Boris Brumshtein
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Explore the profile of Boris Brumshtein including associated specialties, affiliations and a list of published articles.
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19
Citations
462
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Recent Articles
1.
Mulato A, Lansdon E, Aoyama R, Voigt J, Lee M, Liclican A, et al.
Antimicrob Agents Chemother
. 2024 Feb;
68(4):e0137323.
PMID: 38380945
Protease inhibitors (PIs) remain an important component of antiretroviral therapy for the treatment of HIV-1 infection due to their high genetic barrier to resistance development. Nevertheless, the two most commonly...
2.
Prener L, Baszczynski O, Kaiser M, Dracinsky M, Stepan G, Lee Y, et al.
J Med Chem
. 2023 Jan;
66(3):1761-1777.
PMID: 36652602
Non-nucleoside reverse transcriptase inhibitors (NNRTIs) represent cornerstones of current regimens for treatment of human immunodeficiency virus type 1 (HIV-1) infections. However, NNRTIs usually suffer from low aqueous solubility and the...
3.
Brumshtein B, Esswein S, Sawaya M, Rosenberg G, Ly A, Landau M, et al.
J Biol Chem
. 2018 Oct;
293(51):19659-19671.
PMID: 30355736
Systemic light-chain amyloidosis (AL) is a human disease caused by overexpression of monoclonal immunoglobulin light chains that form pathogenic amyloid fibrils. These amyloid fibrils deposit in tissues and cause organ...
4.
Brumshtein B, Esswein S, Salwinski L, Phillips M, Ly A, Cascio D, et al.
Elife
. 2015 Nov;
4:e10935.
PMID: 26576950
Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers...
5.
Brumshtein B, Esswein S, Landau M, Ryan C, Whitelegge J, Phillips M, et al.
J Biol Chem
. 2014 Aug;
289(40):27513-25.
PMID: 25138218
Systemic light chain amyloidosis is a lethal disease characterized by excess immunoglobulin light chains and light chain fragments composed of variable domains, which aggregate into amyloid fibers. These fibers accumulate...
6.
Brumshtein B, Aguilar-Moncayo M, Benito J, Garcia Fernandez J, Silman I, Shaaltiel Y, et al.
Org Biomol Chem
. 2011 Apr;
9(11):4160-7.
PMID: 21483943
Cyclodextrin-based host-guest chemistry has been exploited to facilitate co-crystallization of recombinant human acid β-glucosidase (β-glucocerebrosidase, GlcCerase) with amphiphilic bicyclic nojirimycin analogues of the sp(2)-iminosugar type. Attempts to co-crystallize GlcCerase with...
7.
Brumshtein B, Salinas P, Peterson B, Chan V, Silman I, Sussman J, et al.
Glycobiology
. 2009 Sep;
20(1):24-32.
PMID: 19741058
Gaucher disease, the most common lysosomal storage disease, can be treated with enzyme replacement therapy (ERT), in which defective acid-beta-glucosidase (GlcCerase) is supplemented by a recombinant, active enzyme. The X-ray...
8.
Brumshtein B, Greenblatt H, Futerman A, Silman I, Sussman J
J Appl Crystallogr
. 2009 May;
41(Pt 5):969-971.
PMID: 19461852
Microbatch crystallization under oil is a powerful procedure for obtaining protein crystals. Using this method, aqueous protein solutions are dispensed under liquid oil, and water evaporates through the layer of...
9.
Brumshtein B, Aguilar-Moncayo M, Isabel Garcia-Moreno M, Ortiz Mellet C, Garcia Fernandez J, Silman I, et al.
Chembiochem
. 2009 May;
10(9):1480-5.
PMID: 19437524
No abstract available.
10.
Kacher Y, Brumshtein B, Boldin-Adamsky S, Toker L, Shainskaya A, Silman I, et al.
Biol Chem
. 2008 Sep;
389(11):1361-9.
PMID: 18783340
In mammalian cells, glucosylceramide (GlcCer), the simplest glycosphingolipid, is hydrolyzed by the lysosomal enzyme acid beta-glucosidase (GlcCerase). In the human metabolic disorder Gaucher disease, GlcCerase activity is significantly decreased owing...