about
Nano-Therapeutics for the Lung: State-of-the-Art and Future PerspectivesA cancer specific cell-penetrating peptide, BR2, for the efficient delivery of an scFv into cancer cellsArgininosuccinate synthetase is a functional target for a snake venom anti-hypertensive peptide: role in arginine and nitric oxide production.Role of the N-terminal seven residues of surfactant protein B (SP-B)Activity-based probes for monitoring postproline protease activity.A prokaryotic S1P lyase degrades extracellular S1P in vitro and in vivo: implication for treating hyperproliferative disordersPermeation through phospholipid bilayers, skin-cell penetration, plasma stability, and CD spectra of α- and β-oligoproline derivatives.Cell-Penetrating Penta-Peptides (CPP5s): Measurement of Cell Entry and Protein-Transduction ActivityFull membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptidesPeptide internalization enabled by folding: triple helical cell-penetrating peptides.Activity of the HMGB1-derived immunostimulatory peptide Hp91 resides in the helical C-terminal portion and is enhanced by dimerizationCombinatorial Library Screening with Liposomes for Discovery of Membrane Active Peptides.Colorectal delivery and retention of PEG-Amprenavir-Bac7 nanoconjugates--proof of concept for HIV mucosal pre-exposure prophylaxis.Cell-penetrating peptides: Possible transduction mechanisms and therapeutic applications.Designer nanomaterials using chiral self-assembling peptide systems and their emerging benefit for society.Cell penetration: scope and limitations by the application of cell-penetrating peptides.Parameters and characteristics governing cellular internalization and trans-barrier trafficking of nanostructures.Three valuable peptides from bee and wasp venoms for therapeutic and biotechnological use: melittin, apamin and mastoparan.Strategies to stabilize cell penetrating peptides for in vivo applications.Surface density of polyarginine influence the size, zeta potential, cellular uptake and tissue distribution of the nanostructured lipid carrier.An unexpected cell-penetrating peptide from Bothrops jararaca venom identified through a novel size exclusion chromatography screening.Protein vaccination with HPV16 E7/Pep-1 nanoparticles elicits a protective T-helper cell-mediated immune response.Targeting the Tumour: Cell Penetrating Peptides for Molecular Imaging and Radiotherapy.Building Cell Selectivity into CPP-Mediated Strategies.Synthesis and in vitro inhibition properties of oligonucleotide conjugates carrying amphipathic proline-rich peptide derivatives of the sweet arrow peptide (SAP).Bactenecin 7 peptide fragment as a tool for intracellular delivery of a phosphorescent oxygen sensor.Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation.Antimicrobial activities and action mechanism studies of transportan 10 and its analogues against multidrug-resistant bacteria.Development of a Cell-penetrating Peptide that Exhibits Responsive Changes in its Secondary Structure in the Cellular Environment.Membrane-active peptides and the clustering of anionic lipids.The Formation of Nanoparticles between Small Interfering RNA and Amphipathic Cell-Penetrating Peptides.Complexes of Ir(III)-octaethylporphyrin with peptides as probes for sensing cellular O2.Physicochemical and biological characterization of pep-1/elastin complexes.Quantum Dot-Peptide-Fullerene Bioconjugates for Visualization of in Vitro and in Vivo Cellular Membrane Potential.Cell-Penetrating Peptides: Design Strategies beyond Primary Structure and Amphipathicity.(R-X-R)4 -Motif Peptides Containing Conformationally Constrained Cyclohexane-Derived Spacers: Effect on Cellular Uptake.The toxic alpha-gliadin peptide 31-43 enters cells without a surface membrane receptor.Convergent synthesis and cellular uptake of multivalent cell penetrating peptides derived from Tat, Antp, pVEC, TP10 and SAP.Peptide Mediated Brain Delivery of Nano- and Submicroparticles: a Synergistic Approach.Construction of a polyproline structure with hydrophobic exterior using octahydroindole-2-carboxylic acid.
P2860
Q26786162-F3F72693-F6EF-4C86-8B35-4460A8D608F0Q28533791-639C8491-66C5-4977-BF20-E5F5B86CF2C1Q29144136-20B5DD09-6029-451B-BC05-D5816DF1E966Q30666184-D80713CB-A8D9-4FD0-BAAF-0EFAF3C9DC06Q33761011-3CE72DD5-9B78-4B11-B73E-992CBE4DE4BCQ33988392-BA0951CA-D563-4F68-9301-CC6B60EA84C6Q34557817-438D01AC-9531-4F40-A16F-8B703BEF2EAAQ34606888-F1C0835A-4F23-4BF2-9A51-5BD873CE9CD6Q35107072-66F499D5-6DF1-41D4-B895-A290A9219CD4Q35601619-85298E8B-7397-4439-A74E-7EC032DC4B09Q35903765-5DF5482F-397A-4AD8-B67D-06459D8AB541Q36335427-176F8CBF-98DC-41EC-AF88-507FD7AC0B6CQ36529598-91B3E5D2-EBCF-43D5-8A11-16E38D4CFF69Q36824518-3E90E049-2A50-4A5E-AB13-9892D11D12EEQ38013053-0502C094-7ACD-49B4-93AA-FCFAE68C559BQ38238902-E8FD9E2A-51AB-4D9D-8F2A-2C03C66CC85FQ38401187-CF3D4952-E5A3-4C2B-82EA-F4DF9023733DQ38401839-A308F29F-0B4D-44D1-BD96-95B60E85737AQ38602460-95E8768B-3D69-4273-9D24-A5A27A22E974Q38717127-99592CD3-4559-4EC1-B18B-FE6F34EA0FD2Q38722880-1D791B64-6B52-44C7-BE66-FB41982E0406Q38777042-8B17A8F3-835B-46AB-844A-3CA9834978BFQ38974209-84275F7E-35A7-4865-BE2A-D4AF8E6D066AQ38974301-4CB735A3-A770-4DAB-8635-402F5376F3D5Q39384935-BEF6D343-6A14-4277-8701-2F84D53193EFQ39649638-91D94135-0D08-427C-B816-905175420718Q40768103-6785F808-0FFE-47F1-BD5E-44EA795E4B60Q41043429-9EF4668A-6FAD-40D9-935C-BA43A9CFE847Q41050184-985DDD03-0958-4EFC-86DC-AC70028A8483Q41887010-327D46AB-79C2-4863-A656-6764CC6CD17DQ42314583-0C844FF6-A4C0-49C4-B1A5-A5C7F1A40DE8Q42324152-75F55939-E4FB-468C-A164-2C6AE393C9FDQ42822856-6BCA7195-1FDD-4331-9645-0581085B0453Q45059266-250C6C29-5632-466D-AC5F-0A0DC8E78D8CQ47586545-0C521B23-951B-4612-A237-F72D9BDEFCD3Q47742760-4827F04C-E9DC-4A13-B821-EC457BC7F221Q47796909-41B31F0F-93BC-4B05-9D92-0E9059001E05Q47810720-4EA66485-4444-48CC-A578-E2223DCF3DB6Q47933170-D896E64F-B4E2-448B-9AB9-9D92CF86D4CAQ48160501-ED3B2620-E544-4FA9-BEA0-5647398F8827
P2860
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Proline-rich, amphipathic cell-penetrating peptides.
@en
Proline-rich, amphipathic cell-penetrating peptides.
@nl
type
label
Proline-rich, amphipathic cell-penetrating peptides.
@en
Proline-rich, amphipathic cell-penetrating peptides.
@nl
prefLabel
Proline-rich, amphipathic cell-penetrating peptides.
@en
Proline-rich, amphipathic cell-penetrating peptides.
@nl
P1476
Proline-rich, amphipathic cell-penetrating peptides.
@en
P304
P356
10.1016/J.ADDR.2007.09.012
P407
P577
2007-11-17T00:00:00Z