M. Prorok

发表

Ca 2+-induced self-assembly in designed peptides with optimally spaced gamma-carboxyglutamic acid residues.

F. Castellino, Mary Prorok, Qiuyun Dai, 2011, Journal of inorganic biochemistry.

Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid Vesicles.

F. Castellino, M. Prorok, W. T. Christiansen, 1995, Biochemistry.

Structure-Function Analysis of the Streptokinase Amino Terminus (Residues 1–59)*

F. Castellino, W. Fay, M. Prorok, 2003, Journal of Biological Chemistry.

Substrate specificity of cyclic amp dependent protein kinase

D. Lawrence, M. Prorok, 1988 .

The Lack of Binding of VEK-30, an Internal Peptide from the Group A Streptococcal M-like Protein, PAM, to Murine Plasminogen Is due to Two Amino Acid Replacements in the Plasminogen Kringle-2 Domain*

J. Geiger, F. Castellino, V. Ploplis, 2008, Journal of Biological Chemistry.

Cathepsin E Is a Specific Marker of Dysplasia in APCMin/+ Mouse Intestine

M. Suckow, F. Castellino, R. Navari, 2005, Tumor Biology.

The Amino Acid Residue at Sequence Position 5 in the Conantokin Peptides Partially Governs Subunit-selective Antagonism of RecombinantN-Methyl-d-aspartate Receptors*

F. Castellino, M. Prorok, Z. Galdzicki, 2001, The Journal of Biological Chemistry.

NMDA‐receptor antagonist requirements in conantokin‐G

F. Castellino, T. Blandl, M. Prorok, 1998, FEBS letters.

Calcium binding properties of synthetic gamma-carboxyglutamic acid-containing marine cone snail "sleeper" peptides, conantokin-G and conantokin-T.

F. Castellino, S. Warder, T. Blandl, 1996, Biochemistry.

Specific determinants of conantokins that dictate their selectivity for the NR2B subunit of N-methyl-d-aspartate receptors

F. Castellino, M. Prorok, Z. Sheng, 2010, Neuroscience.

Kinetic and mechanistic characterization of NMDA receptor antagonism by replacement and truncation variants of the conantokin peptides

F. Castellino, S. Warder, M. Prorok, 2001, Neuropharmacology.

A Conantokin Peptide Con-T[M8Q] Inhibits Morphine Dependence with High Potency and Low Side Effects

Shuo Yu, Qiuyun Dai, Mingxin Dong, 2021, Marine drugs.

Conantokins and variants derived from cone snail venom inhibit naloxone-induced withdrawal jumping in morphine-dependent mice

F. Castellino, Qiuyun Dai, Mingxin Dong, 2006, Neuroscience Letters.

Metal ion determinants of conantokin dimerization as revealed in the X-ray crystallographic structure of the Cd2+/Mg2+–con-T[K7γ] complex

J. Geiger, F. Castellino, M. Prorok, 2010, JBIC Journal of Biological Inorganic Chemistry.

The molecular basis of conantokin antagonism of NMDA receptor function.

F. Castellino, M. Prorok, 2007, Current drug targets.

A single amino acid replacement results in the Ca2+-induced self-assembly of a helical conantokin-based peptide.

F. Castellino, Qiuyun Dai, M. Prorok, 2004, Biochemistry.

Binding and orientation of conantokins in PL vesicles and aligned PL multilayers.

F. Castellino, J. Zajicek, Qiuyun Dai, 2003, Biochemistry.

Enhancement through Mutagenesis of the Binding of the Isolated Kringle 2 Domain of Human Plasminogen to ω-Amino Acid Ligands and to an Internal Sequence of a Streptococcal Surface Protein*

F. Castellino, M. Prorok, S. L. Nilsen, 1999, The Journal of Biological Chemistry.

Direct binding properties of conantokins to native N-methyl-d-aspartate receptors.

F. Castellino, M. Prorok, R. C. Klein, 2003, The journal of peptide research : official journal of the American Peptide Society.

NR2B-selective conantokin peptide inhibitors of the NMDA receptor display enhanced antinociceptive properties compared to non-selective conantokins

F. Castellino, Qiuyun Dai, Mingxin Dong, 2008, Neuropeptides.

Binding of the gene repressor BlaI to the bla operon in methicillin-resistant Staphylococcus aureus.

S. Mobashery, Leticia I. Llarrull, M. Prorok, 2010, Biochemistry.

Binding of calcium to individual gamma-carboxyglutamic acid residues of human protein C.

F. Castellino, T. Colpitts, M. Prorok, 1995, Biochemistry.

Three-dimensional structure of chymotrypsin inactivated with (2S)-N-acetyl-L-alanyl-L-phenylalanyl alpha-chloroethane: implications for the mechanism of inactivation of serine proteases by chloroketones.

D. Ringe, A. Steinmetz, T. Liang, 1994, Biochemistry.

Chloroketone hydrolysis by chymotrypsin and N-methylhistidyl-57-chymotrypsin: implications for the mechanism of chymotrypsin inactivation by chloroketones.

B. Foxman, A. Albeck, R. Abeles, 1994, Biochemistry.

The entire gamma-carboxyglutamic acid- and helical stack-domains of human coagulation factor IX are required for optimal binding to its endothelial cell receptor.

F. Castellino, S. Warder, M. Prorok, 2009, International journal of peptide and protein research.

Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers.

F. Castellino, D. Weliky, M. Prorok, 2004, Biophysical journal.

The cyclic AMP-dependent protein kinase from bovine cardiac muscle is a homoserine kinase.

D. Lawrence, D. Sukumaran, M. Prorok, 1989, The Journal of biological chemistry.

Noncovalent active site interactions enhance the affinity and control the binding order of reversible inhibitors of the cAMP-dependent protein kinase.

D. Lawrence, M. Prorok, A. Salerno, 1990, The Journal of biological chemistry.

The selectivity of conantokin-G for ion channel inhibition of NR2B subunit-containing NMDA receptors is regulated by amino acid residues in the S2 region of NR2B

J. Geiger, F. Castellino, M. Prorok, 2009, Neuropharmacology.

N-methyl-d-aspartate receptor inhibition by an apolipoprotein E-derived peptide relies on low-density lipoprotein receptor-associated protein

F. Castellino, M. Prorok, Z. Sheng, 2008, Neuropharmacology.

Non-strict strand orientation of the Ca2+-induced dimerization of a conantokin peptide variant with sequence-shifted γ-carboxyglutamate residues

Zhenyu Sheng, Francis J. Castellino, F. Castellino, 2009, Peptides.

A new mechanism for metal ion-assisted interchain helix assembly in a naturally occurring peptide mediated by optimally spaced gamma-carboxyglutamic acid residues.

F. Castellino, Mary Prorok, Qiuyun Dai, 2004, Journal of molecular biology.

NMR backbone dynamics of VEK-30 bound to the human plasminogen kringle 2 domain.

F. Castellino, M. Prorok, Min Wang, 2010, Biophysical journal.

Solution structure of the complex of VEK-30 and plasminogen kringle 2.

J. Geiger, F. Castellino, J. Zajicek, 2009, Journal of structural biology.

Effects on human plasminogen conformation and activation rate caused by interaction with VEK-30, a peptide derived from the group A streptococcal M-like protein (PAM).

F. Castellino, M. Ranson, M. Walker, 2010, Biochimica et biophysica acta.

ATPase-promoting dead end inhibitors of the cAMP-dependent protein kinase.

D. Lawrence, M. Prorok, A. Salerno, 1993, The Journal of biological chemistry.

The crystal structures of the calcium-bound con-G and con-T[K7gamma] dimeric peptides demonstrate a metal-dependent helix-forming motif.

J. Geiger, F. Castellino, James H Geiger, 2007, Journal of the American Chemical Society.

Structure–function relationships of the NMDA receptor antagonist peptide, conantokin‐R

F. Castellino, S. Warder, T. Blandl, 2000, FEBS letters.

Subtype-selective antagonism of N-methyl-d-aspartate receptor ion channels by synthetic conantokin peptides

F. Castellino, Qiuyun Dai, M. Prorok, 2007, Neuropharmacology.

Helix-Helix Interactions between Homo- and Heterodimeric γ-Carboxyglutamate-containing Conantokin Peptides and Their Derivatives*

Zhenyu Sheng, J. Geiger, F. Castellino, 2007, Journal of Biological Chemistry.

Cryopreservation of the cyclic 3',5'-adenosine monophosphate-dependent protein kinase from bovine cardiac muscle.

D. Lawrence, M. Prorok, 1989, Journal of biochemical and biophysical methods.

X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound to a peptide from the group A streptococcal surface protein PAM.

J. Geiger, F. Castellino, M. Prorok, 2006, Biochemistry.

Glycosylation of Asparagine-28 of Recombinant Staphylokinase with High-Mannose-type Oligosaccharides Results in a Protein with Highly Attenuated Plasminogen Activator Activity*

F. Castellino, R. Miele, M. Prorok, 1999, The Journal of Biological Chemistry.

Deciphering the US News and World Report Ranking of US Chemistry Graduate Programs

Masaru Kuno, Shubin Zhang, Huy-Quoc Huynh, 2022, Scientometrics.

High‐level secretion in Pichia pastoris and biochemical characterization of the recombinantkringle 2 domain of tissue‐type plasminogen activator

F. Castellino, R. Bretthauer, M. Prorok, 1997, Biotechnology and applied biochemistry.

The Roles of Individual γ-Carboxyglutamate Residues in the Solution Structure and Cation-dependent Properties of Conantokin-T*

L. Pedersen, F. Ni, F. Castellino, 1998, The Journal of Biological Chemistry.

A trimeric HIV-1 fusion peptide construct which does not self-associate in aqueous solution and which has 15-fold higher membrane fusion rate.

F. Castellino, D. Weliky, M. Prorok, 2004, Journal of the American Chemical Society.

A molecular constraint that generates a cis peptide bond

David S. Lawrence, D. Lawrence, D. Sukumaran, 1991 .

Amino acid determinants for NMDA receptor inhibition by conantokin‐T

F. Castellino, S. Warder, M. Prorok, 2001, Journal of neurochemistry.

Thermodynamics of Binding of Calcium, Magnesium, and Zinc to theN-Methyl-d-aspartate Receptor Ion Channel Peptidic Inhibitors, Conantokin-G and Conantokin-T*

F. Castellino, M. Prorok, 1998, The Journal of Biological Chemistry.

Role of the Hexapeptide Disulfide Loop in the γ-Carboxyglutamic Acid Domain of Protein C in Ca2+-Mediated Structural and Functional Properties†

Francis J. Castellino, F. Castellino, Mary Prorok, 2005 .

M E STERSÉGE S IN TELLIGENCIA R ENDSZER EK

M. Prorok, Kar, Prorok Máté, 2022 .

An internal histidine residue from the bacterial surface protein, PAM, mediates its binding to the kringle-2 domain of human plasminogen.

M. Schenone, F. Castellino, S. Warder, 2000, The journal of peptide research : official journal of the American Peptide Society.

Conformational Changes in Conantokin-G Induced upon Binding of Calcium and Magnesium as Revealed by NMR Structural Analysis*

L. Pedersen, F. Castellino, S. Warder, 1998, The Journal of Biological Chemistry.

Intrasubstrate steric interactions in the active site control the specificity of the cAMP-dependent protein kinase.

D. Lawrence, M. Prorok, 1989, Biochemical and biophysical research communications.

The NMR solution structure of the NMDA receptor antagonist, conantokin‐T, in the absence of divalent metal ions

F. Ni, F. Castellino, S. Warder, 1997, FEBS letters.

Serine-578 is a major phosphorylation locus in human plasma plasminogen.

F. Castellino, R. Bretthauer, M. Prorok, 1997, Biochemistry.