Aleksey Lomakin

Summary

Affiliation: Massachusetts Institute of Technology
Country: USA

Publications

  1. ncbi request reprint Quasielastic light scattering study of amyloid beta-protein fibril formation
    Aleksey Lomakin
    Department of Physics and Center for Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
    Protein Pept Lett 13:247-54. 2006
  2. pmc Serum protein profiles predict coronary artery disease in symptomatic patients referred for coronary angiography
    William A LaFramboise
    University of Pittsburgh, Department of Pathology, 5230 Centre Avenue, Pittsburgh, PA 15232, USA
    BMC Med 10:157. 2012
  3. doi request reprint Quasielastic light scattering study of amyloid β-protein fibrillogenesis
    Aleksey Lomakin
    Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA, USA
    Methods Mol Biol 849:69-83. 2012
  4. pmc Phase behavior of mixtures of human lens proteins Gamma D and Beta B1
    Ying Wang
    Materials Processing Center, Department of Physics, and Center for Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 107:13282-7. 2010
  5. doi request reprint Phase transitions in human IgG solutions
    Ying Wang
    Materials Processing Center, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA
    J Chem Phys 139:121904. 2013
  6. pmc Altered phase diagram due to a single point mutation in human gammaD-crystallin
    Jennifer J McManus
    Materials Processing Center, Department of Physics, and Center for Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 104:16856-61. 2007
  7. pmc Pathological crystallization of human immunoglobulins
    Ying Wang
    Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 109:13359-61. 2012
  8. pmc Thickness-radius relationship and spring constants of cholesterol helical ribbons
    Boris Khaykovich
    Nuclear Reactor Laboratory, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 106:15663-6. 2009
  9. ncbi request reprint Quasielastic light scattering for protein assembly studies
    Aleksey Lomakin
    Department of Physics and Center for Materials Sciences and Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA
    Methods Mol Biol 299:153-74. 2005
  10. pmc Phase separation in solutions of monoclonal antibodies and the effect of human serum albumin
    Ying Wang
    Materials Processing Center, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 108:16606-11. 2011

Collaborators

Detail Information

Publications18

  1. ncbi request reprint Quasielastic light scattering study of amyloid beta-protein fibril formation
    Aleksey Lomakin
    Department of Physics and Center for Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
    Protein Pept Lett 13:247-54. 2006
    ..We illustrate practical applications of QLS with examples from studies of fibril formation of the amyloid beta-protein...
  2. pmc Serum protein profiles predict coronary artery disease in symptomatic patients referred for coronary angiography
    William A LaFramboise
    University of Pittsburgh, Department of Pathology, 5230 Centre Avenue, Pittsburgh, PA 15232, USA
    BMC Med 10:157. 2012
    ....
  3. doi request reprint Quasielastic light scattering study of amyloid β-protein fibrillogenesis
    Aleksey Lomakin
    Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA, USA
    Methods Mol Biol 849:69-83. 2012
    ..We illustrate here how QLS has been applied to elucidate features of the oligomerization and fibrillogenesis of the amyloid β-protein, Aβ, thought to be the causative agent of Alzheimer's disease...
  4. pmc Phase behavior of mixtures of human lens proteins Gamma D and Beta B1
    Ying Wang
    Materials Processing Center, Department of Physics, and Center for Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 107:13282-7. 2010
    ..Our findings provide insight into the factors essential for maintaining lens proteins in a single homogeneous phase, thereby enabling lens transparency...
  5. doi request reprint Phase transitions in human IgG solutions
    Ying Wang
    Materials Processing Center, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA
    J Chem Phys 139:121904. 2013
    ..The investigation of the phase diagram of IgG solutions is of great importance for the understanding of immunoglobulin deposition diseases as well as for the understanding of the colloidal stability of IgG pharmaceutical formulations...
  6. pmc Altered phase diagram due to a single point mutation in human gammaD-crystallin
    Jennifer J McManus
    Materials Processing Center, Department of Physics, and Center for Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 104:16856-61. 2007
    ....
  7. pmc Pathological crystallization of human immunoglobulins
    Ying Wang
    Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 109:13359-61. 2012
    ..Remarkably, the crystallization can occur at quite low concentrations. This suggests that, even within the regular immune response to infections, cryoprecipitation of Ig can be possible...
  8. pmc Thickness-radius relationship and spring constants of cholesterol helical ribbons
    Boris Khaykovich
    Nuclear Reactor Laboratory, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 106:15663-6. 2009
    ....
  9. ncbi request reprint Quasielastic light scattering for protein assembly studies
    Aleksey Lomakin
    Department of Physics and Center for Materials Sciences and Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA
    Methods Mol Biol 299:153-74. 2005
    ..We use examples from studies of Abeta fibrillogenesis to illustrate QLS application for understanding the molecular mechanisms of the nucleation and growth of amyloid fibrils...
  10. pmc Phase separation in solutions of monoclonal antibodies and the effect of human serum albumin
    Ying Wang
    Materials Processing Center, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 108:16606-11. 2011
    ..Our findings are relevant to understanding the stability of pharmaceutical solutions of antibodies and the mechanisms of cryoglobulinemia...
  11. ncbi request reprint Quantitative Evaluation of Colloidal Stability of Antibody Solutions using PEG-Induced Liquid-Liquid Phase Separation
    Ying Wang
    Materials Processing Center, Department of Physics, and Center for Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States
    Mol Pharm 11:1391-402. 2014
    ..This binding energy is a measure of attractive interactions between antibody molecules and can be used for quantitative characterization of the colloidal stability of antibody solutions. ..
  12. pmc Structure determination of micelle-like intermediates in amyloid beta -protein fibril assembly by using small angle neutron scattering
    Winnie Yong
    Department of Physics, Center for Materials Science and Engineering, and Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139 4307, USA
    Proc Natl Acad Sci U S A 99:150-4. 2002
    ..The concentration independence of the length of the cylindrical aggregate indicates the presence of an internal nonrepetitive structure that spans the entire length of the Abeta assembly...
  13. pmc Structure of cholesterol helical ribbons and self-assembling biological springs
    Boris Khaykovich
    Nuclear Reactor Laboratory, Massachusetts Institute of Technology, 138 Albany Street, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 104:9656-60. 2007
    ..We discuss possible origins for this triplication as well as the connection between the crystalline structure and the geometrical form of the helical ribbons...
  14. pmc Liquid-solid transition in nuclei of protein crystals
    Aleksey Lomakin
    Department of Physics, Center for Materials Science and Engineering and Material Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139 4307, USA
    Proc Natl Acad Sci U S A 100:10254-7. 2003
    ..A nucleus first forms and grows as a disordered, liquid-like aggregate. Once the aggregate grows beyond a critical size (about a few hundred particles) crystal nucleation becomes possible...
  15. pmc Effect of polyethylene glycol on the liquid-liquid phase transition in aqueous protein solutions
    Onofrio Annunziata
    Department of Physics, Center for Materials Science and Engineering, and Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139 4307, USA
    Proc Natl Acad Sci U S A 99:14165-70. 2002
    ..Finally, we show that the increase of the LLPS temperature with PEG concentration is due to attractive protein-protein interactions...
  16. pmc Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleus
    Marianne A Grant
    Division of Molecular and Vascular Medicine, Beth Israel Deaconess Medical Center, and Department of Medicine, Harvard Medical School, Boston, MA 02215, USA
    Proc Natl Acad Sci U S A 104:16522-7. 2007
    ..The implications of these findings for understanding Abeta monomer folding and disease causation are discussed...
  17. pmc Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
    Gal Bitan
    Center for Neurologic Diseases, Brigham and Women s Hospital, Boston, MA 02115, USA
    Proc Natl Acad Sci U S A 100:330-5. 2003
    ..The strong etiologic association of Abeta42 with AD may thus be a result of assemblies formed at the earliest stages of peptide oligomerization...
  18. pmc C-terminal peptides coassemble into Abeta42 oligomers and protect neurons against Abeta42-induced neurotoxicity
    Erica A Fradinger
    Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA
    Proc Natl Acad Sci U S A 105:14175-80. 2008
    ..Thus, Abeta(31-42) and Abeta(39-42) are leads for obtaining mechanism-based drugs for treatment of AD using a systematic structure-activity approach...