A. Alexandrescu

发表

How phage L capsid decoration protein distinguishes between nearly identical binding sites on an icosahedral virion

Kristin N. Parent, S. Casjens, M. Feig, 2018, bioRxiv.

NMR determination of pK a values in a-synuclein

A. Alexandrescu, D. Kendall, Robyn L Croke, 2011 .

NMR assignments for monomeric phage L decoration protein

C. Teschke, Helen B. Belato, Rebecca L Newcomer, 2018, Biomolecular NMR assignments.

NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold

A. R. Kaplan, A. Alexandrescu, S. De, 2017, Scientific Reports.

Relative Stabilities of Conserved and Non-Conserved Structures in the OB-Fold Superfamily

A. Alexandrescu, Kaitlyn M. Guardino, S. R. Sheftic, 2009, International journal of molecular sciences.

NMR assignments for acid–denaturated cold shock protein A

A. Alexandrescu, K. Rathgeb-Szabo, K. Rathgeb‐Szabo, 1998, Journal of biomolecular NMR.

Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.

C M Dobson, C. Dobson, J. Baum, 1993, Biochemistry.

IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies.

A. Alexandrescu, Bibekanand Mallick, S. Jha, 2018, Biochimica et biophysica acta. Biomembranes.

pH dependence of amylin fibrillization.

A. Alexandrescu, Sharadrao M. Patil, S. R. Sheftic, 2014, Biochemistry.

NMR Mapping of Disordered Segments from a Viral Scaffolding Protein Enclosed in a 23 MDa Procapsid.

C. Teschke, A. Alexandrescu, R. Whitehead, 2019, Biophysical journal.

Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling.

M. Baker, W. Chiu, M. Gross, 2014, Structure.

Strategy for supplementing structure calculations using limited data with hydrophobic distance restraints

A. Alexandrescu, 2004, Proteins.

Sensitivity of NMR residual dipolar couplings to perturbations in folded and denatured staphylococcal nuclease.

A. Alexandrescu, Christine O. Sallum, David Martel, 2005, Biochemistry.

Structure-activity relationships of mitochondria-targeted tetrapeptide pharmacological compounds

Eric R. May, A. Alexandrescu, H. Szeto, 2022, eLife.

Mechanism of Amylin Fibrillization Enhancement by Heparin*

A. Alexandrescu, Sharadrao M. Patil, N. Alder, 2011, The Journal of Biological Chemistry.

Quenched Hydrogen Exchange NMR of Amyloid Fibrils.

A. Alexandrescu, 2016, Methods in molecular biology.

NMR assignments for the telokin-like domain of bacteriophage P22 coat protein

C. Teschke, A. Alexandrescu, S. R. Sheftic, 2012, Biomolecular NMR Assignments.

Nuclear magnetic resonance structure and dynamics of the response regulator Sma0114 from Sinorhizobium meliloti.

V. Robinson, A. Alexandrescu, D. Gage, 2012, Biochemistry.

Pulse‐field gradient nuclear magnetic resonance of protein translational diffusion from native to non‐native states

C. Teschke, A. Alexandrescu, R. Whitehead, 2022, Protein science : a publication of the Protein Society.

Hydrogen-1 NMR evidence for three interconverting forms of staphylococcal nuclease: effects of mutations and solution conditions on their distribution [Erratum to document cited in CA110(5):36063b]

E. Ulrich, J. Markley, A. Alexandrescu, 1989 .

NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain

A. R. Kaplan, A. Alexandrescu, R. Olson, 2014, Biomolecular NMR assignments.

NMR Structure and Dynamics of the Response Regulator Sma0114 from Sinorhizobium Meliloti

A. Alexandrescu, S. R. Sheftic, 2013 .

Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper

A. Alexandrescu, S. R. Sheftic, S. Jha, 2012, European Biophysics Journal.

NMR assignments for monomeric phage L decoration protein

C. Teschke, Helen B. Belato, Rebecca L Newcomer, 2018, Biomolecular NMR Assignments.

15N backbone dynamics of the S‐peptide from ribonuclease A in its free and S‐protein bound forms: Toward a site‐specific analysis of entropy changes upon folding

W. Jahnke, R. Kammerer, T. Schulthess, 1998, Protein science : a publication of the Protein Society.

NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.

D. Shortle, A. Gittis, A. Alexandrescu, 1995, Journal of molecular biology.

Structure-Activity Relationships in the Design of Mitochondria-Targeted Peptide Therapeutics

Eric R. May, A. Alexandrescu, H. Szeto, 2021, bioRxiv.

Characterization of a Trifluoroethanol-induced Partially Folded State of α-Lactalbumin

C. Dobson, A. Alexandrescu, Y. Ng, 1994 .

Chiral probes for the handedness of DNA helices: enantiomers of tris(4,7-diphenylphenanthroline)ruthenium(II).

J. Barton, A. Alexandrescu, L. Basile, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Hydrogen exchange of monomeric α‐synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli

A. Alexandrescu, Andrei T Alexandrescu, Eric D Watt, 2008, Protein science : a publication of the Protein Society.

Heterogeneous amylin fibril growth mechanisms imaged by total internal reflection fluorescence microscopy.

A. Alexandrescu, Sharadrao M. Patil, S. Jha, 2011, Biochemistry.

NMR of hydrogen bonding in cold‐shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths

F. Abildgaard, A. Alexandrescu, A T Alexandrescu, 2001, Protein science : a publication of the Protein Society.

Microscopic stability of cold shock protein a examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N‐oxide

A. Alexandrescu, V. Jaravine, V A Jaravine, 2008, Protein science : a publication of the Protein Society.

An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils.

A. Alexandrescu, K. Rathgeb‐Szabo, 1999, Journal of molecular biology.

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.

Viktor A. Jaravine, A. Alexandrescu, S. Dames, 1999, Journal of molecular biology.

The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy

S. Casjens, M. Feig, K. Parent, 2018, eLife.

Modulation of agrin function by alternative splicing and Ca2+ binding.

R. Kammerer, M. Ruegg, J. Stetefeld, 2004, Structure.

Protein yoga: Conformational versatility of the Hemolysin II C‐terminal domain detailed by NMR structures for multiple states

A. R. Kaplan, A. Alexandrescu, R. Olson, 2021, Protein science : a publication of the Protein Society.

1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin.

C. Dobson, J. Baum, R. Broadhurst, 1992, European journal of biochemistry.

Thermodynamic and structural studies of carbohydrate binding by the agrin-G3 domain.

R. Kammerer, A. Alexandrescu, Christine O. Sallum, 2007, Biochemistry.

Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins

C. Teschke, A. Alexandrescu, Corynne L Dedeo, 2020, Viruses.

Molecular basis of coiled-coil formation

Wolfgang Jahnke, W. Jahnke, J. Missimer, 2007, Proceedings of the National Academy of Sciences.

Amyloid accomplices and enforcers

A. Alexandrescu, 2005, Protein science : a publication of the Protein Society.

Letter to the Editor: 1H, 13C and 15N backbone assignments for the C-terminal globular domain of agrin

R. Kammerer, J. Engel, A. Alexandrescu, 2001, Journal of biomolecular NMR.

Conservation and Divergence of the I-Domain Inserted into the Ubiquitous HK97 Coat Protein Fold in P22-Like Bacteriophages

C. Teschke, A. R. Kaplan, A. Alexandrescu, 2019, Journal of Virology.

NMR structure of the HWE kinase associated response regulator Sma0114 in its activated state.

A. Alexandrescu, D. Gage, S. R. Sheftic, 2014, Biochemistry.

Nuclear Magnetic Resonance Structure and Dynamics of the Response Regulator Sma 0114 from Sinorhizobium meliloti

V. Robinson, A. Alexandrescu, D. Gage, 2012 .

Dynamic α-Helix Structure of Micelle-bound Human Amylin*

A. Alexandrescu, Sharadrao M. Patil, S. R. Sheftic, 2009, Journal of Biological Chemistry.

Structure and disorder in the ribonuclease S‐peptide probed by NMR residual dipolar couplings

R. Kammerer, A. Alexandrescu, 2003, Protein science : a publication of the Protein Society.

Accretion of structure in staphylococcal nuclease: an 15N NMR relaxation study.

W. Jahnke, A. Alexandrescu, M. Blommers, 1996, Journal of molecular biology.

A fragment of staphylococcal nuclease with an OB‐fold structure shows hydrogen‐exchange protection factors in the range reported for “molten globules”

A. Alexandrescu, S. Dames, R. Wiltscheck, 1996, Protein science : a publication of the Protein Society.

NMR Mapping of Disordered Segments from a Viral Scaffolding Protein Encapsulated in a 23 MDa Procapsid Complex

C. Teschke, A. Alexandrescu, R. Whitehead, 2019, bioRxiv.

Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin‐1

R. Kammerer, J. Engel, A. Alexandrescu, 1999, FEBS letters.

Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix.

R. Kammerer, A. R. Kaplan, A. Alexandrescu, 2017, Biochemistry.

Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain*

Tina Motwani, C. Teschke, A. Alexandrescu, 2016, The Journal of Biological Chemistry.

Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.

C. Teschke, Rebecca L Newcomer, A. Alexandrescu, 2015, Biophysical journal.

NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain

A. R. Kaplan, A. Alexandrescu, R. Olson, 2013, Biomolecular NMR Assignments.

NMR assignments for the telokin-like domain of bacteriophage P22 coat protein

C. Teschke, A. Alexandrescu, S. R. Sheftic, 2012, Biomolecular NMR Assignments.

NMR assignments for the Sinorhizobium meliloti response regulator Sma0114

V. Robinson, A. Alexandrescu, D. Gage, 2011, Biomolecular NMR assignments.

NMR determination of pKa values in α‐synuclein

A. Alexandrescu, D. Kendall, Sharadrao M. Patil, 2011, Protein science : a publication of the Protein Society.

Electrostatic contributions to the stabilities of native proteins and amyloid complexes.

A. Alexandrescu, S. R. Sheftic, Jonathan Larochelle, 2009, Methods in enzymology.

Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms

R. Kammerer, J. Engel, T. Schulthess, 1997, Protein science : a publication of the Protein Society.

Charge-Based Inhibitors of Amylin Fibrillization and Toxicity

A. Alexandrescu, Sharadrao M. Patil, 2015, Journal of diabetes research.

NMR structure of a parallel homotrimeric coiled coil

Andrei T. Alexandrescu, R. Kammerer, J. Engel, 1998, Nature Structural &Molecular Biology.

Chemical exchange spectroscopy based on carbon-13 NMR. Applications to enzymology and protein folding

J. Markley, S. Loh, A. Alexandrescu, 1990 .

Observation of the closing of individual hydrogen bonds during TFE–induced helix formation in a peptide

S. Grzesiek, A. Alexandrescu, V. Jaravine, 2001, Protein science : a publication of the Protein Society.

Electrostatic contributions to the stability of the GCN4 leucine zipper structure.

R. Kammerer, C. A. Fitch, A. Alexandrescu, 2007, Journal of molecular biology.

NMR structure verifies the eponymous degenerate zinc finger domain of transcription factor ZNF750

A. Alexandrescu, R. Whitehead, Antonio J. Rua, 2023, bioRxiv.

NMR structure of the C-terminal domain of SecA in the free state.

A. Alexandrescu, W. M. Matousek, 2004, Biochimica et biophysica acta.

An NMR-Based Quenched Hydrogen Exchange Investigation of Model Amyloid Fibrils Formed by Cold Shock Protein A

Andrei T. Alexandrescu, A. Alexandrescu, 2000, Pacific Symposium on Biocomputing.

Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease.

D. Shortle, A. Alexandrescu, 1994, Journal of molecular biology.

Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study.

D. Shortle, A. Alexandrescu, C. Abeygunawardana, 1994, Biochemistry.

NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.

A. Alexandrescu, V. Jaravine, F. Lamour, 2000, Journal of molecular biology.

An Intrahelical Salt Bridge within the Trigger Site Stabilizes the GCN4 Leucine Zipper*

M. Steinmetz, R. Kammerer, A. Lustig, 2001, The Journal of Biological Chemistry.

Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.

A. Alexandrescu, W. M. Matousek, E. Watson, 2007, Biochemistry.

Effects of Heparin on Amylin Fibrillization

Craig E. Nelson, A. Alexandrescu, Sharadrao M. Patil, 2012 .

NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides

C. Teschke, A. Alexandrescu, A. Dregni, 2023, Journal of Biomolecular NMR.

Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease.

A. Hinck, J. Markley, A. Alexandrescu, 1990, Biochemistry.

Hydrogen-1 NMR evidence for three interconverting forms of staphylococcal nuclease: effects of mutations and solution conditions on their distribution.

E. Ulrich, J. Markley, A. Alexandrescu, 1989, Biochemistry.

NMR assignments of the four histidines of staphylococcal nuclease in native and denatured states.

E. Ulrich, J. Markley, A. Alexandrescu, 1988, Biochemistry.

Mechanism of interaction of the double-stranded RNA (dsRNA) binding domain of protein kinase R with short dsRNA sequences.

A. Alexandrescu, J. Cole, Yumiko Kobayashi, 2007, Biochemistry.

Solution structure of a peptide fragment of human alpha-lactalbumin in trifluoroethanol: a model for local structure in the molten globule.

C. Dobson, A. Alexandrescu, M. Pitkeathly, 1994, Structure.

The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy

Kristin N. Parent, S. Casjens, M. Feig, 2019, eLife.

NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750

A. Alexandrescu, R. Whitehead, Antonio J. Rua, 2023, Journal of structural biology: X.

NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750.

A. Alexandrescu, Antonio J. Rua, Richard D Whitehead Iii, 2023, Journal of structural biology.

Amide Proton Solvent Protection in Amylin Fibrils Probed by Quenched Hydrogen Exchange NMR

A. Alexandrescu, 2013, PloS one.

Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases

A. Alexandrescu, W. Mitchell, Nathan N. Alder, 2023, Frontiers in physiology.

Solution NMR assignments and structure for the dimeric kinesin neck domain

R. Kammerer, A. Alexandrescu, Diana Seo, 2023, Biomolecular NMR Assignments.

Initial studies of the equilibrium folding pathway of staphylococcal nuclease.

D. Shortle, A. Alexandrescu, Y. Wang, 1995, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix.

R. Kammerer, A. R. Kaplan, A. Alexandrescu, 2017, Biochemistry.

Perturbations in mitochondrial metabolism associated with defective cardiolipin biosynthesis: An in-organello real-time NMR study

A. Alexandrescu, S. Claypool, W. Mitchell, 2024, bioRxiv.

Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper

A. Alexandrescu, S. R. Sheftic, S. Jha, 2012, European Biophysics Journal.

Formerly degenerate seventh zinc finger domain from transcription factor ZNF711 rehabilitated by experimental NMR structure

A. Alexandrescu, Antonio J. Rua, 2024, bioRxiv.