| Year |
Citation |
Score |
| 2020 |
Karkisaval AG, Rostagno A, Azimov R, Ban DK, Ghiso J, Kagan BL, Lal R. Ion channel formation by N-terminally truncated Aβ (4-42): Relevance for the pathogenesis of Alzheimer's disease. Nanomedicine : Nanotechnology, Biology, and Medicine. 102235. PMID 32531337 DOI: 10.1016/J.Nano.2020.102235 |
0.467 |
|
| 2017 |
Lee J, Kim YH, Teran Arce F, Gillman AL, Jang H, Kagan BL, Nussinov R, Yang J, Lal R. Amyloid β ion channels in a membrane comprised of brain total lipid extracts. Acs Chemical Neuroscience. PMID 28135799 DOI: 10.1021/Acschemneuro.7B00006 |
0.608 |
|
| 2016 |
Jang H, Arce FT, Lee J, Gillman AL, Ramachandran S, Kagan BL, Lal R, Nussinov R. Computational Methods for Structural and Functional Studies of Alzheimer's Amyloid Ion Channels. Methods in Molecular Biology (Clifton, N.J.). 1345: 251-68. PMID 26453217 DOI: 10.1007/978-1-4939-2978-8_16 |
0.57 |
|
| 2015 |
Patel N, Ramachandran S, Azimov R, Kagan BL, Lal R. Ion Channel Formation by Tau Protein: Implications for Alzheimer's Disease and Taupathies. Biochemistry. PMID 26575330 DOI: 10.1021/acs.biochem.5b00988 |
0.608 |
|
| 2014 |
Lee J, Gillman AL, Jang H, Ramachandran S, Kagan BL, Nussinov R, Teran Arce F. Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability. Biochemistry. 53: 4704-14. PMID 24950761 DOI: 10.1021/Bi500587P |
0.542 |
|
| 2014 |
Gillman AL, Jang H, Lee J, Ramachandran S, Kagan BL, Nussinov R, Teran Arce F. Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) pores. The Journal of Physical Chemistry. B. 118: 7335-44. PMID 24922585 DOI: 10.1021/Jp5040954 |
0.508 |
|
| 2014 |
Jang H, Arce FT, Ramachandran S, Kagan BL, Lal R, Nussinov R. Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs. Chemical Society Reviews. 43: 6750-64. PMID 24566672 DOI: 10.1039/C3Cs60459D |
0.527 |
|
| 2014 |
Azimov R, Kagan BL. Tau Protein Forms Ion Channels Biophysical Journal. 106: 549. DOI: 10.1016/J.Bpj.2013.11.3056 |
0.632 |
|
| 2013 |
Jang H, Arce FT, Ramachandran S, Kagan BL, Lal R, Nussinov R. Familial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment. The Journal of Physical Chemistry. B. 117: 11518-29. PMID 24000923 DOI: 10.1021/Jp405389N |
0.438 |
|
| 2013 |
Jang H, Connelly L, Arce FT, Ramachandran S, Lal R, Kagan BL, Nussinov R. Alzheimer's disease: which type of amyloid-preventing drug agents to employ? Physical Chemistry Chemical Physics : Pccp. 15: 8868-77. PMID 23450150 DOI: 10.1039/C3Cp00017F |
0.52 |
|
| 2013 |
Jang H, Connelly L, Arce FT, Ramachandran S, Kagan BL, Lal R, Nussinov R. Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane. Journal of Chemical Theory and Computation. 9: 822-833. PMID 23316126 DOI: 10.1021/Ct300916F |
0.504 |
|
| 2013 |
Jang H, Connelly L, Teran Arce F, Ramachandran S, Kagan BL, Lal R, Nussinov R. Modeling Variants of Alzheimer's Ion Channels in the Lipid Bilayer formed by an Aggregation-Intermediate β-Hairpin and E22Δ Mutant Biophysical Journal. 104: 390a-391a. DOI: 10.1016/J.Bpj.2012.11.2177 |
0.382 |
|
| 2012 |
Kagan BL. Membrane pores in the pathogenesis of neurodegenerative disease. Progress in Molecular Biology and Translational Science. 107: 295-325. PMID 22482454 DOI: 10.1016/B978-0-12-385883-2.00001-1 |
0.506 |
|
| 2012 |
Capone R, Jang H, Kotler SA, Connelly L, Teran Arce F, Ramachandran S, Kagan BL, Nussinov R, Lal R. All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers. Journal of Chemical Theory and Computation. 8: 1143-1152. PMID 22423218 DOI: 10.1021/Ct200885R |
0.533 |
|
| 2012 |
Connelly L, Jang H, Arce FT, Ramachandran S, Kagan BL, Nussinov R, Lal R. Effects of point substitutions on the structure of toxic Alzheimer's β-amyloid channels: atomic force microscopy and molecular dynamics simulations. Biochemistry. 51: 3031-8. PMID 22413858 DOI: 10.1021/Bi300257E |
0.491 |
|
| 2012 |
Capone R, Jang H, Kotler SA, Kagan BL, Nussinov R, Lal R. Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions. Biochemistry. 51: 776-85. PMID 22242635 DOI: 10.1021/Bi2017427 |
0.59 |
|
| 2012 |
Connelly L, Jang H, Arce FT, Capone R, Kotler SA, Ramachandran S, Kagan BL, Nussinov R, Lal R. Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology. The Journal of Physical Chemistry. B. 116: 1728-35. PMID 22217000 DOI: 10.1021/Jp2108126 |
0.576 |
|
| 2012 |
Kagan BL, Jang H, Capone R, Teran Arce F, Ramachandran S, Lal R, Nussinov R. Antimicrobial properties of amyloid peptides. Molecular Pharmaceutics. 9: 708-17. PMID 22081976 DOI: 10.1021/Mp200419B |
0.6 |
|
| 2012 |
Capone R, Jang H, Kotler SA, Connelly L, Williams M, Ramachandra Reddy S, Kagan BL, Nussinov R, Lal R. All D-Amino Acids Amyloid β Forms Ion Channels in Lipid Bilayers and is Toxic to Cells Biophysical Journal. 102: 616a-617a. DOI: 10.1016/J.Bpj.2011.11.3360 |
0.546 |
|
| 2012 |
Connelly LS, Teran Arce F, Jang H, Capone R, Kotler S, Kagan B, Nussinov R, Lal R. Alzheimer's β-Amyloid All-D-Enantiomers and Native All-L-Enantiomers Exhibit Similar Pore Structures in Lipid Bilayers: Atomic Force Microscopy Biophysical Journal. 102: 588a-589a. DOI: 10.1016/J.Bpj.2011.11.3207 |
0.534 |
|
| 2012 |
Jang H, Capone R, Kotler SA, Teran Arce F, Connelly L, Ramachandran S, Kagan BL, Lal R, Nussinov R. Modeling Alzheimer's Ion Channel Structures in Lipid Bilayers Formed by D- and L-Enantiomers of Beta-Amyloid (1-42) Peptide Biophysical Journal. 102: 440a. DOI: 10.1016/J.Bpj.2011.11.2410 |
0.529 |
|
| 2011 |
Hirakura Y, Azimov R, Azimova R, Javier F, Schweitzer ES, Kagan BL. Transthyretin channel formation in lipid membranes: implications for pathogenesis. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 18: 8-10. PMID 21838414 DOI: 10.3109/13506129.2011.574354002 |
0.632 |
|
| 2010 |
Kagan BL, Thundimadathil J. Amyloid peptide pores and the beta sheet conformation. Advances in Experimental Medicine and Biology. 677: 150-67. PMID 20687488 DOI: 10.1007/978-1-4419-6327-7_13 |
0.578 |
|
| 2010 |
Jang H, Arce FT, Ramachandran S, Capone R, Azimova R, Kagan BL, Nussinov R, Lal R. Truncated beta-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndrome. Proceedings of the National Academy of Sciences of the United States of America. 107: 6538-43. PMID 20308552 DOI: 10.1073/Pnas.0914251107 |
0.524 |
|
| 2008 |
Epand RF, Zhang YL, Mirzabekov T, Kagan B, Silberstein A, Hubbell WL, Epand RM, Chakraborti S, Dimitrov DS, Anderson WF, Rozenberg-Adler Y. Membrane activity of an amphiphilic alpha-helical membrane-proximal cytoplasmic domain of the MoMuLV envelope glycoprotein. Experimental and Molecular Pathology. 84: 9-17. PMID 18206141 DOI: 10.1016/j.yexmp.2007.11.003 |
0.756 |
|
| 2006 |
Fagan T, Kagan B, Corbin D, Hwang W, Glabe C, Nault L, Lal R, Teplow D, Albensi B, Sokolov Y. Alzheimer Research Forum Live Discussion: Now you see them, now you don't: The amyloid channel hypothesis. Journal of Alzheimer's Disease : Jad. 9: 219-24. PMID 16873968 DOI: 10.3233/Jad-2006-9213 |
0.427 |
|
| 2006 |
Ghiso JA, Quist A, Doudevski I, Lin H, Azimova R, Ng D, Frangione B, Kagan B, Lal R. P4-083 : Amyloid ion channels: A common structural link for protein-misfolding disease pathogenesis? Alzheimers & Dementia. 2. DOI: 10.1016/J.Jalz.2006.05.1821 |
0.472 |
|
| 2005 |
Quist A, Doudevski I, Lin H, Azimova R, Ng D, Frangione B, Kagan B, Ghiso J, Lal R. Amyloid ion channels: a common structural link for protein-misfolding disease. Proceedings of the National Academy of Sciences of the United States of America. 102: 10427-32. PMID 16020533 DOI: 10.1073/Pnas.0502066102 |
0.528 |
|
| 2005 |
Kagan BL, Azimov R. Channels Formed in Planar Lipid Bilayers by Amyloid Peptides Advances in Planar Lipid Bilayers and Liposomes. 1: 207-220. DOI: 10.1016/S1554-4516(05)01007-0 |
0.506 |
|
| 2004 |
Kagan BL, Azimov R, Azimova R. Amyloid peptide channels. The Journal of Membrane Biology. 202: 1-10. PMID 15702375 DOI: 10.1007/s00232-004-0709-4 |
0.623 |
|
| 2002 |
Kagan BL, Hirakura Y, Azimov R, Azimova R, Lin MC. The channel hypothesis of Alzheimer's disease: current status. Peptides. 23: 1311-5. PMID 12128087 DOI: 10.1016/S0196-9781(02)00067-0 |
0.789 |
|
| 2002 |
Lin MC, Kagan BL. Electrophysiologic properties of channels induced by Abeta25-35 in planar lipid bilayers. Peptides. 23: 1215-28. PMID 12128079 DOI: 10.1016/S0196-9781(02)00057-8 |
0.807 |
|
| 2002 |
Hirakura Y, Carreras I, Sipe JD, Kagan BL. Channel formation by serum amyloid A: a potential mechanism for amyloid pathogenesis and host defense. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 9: 13-23. PMID 12000193 DOI: 10.3109/13506120209072440 |
0.553 |
|
| 2001 |
Kagan BL, Hirakura Y, Azimov R, Azimova R. The channel hypothesis of Huntington's disease. Brain Research Bulletin. 56: 281-4. PMID 11719262 DOI: 10.1016/S0361-9230(01)00654-2 |
0.635 |
|
| 2001 |
Hirakura Y, Kagan BL. Pore formation by beta-2-microglobulin: a mechanism for the pathogenesis of dialysis associated amyloidosis. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 8: 94-100. PMID 11409039 DOI: 10.3109/13506120109007350 |
0.453 |
|
| 2000 |
Hirakura Y, Yiu WW, Yamamoto A, Kagan BL. Amyloid peptide channels: blockade by zinc and inhibition by Congo red (amyloid channel block). Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 7: 194-9. PMID 11019860 DOI: 10.3109/13506120009146834 |
0.573 |
|
| 2000 |
Hirakura Y, Azimov R, Azimova R, Kagan BL. Polyglutamine-induced ion channels: a possible mechanism for the neurotoxicity of Huntington and other CAG repeat diseases. Journal of Neuroscience Research. 60: 490-4. PMID 10797551 DOI: 10.1002/(SICI)1097-4547(20000515)60:4<490::AID-JNR7>3.0.CO;2-9 |
0.532 |
|
| 2000 |
Chen QS, Kagan BL, Hirakura Y, Xie CW. Impairment of hippocampal long-term potentiation by Alzheimer amyloid beta-peptides. Journal of Neuroscience Research. 60: 65-72. PMID 10723069 DOI: 10.1002/(Sici)1097-4547(20000401)60:1<65::Aid-Jnr7>3.0.Co;2-Q |
0.346 |
|
| 1999 |
Sokolov Y, Mirzabekov T, Martin DW, Lehrer RI, Kagan BL. Membrane channel formation by antimicrobial protegrins. Biochimica Et Biophysica Acta. 1420: 23-9. PMID 10446287 DOI: 10.1016/S0005-2736(99)00086-3 |
0.817 |
|
| 1999 |
Hirakura Y, Lin MC, Kagan BL. Alzheimer amyloid abeta1-42 channels: effects of solvent, pH, and Congo Red. Journal of Neuroscience Research. 57: 458-66. PMID 10440895 DOI: 10.1002/(SICI)1097-4547(19990815)57:4<458::AID-JNR5>3.0.CO;2-4 |
0.572 |
|
| 1999 |
Schendel SL, Azimov R, Pawlowski K, Godzik A, Kagan BL, Reed JC. Ion channel activity of the BH3 only Bcl-2 family member, BID. The Journal of Biological Chemistry. 274: 21932-6. PMID 10419515 DOI: 10.1074/jbc.274.31.21932 |
0.526 |
|
| 1999 |
Koo SP, Bayer AS, Kagan BL, Yeaman MR. Membrane permeabilization by thrombin-induced platelet microbicidal protein 1 is modulated by transmembrane voltage polarity and magnitude. Infection and Immunity. 67: 2475-81. PMID 10225910 DOI: 10.1128/Iai.67.5.2475-2481.1999 |
0.511 |
|
| 1999 |
Mirzabekov TA, Silberstein AY, Kagan BL. Use of planar lipid bilayer membranes for rapid screening of membrane active compounds. Methods in Enzymology. 294: 661-74. PMID 9916254 DOI: 10.1016/S0076-6879(99)94038-7 |
0.787 |
|
| 1998 |
Hirakura Y, Satoh Y, Hirashima N, Suzuki T, Kagan BL, Kirino Y. Membrane perturbation by the neurotoxic Alzheimer amyloid fragment beta 25-35 requires aggregation and beta-sheet formation. Biochemistry and Molecular Biology International. 46: 787-94. PMID 9844740 DOI: 10.1080/15216549800204332 |
0.431 |
|
| 1998 |
Shang ES, Skare JT, Exner MM, Blanco DR, Kagan BL, Miller JN, Lovett MA. Isolation and characterization of the outer membrane of Borrelia hermsii. Infection and Immunity. 66: 1082-91. PMID 9488399 DOI: 10.1128/Iai.66.3.1082-1091.1998 |
0.475 |
|
| 1998 |
Mirzabekov TA, Silberstein AY, Hirakura Y, Kagan BL. A low volume, high resolution perfusion chamber for planar lipid bilayer membranes Seibutsu Butsuri. 38: 217-222. DOI: 10.2142/Biophys.38.217 |
0.445 |
|
| 1997 |
Skare JT, Mirzabekov TA, Shang ES, Blanco DR, Erdjument-Bromage H, Bunikis J, Bergström S, Tempst P, Kagan BL, Miller JN, Lovett MA. The Oms66 (p66) protein is a Borrelia burgdorferi porin. Infection and Immunity. 65: 3654-61. PMID 9284133 DOI: 10.1128/Iai.65.9.3654-3661.1997 |
0.729 |
|
| 1997 |
Sellman BR, Kagan BL, Tweten RK. Generation of a membrane-bound, oligomerized pre-pore complex is necessary for pore formation by Clostridium septicum alpha toxin. Molecular Microbiology. 23: 551-8. PMID 9044288 DOI: 10.1046/J.1365-2958.1997.D01-1876.X |
0.406 |
|
| 1997 |
Lin MC, Mirzabekov T, Kagan BL. Channel formation by a neurotoxic prion protein fragment. The Journal of Biological Chemistry. 272: 44-7. PMID 8995224 DOI: 10.1074/jbc.272.1.44 |
0.813 |
|
| 1997 |
Lin MC, Kagan BL. Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP-(1-40)] in bilayer membranes - Zn 2+ interaction with Alzheimer amyloid β-protein calcium channels Chemtracts. 10: 251-254. |
0.444 |
|
| 1996 |
Skare JT, Champion CI, Mirzabekov TA, Shang ES, Blanco DR, Erdjument-Bromage H, Tempst P, Kagan BL, Miller JN, Lovett MA. Porin activity of the native and recombinant outer membrane protein Oms28 of Borrelia burgdorferi. Journal of Bacteriology. 178: 4909-18. PMID 8759855 DOI: 10.1128/Jb.178.16.4909-4918.1996 |
0.753 |
|
| 1996 |
Mirzabekov TA, Lin MC, Kagan BL. Pore formation by the cytotoxic islet amyloid peptide amylin. The Journal of Biological Chemistry. 271: 1988-92. PMID 8567648 DOI: 10.1074/jbc.271.4.1988 |
0.815 |
|
| 1995 |
Skare JT, Shang ES, Foley DM, Blanco DR, Champion CI, Mirzabekov T, Sokolov Y, Kagan BL, Miller JN, Lovett MA. Virulent strain associated outer membrane proteins of Borrelia burgdorferi. The Journal of Clinical Investigation. 96: 2380-92. PMID 7593626 DOI: 10.1172/Jci118295 |
0.738 |
|
| 1995 |
Baldwin RL, Mirzabekov T, Kagan BL, Wisnieski BJ. Conformation and ion channel activity of lymphotoxin at neutral and low pH. Journal of Immunology (Baltimore, Md. : 1950). 154: 790-8. PMID 7529287 |
0.766 |
|
| 1994 |
Kagan BL, Sokolov Y. Use of lipid bilayer membranes to detect pore formation by toxins. Methods in Enzymology. 235: 691-705. PMID 7520122 DOI: 10.1016/0076-6879(94)35182-1 |
0.494 |
|
| 1994 |
Mirzabekov T, Lin MC, Yuan WL, Marshall PJ, Carman M, Tomaselli K, Lieberburg I, Kagan BL. Channel formation in planar lipid bilayers by a neurotoxic fragment of the beta-amyloid peptide. Biochemical and Biophysical Research Communications. 202: 1142-8. PMID 7519420 DOI: 10.1006/bbrc.1994.2047 |
0.761 |
|
| 1994 |
Kagan BL, Ganz T, Lehrer RI. Defensins: a family of antimicrobial and cytotoxic peptides. Toxicology. 87: 131-49. PMID 7512758 DOI: 10.1016/0300-483X(94)90158-9 |
0.518 |
|
| 1993 |
Kagan BL, Mirzabekov T, Munoz D, Baldwin RL, Wisnieski B. The role of channel formation in the mechanism of action of tumor necrosis factors. Annals of the New York Academy of Sciences. 707: 317-27. PMID 9137562 DOI: 10.1111/J.1749-6632.1993.Tb38062.X |
0.718 |
|
| 1993 |
Ballard J, Sokolov Y, Yuan WL, Kagan BL, Tweten RK. Activation and mechanism of Clostridium septicum alpha toxin. Molecular Microbiology. 10: 627-34. PMID 7968539 DOI: 10.1111/J.1365-2958.1993.Tb00934.X |
0.474 |
|
| 1992 |
Kagan BL, Baldwin RL, Munoz D, Wisnieski BJ. Formation of ion-permeable channels by tumor necrosis factor-alpha. Science (New York, N.Y.). 255: 1427-30. PMID 1371890 DOI: 10.1126/Science.1371890 |
0.555 |
|
| 1991 |
Kagan BL. Inositol 1,4,5-trisphosphate directly opens diphtheria toxin channels. Biochimica Et Biophysica Acta. 1069: 145-50. PMID 1932055 DOI: 10.1016/0005-2736(91)90116-P |
0.446 |
|
| 1991 |
Krantz DD, Zidovetzki R, Kagan BL, Zipursky SL. Amphipathic beta structure of a leucine-rich repeat peptide. The Journal of Biological Chemistry. 266: 16801-7. PMID 1715870 |
0.308 |
|
| 1990 |
Kagan BL, Selsted ME, Ganz T, Lehrer RI. Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proceedings of the National Academy of Sciences of the United States of America. 87: 210-4. PMID 1688654 DOI: 10.1073/Pnas.87.1.210 |
0.633 |
|
| 1984 |
Kagan BL, Reich KA, Collier RJ. Orientation of the diphtheria toxin channel in lipid bilayers. Biophysical Journal. 45: 102-4. PMID 19431527 DOI: 10.1016/S0006-3495(84)84126-0 |
0.657 |
|
| 1983 |
Kagan BL. Mode of action of yeast killer toxins: channel formation in lipid bilayer membranes. Nature. 302: 709-11. PMID 6300695 DOI: 10.1038/302709A0 |
0.625 |
|
| 1982 |
Kagan BL, Pollard HB, Hanna RB. Induction of ion-permeable channels by the venom of the fanged bloodworm Glycera dibranchiata. Toxicon : Official Journal of the International Society On Toxinology. 20: 887-93. PMID 6294921 DOI: 10.1016/0041-0101(82)90076-9 |
0.568 |
|
| 1982 |
Misler S, Kagan BL, Finkelstein A. Single channel conductances formed by diphtheria toxin fragments in planar bilayers Biophysical Journal. 37: 323a. |
0.765 |
|
| 1981 |
Kagan BL, Finkelstein A, Colombini M. Diphtheria toxin fragment forms large pores in phospholipid bilayer membranes. Proceedings of the National Academy of Sciences of the United States of America. 78: 4950-4. PMID 6272284 DOI: 10.1073/Pnas.78.8.4950 |
0.65 |
|
| 1981 |
Weaver CA, Kagan BL, Finkelstein A, Konisky J. Mode of action of colicin ib: formation of ion-permeable membrane channels. Biochimica Et Biophysica Acta. 645: 137-42. PMID 6266474 DOI: 10.1016/0005-2736(81)90521-6 |
0.698 |
|
| 1978 |
Schein SJ, Kagan BL, Finkelstein A. Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes. Nature. 276: 159-63. PMID 740032 DOI: 10.1038/276159a0 |
0.698 |
|
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