Alexei R. Koudinov koudin at IMB.IMB.AC.RU
Sun Jun 23 15:24:10 EST 1996

        Dear Amyloid/Ageing subscribers:
        I began to study Alzheimer's amyloid beta (Ab) protein in 1992, at
the time when it was becoming clear that this protein exists normally in a
soluble form (soluble Ab) and that it is not just a pathological protein. My
research activities yielded an on-going project, devoted to understanding in
more detail the normal biology of amyloid beta. Understanding the normal
biology of Ab would answer the questions of why soluble Ab does not undergo
fibrillogenesis in biological fluids but does polymerize into amyloid
fibrils in the disease, and what the biological consequences of Ab
deposition within the brain tissue are. This, in turn, would be crucial for
understanding the pathophysiology of Alzheimer's disease and for delineating
pathologically grounded new approaches to therapy. 
        My current postdoctoral position at NYU Medical Center  just
expired. Thus, to continue my research I have to find another position. I
would be happy to continue my research as a part of your Department/
University/ Center, if you might wish to consider such a possibility.

Sincerely Yours,

Alexei R. Koudinov, M.D., Ph.D.

P.S. My CV is available in David Small (special thanks to him for this
possibility) WEB site  under JOB CORNER. 

Alexei Koudinov PUBLICATIONS:

		KUDINOV, Alexei R., Bronstein, Igor B., Gabibov, Alexander G. and
Gololobov, Gennady V. (1992) Two subforms of eukaryotic topoisomerase I:
Purification and structure-function relationship. FEBS Lett  314: 267-270.

		Tkachenko, Andrei V., Starkov, Ivan V., Shuster, Alexander M., KOUDINOV,
Alexei R., Zakharov, Sergei F., Shishkin, Sergei S., Mordovtsev, Vladimir
N., and Kisselev, Lev, L. (1992) Autoimmune reaction  in psoriatic skin. In
Proceedings of the conference "Modern Enzymology: problems and trends".

		Ghiso, Jorge, Matsubara, Etsuro, KOUDINOV, Alexei, ChoiMiura,  Nam Ho,
Tomita, Motono, Wisniewski, Thomas, Frangione, Blas. (1993). The
cerebrospinal fluid soluble form of Alzheimer's amyloid beta is complexed to
SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack
complex. Biochem J 293: 2730.

		KOUDINOV, Alexei, Matsubara, Etsuro, Frangione, Blas, Ghiso, Jorge.
(1994). The Soluble Form of Alzheimer's Amyloid Beta Protein is Complexed to
High Density Lipoprotein 3 and Very High Density Lipoprotein in Normal Human
Plasma Biochem Biophys Res Commun 205: 1164-1171.

		Tomlinson, Stephen, Jansen, Ana-Maria, KOUDINOV, Alexei, Ghiso, Jorge,
Choi-Miura, Nam-ho, Rifkin, Mary, Ohtaki, Sachiya, and Nussenzweig, Victor.
(1995) High-density-lipoprotein-independent  killing of Trypanosoma brucei
by human serum. Molecular and Biochemical Parasitology 70: 131-138. 

		KOUDINOV, Alexei, R., Koudinova, Natalia, V., and Berezov, Temirbolat, T.
(1996). Alzheimer's peptides Ab1-40 and Ab1-28 inhibit the plasma
cholesterol esterification rate. Biochem Mol Biol Internat. 38(4): 747-752.

		KOUDINOV, Alexei, R., Berezov, Temirbolat, T., and Koudinova, Natalia, V.
Multiple inhibitory effects of Alzheimer's peptide Ab1-40 on lipid
byosynthesis in cultured human HepG2 cells. In press. (SEE ABSTRACT BELOW)   

		KOUDINOV, Alexei, R., Koudinova, Natalia, V., Kumar, Asok, Beavis, Ronald,
and Ghiso, Jorge. (1996) Biochemical Biophysical Research Communication.
Biochemical characterization of Alzheimer's soluble amyloid beta protein in
human cerebrospinal fluid: association with high density lipoproteins.
Biochem Biophys Res Commun. In Press. (SEE ABSTRACT BELOW)


		KOUDINOV, Alexei, R., Koudinova, Natalia, V., Kumar, Asok. Is amyloid beta
an apolipoprotein?  New York University Medical Center Neuroscience Meeting.
New York. December 1995. 		

		KOUDINOV, Alexei, R., Koudinova, Natalia, V., Kumar, Asok, Beavis, Ronald,
and Ghiso, Jorge. Alzheimer's soluble amyloid beta protein is associated
with high density lipoproteins in normal human cerebrospinal fluid and is
secreted by HepG2 cells as a part of lipoprotein complexes. Society for
Neuroscience Annual Meeting. Washington, DC, 1996. Submitted. (SEE ABSTRACT


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