I think we're not allowed to put PDFs on the web, but if you send an e-mail request for a reprint (andrei@uconn.edu), you should get it in 2-3 days. We write them so that people will read them!
Legend: Underlined = correponding author
* - more than 50 citations
** - more than 100 citations
------------------------------------------------------------------------------------------------------------------------------------
Publications (last updated 9/13/07)
1) Matousek, W.M., Ciani, B., Fitch, C.A., Garcia-Moreno E., B., Kammerer, R.A.
& Alexandrescu, A.T. (2007) “Electrostatic contributions to
the stability of the GCN4 leucine zipper structure”, J Mol Biol, in
press.http://dx.doi.org/10.1016/j.jmb.2007.09.007
2) Sallum, C.O., Kammerer, R.A., & Alexandrescu, A.T. (2007) “Thermodynamic and structural studies of carbohydrate binding by the agrin-G3 domain”, Biochemistry, 46, 9541-9550.
3) Watson, E., Matousek, W.M., Irimies, E.L. & Alexandrescu, A.T. (2007) “Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins”, Biochemistry, 46, 9484-9494.
4) Steinmetz, M.O, Jelesarov, I., Matousek, W.M., Honnappa, S., Jahnke, W., Missimer, J.H., Frank, S., Alexandrescu, A.T. & Kammerer, R.A. (2007) “Molecular basis of coiled coil formation”. Proc. Natl. Acad., USA. 104, 7062-7067.
5) Ucci, J.W., Kobayashi, Y., Choi, G. & Alexandrescu, A.T., Cole, J.L. (2007) “Mechanism of interaction of the double-stranded RNA (dsRNA) binding domain of protein kinase R with short dsRNA sequences”. Biochemistry 46, 55-65.
6) Sallum, C.O., Martel, D.M., Fournier, R.S., Matousek, W.M & Alexandrescu, A.T. (2005) “Sensitivity of NMR residual dipolar couplings to perturbations in folded and unfolded staphylococcal nuclease”. Biochemistry 44, 6392-6403.
7 ) Alexandrescu, A.T. (2005) “Amyloid accomplices and enforcers”.
Protein Science 14, 1-12.
8) Matousek, W.M., & Alexandrescu, A.T. (2004) “NMR structure
of the C-terminal domain of SecA in the free state”. Biochem. Biophys.
Acta 1702, 163-171.
9) Alexandrescu, A.T. (2004) “Strategy for supplementing structure
calculations using limited data with hydrophobic distance restraints”.
Proteins 56, 117-129.
10 ) Stetefeld, J., Alexandrescu A. T., Maciejewski, M. W., Jenny,
M., Rathgeb-Szabo, K., Schulthess, T., Landwehr, R., Frank, S., Ruegg, M.A.,
& Kammerer, R.A. (2004) "Modulation of agrin function by alternative
splicing and Ca2+ binding". Structure 12, 503-515.
11 ) Alexandrescu, A.T., & Kammerer, R.A. (2003) “Structure
and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings”.
Protein Sci. 12, 2132-2140.
12 ) Alexandrescu, A.T., Snyder, D.R., & Abildgaard, F. (2001) “NMR
of hydrogen bonding in cold shock protein A and an analysis of the influence
of crystallographic resolution on comparisons of hydrogen bond lengths”.
Protein Sci. 10, 1856-1868.
13 ) Alexandrescu, A.T., Maciejewski, M.W., Rüegg, M.A., Engel,
J., & Kammerer, R.A. (2001) “1H, 13C and 15N backbone assignments
for the C-terminal globular domain of agrin”. J. Biomol. NMR 20, 295-296.
14 ) Jaravine, V.A., Alexandrescu A. T., & Grzesiek, S. (2001)
"Observation of the closing of individual hydrogen bonds during TFE-induced
helix formation in a peptide". Protein Science 10, 943-950.
15) Kammerer, R.A., Jaravine, V.A., Frank, S., Schulthess, T., Landwehr, R.,
Lustig, A., Garcia-Echeveria, C., Alexandrescu, A.T., Engel, J., & Steinmetz,
M.O. (2001) "An interhelical salt bridge within the trigger site stabilizes
the GCN4 leucine zipper". J. Biol. Chem. 276, 13685-13688.
16) Alexandrescu, A.T. (2001) "An NMR-based quenched hydrogen exchange
investigation of model amyloid fibrils formed by the protein CspA". Pac.
Symp. Biocomput. 6, 67-78.
17) Alexandrescu, A.T., Jaravine, V.A., & Lamour, F.P. (2000) "NMR
evidence for progressive stabilization of native-like structure upon aggregation
of acid denatured LysN". J. Mol. Biol. 295, 239-255.
18) Jaravine, V.A., Rathgeb-Szabo, K., & Alexandrescu, A.T. (2000)
"Microscopic stability of cold shock protein A examined by NMR native state
hydrogen exchange as a function of urea and trimethylamine N-oxide". Protein
Science 9, 290-301.
19) Alexandrescu, A.T., & Rathgeb-Szabo, K. (1999) "An NMR investigation
of solution aggregation reactions preceding the misassembly of acid denatured
cold shock protein A into fibrils". J. Mol. Biol. 291, 1191-1206.
20) Alexandrescu, A.T., Jaravine, V.A., Dames, S.A. & Lamour, F.P.
(1999) "NMR hydrogen exchange of the OB-fold protein LysN as a function
of denaturant: The most conserved elements of structure are the most stable
to unfolding". J. Mol. Biol. 289, 1041-1054.
21 ) Dames, S.A., Kammerer, Moskau, D., Engel, J. & Alexandrescu, A.T.
(1999) "Contributions of the ionization states of acidic residues to the
stability of the coiled coil domain of matrilin-1". FEBS Lett. 446, 75-80.
22 ) Dames, S.A., Wiltscheck, R., Kammerer, R.A., Engel, J., & Alexandrescu,
A.T. (1998) "NMR structure of a parallel homotrimeric coiled coil".
Nature Struct. Biol. 5, 687-691.
23 ) Alexandrescu, A.T., & Rathgeb-Szabo, K. (1998) "NMR assignments
for acid-denatured cold shock protein A". J. Biomol. NMR 11, 461-462.
24 ) Alexandrescu, A.T., Rathgeb-Szabo, K., Rumpel, K., Jahnke, W., Schulthess,
T., & Kammerer, R.A. (1998) "15N backbone dynamics of the S-Peptide
from Ribonuclease A in its free and S-Protein bound forms: Towards a site-specific
analysis of entropy changes upon folding". Protein Science 7, 389-402.
25) Wiltscheck, R., Kammerer, R.A., Dames, S.A., Schulthess, T., Blommers, M.J.J.,
Engel, J., & Alexandrescu, A.T. (1997) "Heteronuclear NMR assignments
and secondary structure of the coiled coil trimerization domain from cartilage
matrix protein in oxidized and reduced forms". Protein Science 6, 1734-1745.
26) Alexandrescu, A.T., Dames, S.A., & Wiltscheck, R. (1996) "A
fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange
protection factors in the range reported for 'Molten Globules'". Protein
Science 5, 1942-1946.
27) Alexandrescu, A.T., Jahnke, W., Wiltscheck, R., & Blommers, M.J.J
(1996) "Accretion of structure in staphylococcal nuclease: An 15N NMR relaxation
study". J. Mol. Biol. 260, 570-587.
28) Alexandrescu, A. T., Gittis, A., Abeygunawardana, C., & Shortle,
D. (1995) “NMR structure of a stable "OB-fold" sub-domain isolated
from staphylococcal nuclease”. J. Mol. Biol. 250, 134-143.
29) Wang, Y., Alexandrescu, A. T., & Shortle, D. (1995) “Initial studies
of the equilibrium folding pathway of staphylococcal nuclease”. Philos.
Trans. R. Soc. Lond. B Biol. Sci. 348, 27-34.
* 30) Alexandrescu, A. T., & Shortle, D. (1994)
“Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal
nuclease”. J. Mol. Biol. 242, 527-546.
** 31) Alexandrescu, A. T., Abeygunawardana, C.,
& Shortle, D. (1994) “Structure and dynamics of a denatured 131-residue
fragment of staphylococcal nuclease: A heteronuclear NMR study”. Biochemistry
33, 1063-1072.
32 ) Smith, L., Alexandrescu, A. T., Pitkeathly, M. & Dobson, C. M. (1994)
“Solution structure of a peptide fragment of human alpha-lactalbumin in
trifluoroethanol: a model for local structure in the molten globule”.
Structure 2, 703-712.
**33) Alexandrescu, A. T., Ng, Y-L., & Dobson,
C. M. (1994) “Characterization of a TFE-induced partially folded state
of alpha-lactalbumin”. J. Mol. Biol. 235, 587-599.
** 34) Alexandrescu, A. T., Evans, P. A., Pitkeathly,
M., & Dobson, C. M. (1993) “Structure and dynamics of the acid-denatured
molten globule state of alpha-lactalbumin: A two-dimensional NMR study”.
Biochemistry 32, 1707-1718.
35) Alexandrescu, A. T., Broadhurst, W., Wormald, C., Chyan, C.-L., Baum, J.,
& Dobson, C. M. (1992) “1H-NMR assignments and local environments
of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin”.
European Journal of Biochemistry 210, 699-709.
36) Alexandrescu, A. T., Drendel, W. & Sundaralingam, M. (1991) “A
highly propeller twisted adenine-adenine base pair in 8-tertiary butyl adenine”.
Acta Crystallographica C47, 1041-1044.
37) Alexandrescu, A. T., Loh, S. N., & Markley, J. L. (1990) “Chemical
exchange spectroscopy based on carbon-13 NMR. Applications to enzymology and
protein folding”. Journal of Magnetic Resonance 87, 523-535.
38) Markley, J. L., Seavey, B. R., Alexandrescu, A. T., Darba, P., Hinck, A.
P., Loh, S. N., McNemar, C. W., Mooberry, E. S., Oh, B. H., et al. (1990) “Multinuclear
magnetic resonance spectroscopy of proteins: Information content, data extraction
and analysis, and database design”. Protein Eng. Proc. Int. Conf. Protein
Eng. Editor: Ikehara, M., 285-290.
* 39) Alexandrescu, A. T., Hinck, A. P. & Markley,
J. L. (1990) “Coupling between local structure and global stability of
a protein: Mutants of staphylococcal nuclease”. Biochemistry 29, 4516-4525.
40) Alexandrescu, A. T. (1990) “Nuclear magnetic resonance spectroscopy
of staphylococcal nuclease: Effects of solution conditions and sequence changes
on conformational forms”. Ph.D. Thesis, University of Wisconsin-Madison.
* 41) Alexandrescu, A. T., Ulrich, E. L., &
Markley, J. L. (1989) “Hydrogen - 1 NMR evidence for three interconverting
forms of staphylococcal nuclease: Effects of mutations and solution conditions
on their distribution”. Biochemistry 28, 204-212.
42 ) Alexandrescu, A. T., Mills, D. A., Ulrich, E. L., Chinami, M. & Markley,
J. L. (1988) “NMR assignments of the four histidines of staphylococcal
nuclease in native and denatured states”. Biochemistry 27, 2158-2165.
** 43) Barton, J. K., Basile, L. A., Danishefsky,
A., & Alexandrescu, A. (1984) “Chiral probes for the handedness of
DNA helices: Enantiomers of Tris(4,7-diphenyl phenanthroline) Ruthenium(II)”.
Proc. Natl. Acad. Sci. U.S.A. 81, 1961-1965.
in preparation:
44 ) Matousek, W.M., Maciejewski, M.W, Bernado, P., Ciani, B., Blackledge, M.,
Kammerer, R.A. & Alexandrescu, A.T. “Residual structure in
the denatured state of a non-globular protein: the GCN4 leucine zipper”.