Solution structures and biological functions of the antimicrobial peptide, arenicin-1, and its linear derivative

Biopolymers ◽

10.1002/bip.20700 ◽

2007 ◽

Vol 88 (2) ◽

pp. 208-216 ◽

Cited By ~ 43

Author(s):

Ju-Un Lee ◽

Dong-Il Kang ◽

Wan Long Zhu ◽

Song Yub Shin ◽

Kyung-Soo Hahm ◽

...

Keyword(s):

Antimicrobial Peptide ◽

Biological Functions ◽

Solution Structures

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Solution structures and model membrane interactions of lactoferrampin, an antimicrobial peptide derived from bovine lactoferrin

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/j.bbamem.2007.04.018 ◽

2007 ◽

Vol 1768 (10) ◽

pp. 2355-2364 ◽

Cited By ~ 60

Author(s):

Evan F. Haney ◽

Fanny Lau ◽

Hans J. Vogel

Keyword(s):

Antimicrobial Peptide ◽

Model Membrane ◽

Bovine Lactoferrin ◽

Membrane Interactions ◽

Solution Structures

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Correlation between Single-Molecule Dynamics and Biological Functions of Antimicrobial Peptide Melittin

The Journal of Physical Chemistry Letters ◽

10.1021/acs.jpclett.0c01169 ◽

2020 ◽

Vol 11 (12) ◽

pp. 4834-4841

Author(s):

Cheng Xu ◽

Wendong Ma ◽

Kang Wang ◽

Kejie He ◽

Zhonglan Chen ◽

...

Keyword(s):

Antimicrobial Peptide ◽

Single Molecule ◽

Biological Functions ◽

Single Molecule Dynamics ◽

Molecule Dynamics

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Solution Structures of the Linear Leaderless Bacteriocins Enterocin 7A and 7B Resemble Carnocyclin A, a Circular Antimicrobial Peptide

Biochemistry ◽

10.1021/bi400359z ◽

2013 ◽

Vol 52 (23) ◽

pp. 3987-3994 ◽

Cited By ~ 22

Author(s):

Christopher T. Lohans ◽

Kaitlyn M. Towle ◽

Mark Miskolzie ◽

Ryan T. McKay ◽

Marco J. van Belkum ◽

...

Keyword(s):

Antimicrobial Peptide ◽

Solution Structures ◽

Carnocyclin A

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Membrane–cytoskeleton interactions in cholesterol-dependent domain formation

Essays in Biochemistry ◽

10.1042/bse0570177 ◽

2015 ◽

Vol 57 ◽

pp. 177-187 ◽

Cited By ~ 9

Author(s):

Jennifer N. Byrum ◽

William Rodgers

Keyword(s):

Biological Properties ◽

Membrane Rafts ◽

Membrane Domains ◽

Biological Functions ◽

Membrane Cytoskeleton ◽

Heterogeneous Structures ◽

Integral Role ◽

Model Cell ◽

Actomyosin Cytoskeleton ◽

Dependent Domain

Since the inception of the fluid mosaic model, cell membranes have come to be recognized as heterogeneous structures composed of discrete protein and lipid domains of various dimensions and biological functions. The structural and biological properties of membrane domains are represented by CDM (cholesterol-dependent membrane) domains, frequently referred to as membrane ‘rafts’. Biological functions attributed to CDMs include signal transduction. In T-cells, CDMs function in the regulation of the Src family kinase Lck (p56lck) by sequestering Lck from its activator CD45. Despite evidence of discrete CDM domains with specific functions, the mechanism by which they form and are maintained within a fluid and dynamic lipid bilayer is not completely understood. In the present chapter, we discuss recent advances showing that the actomyosin cytoskeleton has an integral role in the formation of CDM domains. Using Lck as a model, we also discuss recent findings regarding cytoskeleton-dependent CDM domain functions in protein regulation.

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The structure, genetic polymorphisms, expression and biological functions of complement receptor type 1 (CR1/CD35)

Immunopharmacology and Immunotoxicology ◽

10.1080/08923970902845768 ◽

2009 ◽

Vol 00 (00) ◽

pp. 090923083856073-12

Author(s):

Dong Liu ◽

Zhong-Xiang Niu

Keyword(s):

Genetic Polymorphisms ◽

Receptor Type ◽

Complement Receptor ◽

Biological Functions ◽

Complement Receptor Type ◽

Complement Receptor Type 1

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The Interaction of β2 Glycoprotein-I and Heparin and Its Effect on β2 Glycoprotein-I Antiphospholipid Antibody Cofactor Function in Plasma

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648918 ◽

1994 ◽

Vol 72 (04) ◽

pp. 578-581 ◽

Cited By ~ 3

Author(s):

T McNally ◽

S E Cotterell ◽

I J Mackie ◽

D A Isenberg ◽

S J Machin

Keyword(s):

Solid Phase ◽

Pharmaceutical Preparations ◽

Enzyme Linked Immunosorbent Assay ◽

Antiphospholipid Antibody ◽

Biological Functions ◽

Dermatan Sulphate ◽

Glycoprotein I ◽

Crossed Immunoelectrophoresis ◽

Calcium Heparin ◽

Cofactor Activity

Summaryβ2 glycoprotein-I (β2GPI), a cofactor for antiphospholipid antibody (aPA) binding, binds to many anionic macromolecules including heparin. The nature of this interaction with heparin is not well understood and its effect on the purported biological functions of β2GPI is unknown.We have examined the interactions of dermatan sulphate (DS) and different pharmaceutical preparations of heparin with β2GPI by crossed immunoelectrophoresis (CIE) and investigated the effect of these agents on plasma levels of p2GPI antigen (β2GPI: Ag) by a standardised enzyme linked immunosorbent assay (ELISA). P2GPI aPA cofactor activity (β2GPI:Cof) was also measured using a modified solid phase an-ti-phosphatidylserine (aPS) ELISA. CIE results confirmed a heparin-β2GPI interaction with unfractionated (UF) heparin. β2GPI:Ag levels were unaffected by any of the preparations investigated. There were no significant differences in β2GPI:Cof activities of the samples containing LMW heparins or DS but levels of β2GPI:Cof were increased in samples containing UF sodium and calcium heparin preparations (0.5 IU/ml Monoparin, p <0.05, and 10 IU/ml Liquemin and Calcipa-rine, p <0.05).

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