Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Mark I. Mosevitsky"'
Publikováno v:
Biochemical and biophysical research communications. 616
Earlier it was shown that a group of extracellular low-specific metallopeptidases is present in the mammalian brain Kropotova and Mosevitsky (2016) [1]. These enzymes are weakly connected to the axonal ends of neurons. They were named Neuron bound Ex
Publikováno v:
Bioorganic & Medicinal Chemistry. 28:115184
The main obstacle to the use of many therapeutic peptides in practice is their rapid destruction by extracellular peptidases. Earlier we have found that active in the extracellular medium of mammalian brain exopeptidases are unable to break the bonds
Publikováno v:
Neurochemical research. 41(10)
We have found that isolated from mammalian brain (rat, bovine) axonal endings (synaptosomes) degrade peptides of different composition. With the use of low concentration of non ionic detergent Triton X-100 (0.05-0.1 %) four low specific metallopeptid
Autor:
Mark I. Mosevitsky, Inga Silicheva
Publikováno v:
Acta Histochemica. 113:13-18
Proteins BASP1 and MARCKS are abundant in axonal endings of neurons. Similarly to brain-specific protein GAP-43, BASP1 and MARCKS are reversibly bound to the plasma membrane. These proteins control both actin polymerization and actin cytoskeleton bin
Publikováno v:
FEBS Journal. 278:461-469
BASP1 (also known as CAP-23 and NAP-22) is a brain abundant myristoylated protein localized at the inner surface of the presynaptic plasma membrane. Emerging evidence suggests that BASP1 is critically involved in various cellular processes, in partic
Autor:
Vera Novitskaya, Mark I. Mosevitsky, Marina N. Bogdanova, Ekaterina S. Kropolova, Vladislav V. Zakharov, Jean-Paul Capony, Jean Derancourt
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1622:14-19
BASP1 (also known as CAP-23 and NAP-22) is a novel myristoylated calmodulin-binding protein, abundant in nerve terminals. It is considered as a signal protein participating in neurite outgrowth and synaptic plasticity. BASP1 is also present in signif
Autor:
Vlad V. Zakharov, Mark I. Mosevitsky
Publikováno v:
Neuroscience Research. 39:447-453
GAP-43 is a presynaptic protein participating in signal transduction processes in nerve terminals. GAP-43 exists in neurons along with two truncated forms devoid of 4 and 40 N-terminal residues. In this report, we show that these forms of GAP-43 are
Publikováno v:
Neuroscience Letters. 297:49-52
The participation of the nerve termini growth associated protein GAP-43 in neurite outgrowth and targeting is well documented. Commonly, besides GAP-43 itself, two big fragments devoid of four (GAP-43-2, IB-50) and of about 40 (GAP-43-3, B-60) N-term
Autor:
Mark I. Mosevitsky, V.V. Zakharov, J.P. Capony, A. Yu. Plekhanov, Vera Novitskaya, G. Yu. Skladchikova
Publikováno v:
Biochimie. 79:373-384
Proteins BASP1 and GAP-43/B-50, which are abundant in nerve endings, show a number of similar physico-chemical properties. Nevertheless, they belong to different protein families. In this work, complete amino acid sequences of bovine BASP1 and human
Publikováno v:
Neurochemical research. 38(6)
Protein BASP1 was discovered in brains of mammals and birds. In presynaptic area of synapses, BASP1 is attached to plasma membrane owing to N-terminal myristoylation as well as to the positively charged “effecter domain”. BASP1 interactions with