Template-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein. (Q36278341)

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Language	Label	Description	Also known as
English	Template-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein.	scientific article

Statements

instance of

scholarly article

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Europe PubMed Central

PMC publication ID

2142622

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13 August 2017

title

Template-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein. (English)

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Europe PubMed Central

PMC publication ID

2142622

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13 August 2017

author name string

M Pawlak

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1

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Europe PubMed Central

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2142622

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13 August 2017

U Meseth

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2

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Europe PubMed Central

PMC publication ID

2142622

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13 August 2017

B Dhanapal

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3

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Europe PubMed Central

PMC publication ID

2142622

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13 August 2017

M Mutter

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4

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Europe PubMed Central

PMC publication ID

2142622

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13 August 2017

H Vogel

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5

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Europe PubMed Central

PMC publication ID

2142622

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13 August 2017

publication date

1 October 1994

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Europe PubMed Central

PMC publication ID

2142622

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13 August 2017

published in

Protein Science

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PMC publication ID

2142622

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13 August 2017

volume

3

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Europe PubMed Central

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2142622

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13 August 2017

issue

10

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Europe PubMed Central

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2142622

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13 August 2017

page(s)

1788-1805

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2142622

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13 August 2017

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The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities

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Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue

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Comparative properties and methods of preparation of lipid vesicles (liposomes).

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The sting. Melittin forms channels in lipid bilayers

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Phospholipid bilayers made from monolayers on patch-clamp pipettes

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Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties

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30 September 2017

The structure of melittin in membranes

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30 September 2017

Structural fluctuations of a helical polypeptide traversing a lipid bilayer

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Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers

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30 September 2017

The actions of melittin on membranes

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30 September 2017

Molecular Architecture and Electrostatic Properties of a Bacterial Porin

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30 September 2017

The biophysics of peptide models of ion channels

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Synporins--synthetic proteins that emulate the pore structure of biological ionic channels

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30 September 2017

All-D amino acid-containing channel-forming antibiotic peptides

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30 September 2017

Molecular anatomy and molecular design of channel proteins

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PubMed Central

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30 September 2017

Atomic scale structure and functional models of voltage-gated potassium channels

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30 September 2017

Acetylcholine receptor channel structure probed in cysteine-substitution mutants.

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30 September 2017

Crystal structures explain functional properties of two E. coli porins

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Total chemical synthesis, characterization, and immunological properties of an MHC class I model using the TASP concept for protein de novo design

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30 September 2017

Identifiers

DOI

10.1002/PRO.5560031019

1 reference

stated in

Europe PubMed Central

PMC publication ID

2142622

retrieved

13 August 2017

PMC publication ID

2142622

1 reference

stated in

Europe PubMed Central

PMC publication ID

2142622

retrieved

13 August 2017

PubMed publication ID

7531528

1 reference

stated in

Europe PubMed Central

PMC publication ID

2142622

retrieved

13 August 2017

 

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