+

Braun et al., 2008 - Google Patents

HIV-1 capsid assembly inhibitor (CAI) peptide: structural preferences and delivery into human embryonic lung cells and lymphocytes

Braun et al., 2008

View HTML
Document ID
9304991222252846692
Author
Braun K
Frank M
Pipkorn R
Reed J
Spring H
Debus J
Didinger B
von der Lieth C
Wiessler M
Waldeck W
Publication year
Publication venue
International journal of medical sciences

External Links

Snippet

The Human immunodeficiency virus 1 derived capsid assembly inhibitor peptide (HIV-1 CAI- peptide) is a promising lead candidate for anti-HIV drug development. Its drawback, however, is that it cannot permeate cells directly. Here we report the transport of the …
Continue reading at pmc.ncbi.nlm.nih.gov (HTML) (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K7/00Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04Linear peptides containing only normal peptide links
    • C07K7/08Linear peptides containing only normal peptide links having 12 to 20 amino acids

Similar Documents

Publication Publication Date Title
Geyer et al. Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein
US11390646B2 (en) Structure-based peptide inhibitors of α-synuclein aggregation
Saad et al. Point mutations in the HIV-1 matrix protein turn off the myristyl switch
Luca et al. Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR
Caffrey et al. Three‐dimensional solution structure of the 44 kDa ectodomain of SIV gp41
Young Mechanisms of the Hsp70 chaperone system
Saidi Brikci-Nigassa et al. Phosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubules
Morellet et al. Helical structure determined by NMR of the HIV‐1 (345–392) Gag sequence, surrounding p2: Implications for particle assembly and RNA packaging
Schärpf et al. Antitermination in bacteriophage λ: The structure of the N36 peptide‐boxB RNA complex
Okuda et al. Extended string binding mode of the phosphorylated transactivation domain of tumor suppressor p53
Kowalski et al. NMR solution structure of the isolated Apo Pin1 WW domain: Comparison to the x‐ray crystal structures of Pin1
Shuaib et al. Scrutiny of the mechanism of small molecule inhibitor preventing conformational transition of amyloid-β42 monomer: insights from molecular dynamics simulations
Lacy et al. Molecular basis for the specificity of p27 toward cyclin-dependent kinases that regulate cell division
Bosco et al. Catalysis and binding of cyclophilin A with different HIV-1 capsid constructs
Carotenuto et al. Conformation− activity relationship of designed glycopeptides as synthetic probes for the detection of autoantibodies, biomarkers of multiple sclerosis
Tzakos et al. On the molecular basis of the recognition of angiotensin II (AII) NMR structure of AII in solution compared with the X‐ray structure of AII bound to the mAb Fab131
Wong et al. Solution structure of a double mutant of the carboxy-terminal dimerization domain of the HIV-1 capsid protein
Farina et al. Binding mode of AIF (370–394) peptide to CypA: insights from NMR, label-free and molecular docking studies
Iaccarino et al. Structure-based design of small bicyclic peptide inhibitors of Cripto-1 activity
Braun et al. HIV-1 capsid assembly inhibitor (CAI) peptide: structural preferences and delivery into human embryonic lung cells and lymphocytes
Stote et al. Structure of the His44→ Ala single point mutant of the distal finger motif of HIV-1 nucleocapsid protein: a combined NMR, molecular dynamics simulation, and fluorescence study
Mercurio et al. Peptide Fragments of Odin‐Sam1: Conformational Analysis and Interaction Studies with EphA2‐Sam
Engler et al. Solution structure of human immunodeficiency virus type 1 Vpr (13–33) peptide in micelles
Byrne et al. A β-turn motif in the steroid hormone receptor’s ligand-binding domains interacts with the peptidyl-prolyl isomerase (PPIase) catalytic site of the immunophilin FKBP52
Bellot et al. Structure of the third intracellular loop of the vasopressin V2 receptor and conformational changes upon binding to gC1qR
点击 这是indexloc提供的php浏览器服务,不要输入任何密码和下载