De Novo-designed Peptide Transforms Golgi-specific Lipids into Golgi-like Nanotubules

scientific article published in Journal of Biological Chemistry

De Novo-designed Peptide Transforms Golgi-specific Lipids into Golgi-like Nanotubules is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M104705200
P698PubMed publication ID11406635

P2093author name stringTaira Kiyota
Gohsuke Sugihara
Sannamu Lee
Tomomi Furuya
Yasuro Niidome
Kunihiko Murata
Dale E. Bredesen
H. Michael Ellerby
Noboru Takami
P2860cites workFunctional rafts in cell membranesQ27860768
Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosisQ28137851
Pulmonary surfactant protein B (SP-B): structure-function relationshipsQ28246789
Protein sorting by transport vesiclesQ29619990
Golgi membrane dynamicsQ30483574
Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundlesQ37328277
Morphological behavior of acidic and neutral liposomes induced by basic amphiphilic alpha-helical peptides with systematically varied hydrophobic-hydrophilic balanceQ40139002
Vesicles of variable sizes produced by a rapid extrusion procedureQ47598175
Dynamin undergoes a GTP-dependent conformational change causing vesiculationQ47945531
Golgi membrane dynamics imaged by freeze-etch electron microscopy: views of different membrane coatings involved in tubulation versus vesiculationQ70488207
Design and synthesis of amphiphilic alpha-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranesQ71652703
Interfacial properties of surfactant proteinsQ77545860
P433issue44
P407language of work or nameEnglishQ1860
P921main subjectlipidQ11367
P1104number of pages5
P304page(s)41224-41228
P577publication date2001-06-13
P1433published inJournal of Biological ChemistryQ867727
P1476titleDe Novo-designed Peptide Transforms Golgi-specific Lipids into Golgi-like Nanotubules
P478volume276

Reverse relations

cites work (P2860)
Q57372555A Hydrophobic Patch in a Charged α-Helix Is Sufficient to Target Proteins to Dense Core Secretory Granules
Q55040222A giant amphipathic helix from a perilipin that is adapted for coating lipid droplets.
Q37616695Amphipathic helices and membrane curvature
Q30478852Antimicrobial peptides temporins B and L induce formation of tubular lipid protrusions from supported phospholipid bilayers
Q33893699Biogenesis of nanotubular network in Toxoplasma parasitophorous vacuole induced by parasite proteins
Q36791244Factors influencing local membrane curvature induction by N-BAR domains as revealed by molecular dynamics simulations
Q35189394Mechanisms of membrane deformation
Q29617321Membrane curvature and mechanisms of dynamic cell membrane remodelling
Q42166998Membrane curvature during peroxisome fission requires Pex11.
Q92928680Nanodisc-to-Nanofiber Transition of Noncovalent Peptide-Phospholipid Assemblies
Q40232130Nanotubules formed by highly hydrophobic amphiphilic alpha-helical peptides and natural phospholipids
Q42183433Pulmonary surfactant model systems catch the specific interaction of an amphiphilic peptide with anionic phospholipid
Q33386000Role of amphipathic helix of a herpesviral protein in membrane deformation and T cell receptor downregulation
Q34354306Structure of core domain of fibril-forming PHF/Tau fragments.
Q57362819The formation of helical tubular vesicles by binary monolayers containing a nickel-chelating lipid and phosphoinositides in the presence of basic polypeptides
Q30500318α-Synuclein-induced tubule formation in lipid bilayers

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