Zajac E., Saldova R., Senske M., Ugarte-Berzal E., Martens E., Van den Steen d. S. P. E., Van Damme D. J., Garcia-Pardo A., Froeyen M., Deryugina E. I., Quigley J. P., Moestrup S. K., Rudd P. M., Sagi I. & Opdenakker G. (2015). Circular trimers of gelatinase B/matrix metalloproteinase-9 constitute a distinct population of functional enzyme molecules differentially regulated by tissue inhibitor of metalloproteinases-1.  Biochemical Journal. 465:259-270.  Abstract
  6. Udi Y., Grossman M., Solomonov I., Dym O., Rozenberg H., Moreno V., Cuniasse P., Dive V., Garcia Arroyo A. A. & Sagi I. (2015). Inhibition Mechanism of Membrane Metalloprotease by an Exosite-Swiveling Conformational Antibody.  Structure. 23:(1)104-115.  Abstract
  7. Gaffney J. P., Solomonov I., Zehorai E. & Sagi I. (2015). Multilevel Regulation of Matrix Metalloproteinases in Tissue Homeostasis Indicates Their Molecular Specificity in vivo.  Matrix Biology. 44-46.  Abstract
  8. Chuprin A., Sagi I., Avin A., Goldfarb Y., Herzig Y., Levi B., Jacob A. & Sela A. (2015). The deacetylase Sirt1 is an essential regulator of Aire-mediated induction of central immunological tolerance.  Nature Immunology. Preprint.
  9. Wong E., Maretzky T., Peleg Y., Blobel C. P. & Sagi I. (2015). The Functional Maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 Requires Processing at a Newly Identified Proprotein Convertase (PC) Cleavage Site.  The journal of Biological chemistry. 290:12135-12146.


  1. Dielmann-Gessner J., Grossman M., Nibali V. C., Born B., Solomonov I., Fields G. B., Havenith M. & Sagi I. (2014). Enzymatic turnover of macromolecules generates long-lasting protein-water-coupled motions beyond reaction steady state.  Proceedings of the National Academy of Sciences of the United States of America. 111:(50)17857-17862.  Abstract
  2. Solomonov I., Talmi-Frank D., Milstein Y., Addadi S., Aloshin A. & Sagi I. (2014). Introduction of correlative light and airSEM (TM) microscopy imaging for tissue research under ambient conditions.  Scientific Reports. 4.  Abstract
  3. Cohen-Fredarow A., Tadmor A., Raz T., Meterani N., Addadi Y., Nevo N., Solomonov I., Sagi I., Mor G., Neeman M. & Dekel N. (2014). Ovarian Dendritic Cells Act as a Double-Edged Pro-Ovulatory and Anti-Inflammatory Sword.  Molecular Endocrinology. 28:(7)1039-1054.  Abstract
  4. Romi E., Gokhman I., Wong E., Antonovsky N., Ludwig A., Sagi I., Saftig P., Tessier-Lavigne M. & Yaron A. (2014). ADAM metalloproteases promote a developmental switch in responsiveness to the axonal repellant Sema3A.  Nature Communications. 5.  Abstract
  5. Sharabi O., Shirian J., Grossman M., Lebendiker M., Sagi I. & Shifman J. (2014). Affinity- and Specificity-Enhancing Mutations Are Frequent in Multispecific Interactions between TIMP2 and MMPs.  PLoS One. 9:(4)  Abstract
  6. Binsky-Ehrenreich I., Marom A., Sobotta M. C., Shvidel L., Berrebi A., Hazan-Halevy I., Kay S., Aloshin A., Sagi I., Goldenberg D. M., Leng L., Bucala R., Herishanu Y., Haran M. & Shachar I. (2014). CD84 is a survival receptor for CLL cells.  Oncogene. 33:(8)1006-1016.  Abstract
  7. Ogata H., Decaneto E., Grossman M., Havenith M., Sagi I., Lubitz W. & Knipp M. (2014). Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of membrane type 1 matrix metalloproteinase.  Acta Crystallographica Section F-Structural Biology And Crystallization Communications. 70:232-235.  Abstract
  8. Fragai M., Luchinat C., Martelli T., Ravera E., Sagi I., Solomonov I. & Udi Y. (2014). SSNMR of biosilica-entrapped enzymes permits an easy assessment of preservation of native conformation in atomic detail.  Chemical Communications. 50:(4)421-423.  Abstract
  9. Solomonov I. & Sagi I. (2014). The Effect of Zinc on Amyloid beta-protein Assembly and Toxicity: a Mechanistic Investigation.  . 121-124.  Abstract


  1. Udi Y., Fragai M., Grossman M., Mitternacht S., Arad-Yellin R., Calderone V., Melikian M., Toccafondi M., Berezovsky I. N., Luchinat C. & Sagi I. (2013). Unraveling Hidden Regulatory Sites in Structurally Homologous Metalloproteases.  Journal of Molecular Biology. 425:(13)2330-2346.  Abstract


  1. Pradeep C., Zeisel A., Koestler W. J., Lauriola M., Jacob-Hirsch J., Haibe-Kains B., Amariglio N., Ben Chetrit C. N., Emde A. M., Solomonov I., Neufeld G., Piccart M., Sagi I., Sotiriou C., Rechavi G., Domany E., Desmedt C. & Yarden Y. (2012). Modeling invasive breast cancer: growth factors propel progression of HER2-positive premalignant lesions.  Oncogene. 31:(31)3569-3583.  Abstract
  2. Solomonov I., Korkotian E., Born B., Feldman Y. (., Bitler A., Rahimi F., Li H., Bitan G. & Sagi I. (2012). Zn2+-A beta 40 Complexes Form Metastable Quasi-spherical Oligomers That Are Cytotoxic to Cultured Hippocampal Neurons.  Journal of Biological Chemistry. 287:(24)20555-20564.  Abstract
  3. Sela-Passwell N. A., Kikkeri R., Dym O., Rozenberg H., Margalit R., Arad-Yellin R., Eisenstein M., Brenner O., Shoham T., Danon T., Shanzer A. & Sagi I. (2012). Antibodies targeting the catalytic zinc complex of activated matrix metalloproteinases show therapeutic potential.  Nature Medicine. 18:(1)143-147.  Abstract


  1. Shechter R., Raposo C., London A., Sagi I. & Schwartz M. (2011). The Glial Scar-Monocyte Interplay: A Pivotal Resolution Phase in Spinal Cord Repair.  PLoS One. 6:(12)  Abstract
  2. Grossman M., Sela-Passwell N. & Sagi I. (2011). Achieving broad molecular insights into dynamic protein interactions by integrated structural-kinetic approaches.  Current Opinion in Structural Biology. 21:(5)678-685.  Abstract
  3. Kaminker I., Sushenko A., Potapov A., Daube S., Akabayov B., Sagi I. & Goldfarb D. (2011). Probing Conformational Variations at the ATPase Site of the RNA Helicase DbpA by High-Field Electron-Nuclear Double Resonance Spectroscopy.  Journal of the American Chemical Society. 133:(39)15514-15523.  Abstract
  4. Grossman M., Born B., Heyden M., Tworowski D., Fields G. B., Sagi I. & Havenith M. (2011). Correlated structural kinetics and retarded solvent dynamics at the metalloprotease active site.  Nature Structural & Molecular Biology. 18:(10)1102-U113.  Abstract
  5. Sela-Passwell N., Trahtenherts A., Krueger A. & Sagi I. (2011). New opportunities in drug design of metalloproteinase inhibitors: combination between structure-function experimental approaches and systems biology.  Expert Opinion on Drug Discovery. 6:(5)527-542.  Abstract
  6. Orgel J. P. R. O., Antipova O., Sagi I., Bitler A., Qiu D., Wang R., Xu Y. & Antonio J. D. S. (2011). Collagen fibril surface displays a constellation of sites capable of promoting fibril assembly, stability, and hemostasis.  Connective Tissue Research. 52:(1)18-24.  Abstract


  1. Grossman M., Tworowski D., Dym O., Lee M., Levy Y., Murphy G. & Sagi I. (2010). The Intrinsic Protein Flexibility of Endogenous Protease Inhibitor TIMP-1 Controls Its Binding Interface and Affects Its Function.  Biochemistry. 49:(29)6184-6192.  Abstract
  2. Rosenblum G., Van den Steen d. S. P. E., Cohen S., Bitler A., Brand D. D., Opdenakker G. & Sagi I. (2010). Direct Visualization of Protease Action on Collagen Triple Helical Structure.  PLoS One. 5:(6)  Abstract
  3. Rouffet M., de Oliveira O. C. A. F., Udi Y., Agrawal A., Sagi I., McCammon J. A. & Cohen S. M. (2010). From Sensors to Silencers: Quinoline-and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases.  Journal of the American Chemical Society. 132:(24)8232-+.  Abstract
  4. Sela-Passwell N., Rosenblum G., Shoham T. & Sagi I. (2010). Structural and functional bases for allosteric control of MMP activities: Can it pave the path for selective inhibition?.  Biochimica Et Biophysica Acta-Molecular Cell Research. 1803:(1)29-38.  Abstract
  5. Politi Y., Batchelor D. R., Zaslansky P., Chmelka B. F., Weaver J. C., Sagi I., Weiner S. & Addadi L. (2010). Role of Magnesium Ion in the Stabilization of Biogenic Amorphous Calcium Carbonate: A Structure-Function Investigation.  Chemistry of Materials. 22:(1)161-166.  Abstract


  1. Cayrol B., Nogues C., Dawid A., Sagi I., Silberzan P. & Isambert H. (2009). A Nanostructure Made of a Bacterial Noncoding RNA.  Journal of the American Chemical Society. 131:(47)17270-17276.  Abstract


  1. Politi Y., Metzler R. A., Abrecht M., Gilbert B., Wilt F. H., Sagi I., Addadi L., Weiner S. & Gilbert P. U. P. A. (2008). Transformation mechanism of amorphous calcium carbonate into calcite in the sea urchin larval spicule.  Proceedings of the National Academy of Sciences of the United States of America. 105:(45)17362-17366.  Abstract
  2. Lewis K. C., Selzer T., Shahar C., Udi Y., Tworowski D. & Sagi I. (2008). Inhibition of pectin methyl esterase activity by green tea catechins.  Phytochemistry. 69:(14)2586-2592.  Abstract
  3. Noy D., Solomonov I., Sinkevich O., Arad T., Kjaer K. & Sagi I. (2008). Zinc-amyloid-beta interactions on a millisecond time-scale stabilize non-fibrillar Alzheimer-related species.  Journal of the American Chemical Society. 130:(4)1376-1383.  Abstract
  4. Sagi I. & Milla M. E. (2008). Application of structural dynamic approaches provide novel insights into the enzymatic mechanism of the tumor necrosis factor-alpha-converting enzyme.  Analytical Biochemistry. 372:(1)1-10.


  1. Rosenblum G., Meroueh S., Toth M., Fisher J. F., Fridman R., Mobashery S. & Sagi I. (2007). Molecular structures and dynamics of the stepwise activation mechanism of a matrix metalloproteinase zymogen: Challenging the cysteine switch dogma.  Journal of the American Chemical Society. 129:(44)13566-13574.  Abstract
  2. Rosenblum G., Van den Steen d. S. P. E., Cohen S., Grossmann J. G., Frenkel J., Sertchook R., Slacks N., Strange R. W., Opdenakker G. & Sagi I. (2007). Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9/gelatinase B.  Structure. 15:(10)1227-1236.  Abstract
  3. Solomon A., Akabayov B., Frenkel A., Milla M. E. & Sagi I. (2007). Key feature of the catalytic cycle of TNF-alpha converting enzyme involves communication between distal protein sites and the enzyme catalytic core.  Proceedings of the National Academy of Sciences of the United States of America. 104:(12)4931-4936.  Abstract
  4. Sertchook R., Solomon A., Selzer T. & Sagi I. (2007). Structural dynamic approach as rational input for drug design.  Structure And Biophysics - New Technologies For Current Challenges In Biology Beyond. 231:111-120.  Abstract


  1. Politi Y., Levi-Kalisman Y., Raz S., Wilt F., Addadi L., Weiner S. & Sagi I. (2006). Structural characterization of the transient amorphous calcium carbonate precursor phase in sea urchin embryos.  Advanced Functional Materials. 16:(10)1289-1298.  Abstract
  2. Talavera M., Matthews E., Eliason W., Sagi I., Wang J., Henn A. & De La Cruz L. C. E. (2006). Hydrodynamic characterization of the DEAD-box RNA helicase DbpA.  Journal of Molecular Biology. 355:(4)697-707.  Abstract


  1. Weiner S., Sagi I. & Addadi L. (2005). Choosing the crystallization path less traveled.  Science. 309:(5737)1027-1028.
  2. Akabayov B., Doonan C., Pickering I., George G. & Sagi I. (2005). Using softer X-ray absorption spectroscopy to probe biological systems.  Journal of Synchrotron Radiation. 12:392-401.  Abstract


  1. Yavin E., Stemp E., Weiner L., Sagi I., Arad-Yellin R. & Shanzer A. (2004). Direct photo-induced DNA strand scission by a ruthenium bipyridyl complex.  Journal of Inorganic Biochemistry. 98:(11)1750-1756.  Abstract
  2. Solomon A., Rosenblum G., Gonzales P., Leonard J., Mobashery S., Milla M. & Sagi I. (2004). Pronounced diversity in electronic and chemical properties between the catalytic zinc sites of tumor necrosis factor-alpha-converting enzyme and matrix metalloproteinases despite their high structural similarity.  Journal of Biological Chemistry. 279:(30)31646-31654.  Abstract
  3. Gonzales P., Solomon A., Miller A., Leesnitzer M., Sagi I. & Milla M. (2004). Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.  Journal of Biological Chemistry. 279:(30)31638-31645.  Abstract
  4. Kleifeld O., Rulisek L., Bogin O., Frenkel A., Havlas Z., Burstein Y. & Sagi I. (2004). Higher metal-ligand coordination in the catalytic site of cobalt-substituted Thermoanaerobacter brockii alcohol dehydrogenase lowers the barrier for enzyme catalysis.  Biochemistry. 43:(22)7151-7161.  Abstract


  1. Zajfman D., Rudich Y., Sagi I., Strasser D., Savin D., Goldberg S., Rappaport M. & Heber O. (2003). High resolution mass spectrometry using a linear electrostatic ion beam trap.  International Journal of Mass Spectrometry. 229:(2-Jan)55-60.  Abstract
  2. Rosenblum G., Meroueh S., Kleifeld O., Brown S., Singson S., Fridman R., Mobashery S. & Sagi I. (2003). Structural basis for potent slow binding inhibition of human matrix metalloproteinase-2 (MMP-2).  Journal of Biological Chemistry. 278:(29)27009-27015.  Abstract
  3. Akabayov B., Henn A., Elbaum M. & Sagi I. (2003). RNA labeling and immobilization for nano-displacement measurement: Probing three-dimensional RNA structure.  IEEE Transactions on Nanobioscience. 2:(2)70-74.  Abstract
  4. Kleifeld O., Shi S., Zarivach R., Eisenstein M. & Sagi I. (2003). The conserved Glu-60 residue in Thermoanaerobacter brockii alcohol dehydrogenase is not essential for catalysis.  Protein Science. 12:(3)468-479.  Abstract
  5. Kleifeld O., Frenkel A., Martin J. & Sagi I. (2003). Active site electronic structure and dynamics during metalloenzyme catalysis.  Nature Structural Biology. 10:(2)98-103.  Abstract


  1. Strasser D., Geyer T., Pedersen H., Heber O., Goldberg S., Amarant B., Diner A., Rudich Y., Sagi I., Rappaport M., Tannor D. & Zajfman D. (2002). Negative mass instability for interacting particles in a 1D box: Theory and application.  Physical Review Letters. 89:(28)  Abstract
  2. Henn A., Shi S., Zarivach R., Ben-Zeev E. & Sagi I. (2002). The RNA helicase DbpA exhibits a markedly different conformation in the ADP-bound state when compared with the ATP- or RNA-bound states.  Journal of Biological Chemistry. 277:(48)46559-46565.  Abstract
  3. Federman S., Miller L. & Sagi I. (2002). Following matrix metalloproteinases activity near the cell boundary by infrared micro-spectroscopy.  Matrix Biology. 21:(7)567-577.  Abstract
  4. Frenkel A., Kleifeld O., Wasserman S. & Sagi I. (2002). Phase speciation by extended x-ray absorption fine structure spectroscopy.  Journal of Chemical Physics. 116:(21)9449-9456.  Abstract
  5. Cheng F., Zhang R., Luo X., Shen J., Li X., Gu J., Zhu W., Shen J., Sagi I., Ji R., Chen K. & Jiang H. (2002). Quantum chemistry study on the interaction of the exogenous ligands and the catalytic zinc ion in matrix metalloproteinases.  Journal of Physical Chemistry B. 106:(17)4552-4559.  Abstract
  6. Levi-Kalisman Y., Raz S., Weiner S., Addadi L. & Sagi I. (2002). Structural differences between biogenic amorphous calcium carbonate phases using X-ray absorption spectroscopy.  Advanced Functional Materials. 12:(1)43-48.  Abstract


  1. Henn A., Halfon J., Kela I., Orion I. & Sagi I. (2001). Nucleic acid fragmentation on the millisecond timescale using a conventional X-ray rotating anode source: application to protein-DNA footprinting.  Nucleic Acids Research. 29:(24)  Abstract
  2. Pedersen H., Strasser D., Ring S., Heber O., Rappaport M., Rudich Y., Sagi I. & Zajfman D. (2001). Ion motion synchronization in an ion-trap resonator.  Physical Review Letters. 87:(5)  Abstract
  3. Kleifeld O., Kotra L., Gervasi D., Brown S., Bernardo M., Fridman R., Mobashery S. & Sagi I. (2001). X-ray absorption studies of human matrix metalloproteinase-2 (MMP-2) bound to a highly selective mechanism-based inhibitor - Comparison with the latent and active forms of the enzyme.  Journal of Biological Chemistry. 276:(20)17125-17131.  Abstract
  4. Henn A., Medalia O., Shi H., Steinberg M., Franceschi F. & Sagi I. (2001). Visualization of unwinding activity of duplex RNA by DbpA, a DEAD box helicase, at single-molecule resolution by atomic force microscopy.  Proceedings of the National Academy of Sciences of the United States of America. 98:(9)5007-5012.  Abstract
  5. Kleifeld O., Frenkel A. & Sagi I. (2001). Time-dependent XAS studies of trapped enzyme-substrate complexes of alcohol dehydrogenase from Thermoanaerobacter brockii.  Journal of Synchrotron Radiation. 8:978-980.  Abstract
  6. Orion I., Dilmanian F., Zhong Z., Rosenfeld A., Henn A., Sagi I. & Pena L. (2001). Simulations for x-ray synchrotron beams using the EGS4 code system in medical applications.  Advanced Monte Carlo For Radiation Physics, Particle Transport Simulation And Applications. 93-98.  Abstract


  1. Kleifeld O., Van den Steen d. S. P., Frenkel A., Cheng F., Jiang H., Opdenakker G. & Sagi I. (2000). Structural characterization of the catalytic active site in the latent and active natural gelatinase B from human neutrophils.  Journal of Biological Chemistry. 275:(44)34335-34343.  Abstract
  2. Ring S., Pedersen H., Heber O., Rappaport M., Witte P., Bhushan K., Altstein N., Rudich Y., Sagi I. & Zajfman D. (2000). Fourier transform time-of flight mass spectrometry in an electrostatic ion beam trap.  Analytical Chemistry. 72:(17)4041-4046.  Abstract
  3. Kleifeld O., Frenkel A., Bogin O., Eisenstein M., Brumfeld V., Burstein Y. & Sagi I. (2000). Spectroscopic studies of inhibited alcohol dehydrogenase from Thermoanaerobacter brockii: Proposed structure for the catalytic intermediate state.  Biochemistry. 39:(26)7702-7711.  Abstract
  4. Levi-Kalisman Y., Raz S., Weiner S., Addadi L. & Sagi I. (2000). X-Ray absorption spectroscopy studies on the structure of a biogenic "amorphous" calcium carbonate phase.  Journal Of The Chemical Society-Dalton Transactions. (21)3977-3982.  Abstract


  1. Sagi I., Hochman Y., Bunker G., Carmeli S. & Carmeli C. (1999). The penta-coordinated vanadium formed on binding of ADP-vanadate-Mg(II) to CF1-ATPase functions as a transition-state inhibitor.  Journal of Synchrotron Radiation. 6:409-410.  Abstract


  1. Sagi I., Hochman Y., Bunker G., Carmeli S. & Carmeli C. (1998). Structure function relationship of vanadate bound to a single site in chloroplast CF1-ATPase as determined by X-ray absorption.  Photosynthesis Research. 57:(3)275-285.  Abstract


  1. Sagi I., Bunker G., Hochman Y., Carmeli C. & Zeng M. (1997). Determination by X-ray absorption of redox induced structural changes in iron-sulfur cluster F-x in photosystem I.  Acta Physica Polonica A. 91:(5)871-875.  Abstract
  2. Agmon I., Bartels H., Bashan A., Bennett W., Berkovitch Z., Boddeker N., Dribin A., Eisenstein M., Franceschi F., Hansen H., Harms J., Jahn W., Krumbholz S., Levin I., Malemud M., Morlang S., Peretz M., Sagi I., Schlunzen F., Sharon R., Thygesen J., Volkmann N., Weinrich V., Weinstein S. & Yonath A. (1997). Crystallography, biochemistry and genetics of halophilic and thermophilic ribosomes.  Supramolecular structure and function 5. 155-185.


  1. Thygesen J., Krumbholz S., Levin I., Zaytzev-Bashan A., Harms J., Bartels H., Schlünzen F., Hansen H., Bennett W., Volkmann N., Agmon I., Eisenstein M., Dribin A., Maltz E., Sagi I., Morlang S., Fua M., Franceschi F., Weinstein S., Böddeker N., Sharon R., Anagnostopoulos K., Peretz M., Geva M., Berkovitch-Yellin Z. & Yonath A. (1996). Ribosomal crystallography: From crystal growth to initial phasing.  Journal of Crystal Growth. 168:(1)308-323.  Abstract
  2. Franceschi F., Weinstein S., Sagi I., Peretz M., Werinrich V., Morlang S., Anagnostopoulos K., Boeddeker N., Geva M., Levin I., Agmon I., Berkovitch-Yellin Z., Choli T., Tsiboli P., Schluenzen F., Hanson H., Bartels H., Bennett W., Volkmann N., Thygesen J., Harms J., Zaytzev-Bashan A., Krumbholz S., Sharon R., Dribin A., Maltz E. & Yonath A. (1996). The combination of functional, genetics, biochemical, microscopical and crystallographic studies led to initial phasing of data collected from ribosomal crystals at intermediate resolution.  Biological structure and dynamics. 25-41.


  1. Schlunzen F., Hansen H., Thygesen J., Bennett W., Volkmann N., Levin I., Harms J., Bartels H., Zaytzev-Bashan A., Berkovitch-Yellin Z., Sagi I., Franceschi F., Krumbholz S., Geva M., Weinstein S., Agmon I., Boddeker N., Morlang S., Sharon R., Dribin A., Maltz E., Peretz M., Weinrich V. & Yonath A. (1995). A milestone in ribosomal crystallography: The construction of preliminary electron density maps at intermediate resolution.  Biochemistry And Cell Biology-Biochimie Et Biologie Cellulaire. 73:(11-12)739-749.  Abstract
  2. Sagi I., WEINRICH V., Levin I., GLOTZ C., Laschever M., MELAMUD M., FRANCESCHI F., Weinstein S. & Yonath A. (1995). CRYSTALLOGRAPHY OF RIBOSOMES - ATTEMPTS AT DECORATING THE RIBOSOMAL SURFACE.  Biophysical Chemistry. 55:(2-Jan)31-41.  Abstract


  2. FRANCESCHI F., Sagi I., BODDEKER N., EVERS U., ARNDT E., PAULKE C., HASENBANK R., Laschever M., GLOTZ C., PIEFKE J., MUSSIG J., Weinstein S. & Yonath A. (1994). CRYSTALLOGRAPHIC, BIOCHEMICAL AND GENETIC-STUDIES ON HALOPHILIC RIBOSOMES.  Systematic and Applied Microbiology. 16:(4)697-705.  Abstract


  1. Franceschi F., Weinstein S., Evers U., Arndt E., Jahn W., Hansen H. A. S., von Böhlen K., Berkovitch-Yellin Z., Eisenstein M., Agmon I., Thygesen J., Volkmann N., Bartels H., Schlünzen F., Zaytzev-Bashan A., Sharon R., Levin I., Dribin A., Sagi I., Choli-Papadopoulou T., Tsiboli P., Kryger G., Bennett W. S. & Yonath A. (1993). Towards Atomic Resolution of Prokaryotic Ribosomes:: Crystallographic, Genetic and Biochemical Studies.  The Translational Apparatus: Structure, Function, Regulation, Evolution. 397-410.  Abstract


  1. Chance M. R., Sagi I., Wirt M. D., Frisbie S. M., Scheuring E., Chen E., Bess J. W., Henderson L. E., Arthur L. O. & South T. L. (1992). Extended x-ray absorption fine structure studies of a retrovirus: equine infectious anemia virus cysteine arrays are coordinated to zinc.  Proceedings Of The National Academy Of Sciences Of The United States Of America-Biological Sciences. 89:(21)10041-10045.  Abstract
  2. Sagi I. & Chance M. R. (1992). Extent of trans effects in (nonalkyl)cobalamins: steric effects control the cobalt-nitrogen distance to 5,6-dimethylbenzimidazole.  Journal of the American Chemical Society. 114:(21)8061-8066.  Abstract
  3. Summers M. F., Henderson L. E., Chance M. R., South T. L., Blake P. R., Perez‐Alvarado G., Bess J. W., Sowder R. C., Arthur L. O., Sagi I. & Hare D. R. (1992). Nucleocapsid zinc fingers detected in retroviruses: EXAFS studies of intact viruses and the solution‐state structure of the nucleocapsid protein from HIV‐1.  Protein Science. 1:(5)563-574.  Abstract
  4. Wirt M., Sagi I. & Chance M. (1992). Formation of a square-planar Co(I) B12 intermediate. Implications for enzyme catalysis.  Biophysical Journal. 63:(2)412-417.  Abstract


  1. Wirt M. D., Sagi I., Chen E., Frisbie S. M., Lee R. & Chance M. R. (1991). Geometric conformations of intermediates of B12 catalysis by x-ray edge spectroscopy: cobalt(I) B12, cobalt(II) B12, and base-off adenosylcobalamin.  Journal of the American Chemical Society. 113:(14)5299-5304.  Abstract


  1. Sagi I., Wirt M. D., Chen E., Frisbie S. & Chance M. R. (1990). Structure of an intermediate of coenzyme B12 catalysis by EXAFS: Co2+ B12.  Journal of the American Chemical Society. 112:(24)8639-8644.  Abstract