127 results on '"Craik, David J."'
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2. Delivery to, and Reactivation of, the p53 Pathway in Cancer Cells Using a Grafted Cyclotide Conjugated with a Cell-Penetrating Peptide
3. Development of a Selective Peptide κ-Opioid Receptor Antagonist by Late-Stage Functionalization with Cysteine Staples
4. Structure–Activity Relationships of Alanine Scan Mutants αO-Conotoxins GeXIVA[1,2] and GeXIVA[1,4]
5. Discovery, Characterization, and Engineering of LvIC, an α4/4-Conotoxin That Selectively Blocks Rat α6/α3β4 Nicotinic Acetylcholine Receptors
6. Engineering the Cyclization Loop of MCoTI-II Generates Targeted Cyclotides that Potently Inhibit Factor XIIa
7. Late-Stage Functionalization with Cysteine Staples Generates Potent and Selective Melanocortin Receptor-1 Agonists
8. Melanocortin 1 Receptor Agonists Based on a Bivalent, Bicyclic Peptide Framework
9. Design of a Stable Cyclic Peptide Analgesic Derived from Sunflower Seeds that Targets the κ-Opioid Receptor for the Treatment of Chronic Abdominal Pain
10. Engineered Conotoxin Differentially Blocks and Discriminates Rat and Human α7 Nicotinic Acetylcholine Receptors
11. Designed β-Hairpins Inhibit LDH5 Oligomerization and Enzymatic Activity
12. Computational and Functional Mapping of Human and Rat α6β4 Nicotinic Acetylcholine Receptors Reveals Species-Specific Ligand-Binding Motifs
13. Bioactive Cyclization Optimizes the Affinity of a Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) Peptide Inhibitor
14. Enhanced Activity against Multidrug-Resistant Bacteria through Coapplication of an Analogue of Tachyplesin I and an Inhibitor of the QseC/B Signaling Pathway
15. Structure and Activity Studies of Disulfide-Deficient Analogues of αO-Conotoxin GeXIVA
16. Binding Loop Substitutions in the Cyclic Peptide SFTI-1 Generate Potent and Selective Chymase Inhibitors
17. Computer-Aided Design of Mastoparan-like Peptides Enables the Generation of Nontoxic Variants with Extended Antibacterial Properties
18. Amino Acid Scanning at P5′ within the Bowman–Birk Inhibitory Loop Reveals Specificity Trends for Diverse Serine Proteases
19. Highly Potent and Selective Plasmin Inhibitors Based on the Sunflower Trypsin Inhibitor-1 Scaffold Attenuate Fibrinolysis in Plasma
20. Single Amino Acid Substitution in α-Conotoxin TxID Reveals a Specific α3β4 Nicotinic Acetylcholine Receptor Antagonist
21. Development of Novel Melanocortin Receptor Agonists Based on the Cyclic Peptide Framework of Sunflower Trypsin Inhibitor-1
22. The E15R Point Mutation in Scorpion Toxin Cn2 Uncouples Its Depressant and Excitatory Activities on Human NaV1.6
23. Bioactive Cyclization Optimizes the Affinity of a Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) Peptide Inhibitor
24. α-Conotoxin [S9A]TxID Potently Discriminates between α3β4 and α6/α3β4 Nicotinic Acetylcholine Receptors
25. Design of Potent and Selective Cathepsin G Inhibitors Based on the Sunflower Trypsin Inhibitor-1 Scaffold
26. Binding Loop Substitutions in the Cyclic Peptide SFTI-1 Generate Potent and Selective Chymase Inhibitors
27. Highly Potent and Selective Plasmin Inhibitors Based on the Sunflower Trypsin Inhibitor‑1 Scaffold Attenuate Fibrinolysis in Plasma.
28. Computer-Aided Design of Mastoparan-like Peptides Enables the Generation of Nontoxic Variants with Extended Antibacterial Properties
29. The E15R Point Mutation in Scorpion Toxin Cn2 Uncouples Its Depressant and Excitatory Activities on Human NaV1.6
30. Enhanced Activity against Multidrug-Resistant Bacteria through Coapplication of an Analogue of Tachyplesin I and an Inhibitor of the QseC/B Signaling Pathway
31. Substrate-Guided Design of Selective FXIIa Inhibitors Based on the Plant-Derived Momordica cochinchinensis Trypsin Inhibitor-II (MCoTI-II) Scaffold
32. The E15R Point Mutation in Scorpion Toxin Cn2 Uncouples Its Depressant and Excitatory Activities on Human NaV1.6.
33. Improving the Selectivity of Engineered Protease Inhibitors: Optimizing the P2 Prime Residue Using a Versatile Cyclic Peptide Library
34. α-Conotoxin [S9A]TxID Potently Discriminates between α3β4 and α6/α3β4 Nicotinic Acetylcholine Receptors.
35. Characterization of a Novel α-Conotoxin TxID from Conus textile That Potently Blocks Rat α3β4 Nicotinic Acetylcholine Receptors
36. Correction to Chemical Re-engineering of Chlorotoxin Improves Bioconjugation Properties for Tumor Imaging and Targeted Therapy
37. Determination of the α-Conotoxin Vc1.1 Binding Site on the α9α10 Nicotinic Acetylcholine Receptor
38. Effects of Cyclization on Stability, Structure, and Activity of α-Conotoxin RgIA at the α9α10 Nicotinic Acetylcholine Receptor and GABAB Receptor
39. Chemical Re-engineering of Chlorotoxin Improves Bioconjugation Properties for Tumor Imaging and Targeted Therapy
40. Engineering Stabilized Vascular Endothelial Growth Factor-A Antagonists: Synthesis, Structural Characterization, and Bioactivity of Grafted Analogues of Cyclotides
41. Molecular Engineering of Conotoxins: The Importance of Loop Size to α-Conotoxin Structure and Function
42. Cyclic MrIA: A Stable and Potent Cyclic Conotoxin with a Novel Topological Fold that Targets the Norepinephrine Transporter
43. Synthesis, Structure Elucidation, in Vitro Biological Activity, Toxicity, and Caco-2 Cell Permeability of Lipophilic Analogues of α-Conotoxin MII
44. Characterization of a Novel α-ConotoxinTxID from Conus textileThat Potently Blocks Ratα3β4Nicotinic Acetylcholine Receptors.
45. Solution Structure of α-Conotoxin ImI by 1H Nuclear Magnetic Resonance
46. Low-Molecular-Weight Peptidic and Cyclic Antagonists of the Receptor for the Complement Factor C5a
47. Structure−Activity Studies of Conantokins as HumanN-Methyl-d-aspartate Receptor Modulators,
48. Small Molecular Probes for G-Protein-Coupled C5a Receptors: Conformationally Constrained Antagonists Derived from the C Terminus of the Human Plasma Protein C5a
49. Conformational Dynamics of Thyroid Hormones by Variable Temperature Nuclear Magnetic Resonance: The Role of Side Chain Rotations and Cisoid/Transoid Interconversions
50. H and 13C NMR Relaxation Studies of Molecular Dynamics of the Thyroid Hormones Thyroxine, 3,5,3‘-Triiodothyronine, and 3,5-Diiodothyronine
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