Argentinian small ruminant lentivirus (SRLV) p55gag antigen fused to maltose binding protein to use in SRLV serological confirmatory diagnosis

Faculty Opinions recommendation of The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediated.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.717968797.793468506 ◽

2013 ◽

Author(s):

Mario Lebendiker

Keyword(s):

Binding Protein ◽

Intrinsic Property ◽

Faculty Opinions recommendation of Maltose-Binding Protein (MBP), a Secretion-Enhancing Tag for Mammalian Protein Expression Systems.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.726253920.793520308 ◽

2016 ◽

Author(s):

Mario Lebendiker

Keyword(s):

Protein Expression ◽

Binding Protein ◽

Maltose Binding Protein ◽

Expression Systems ◽

Mammalian Protein

Intragenic reversion mutations that improve export of maltose-binding protein in Escherichia coli malE signal sequence mutants.

10.1016/s0021-9258(17)35795-2 ◽

1986 ◽

Vol 261 (7) ◽

pp. 3389-3395

Author(s):

J P Ryan ◽

M C Duncan ◽

V A Bankaitis ◽

P J Bassford

Keyword(s):

Escherichia Coli ◽

Signal Sequence ◽

Binding Protein ◽

Production of MBP(maltose binding protein)-GroES fusion protein and utilization to stimulate GroEL-mediated protein refolding

Journal of Fermentation and Bioengineering ◽

10.1016/s0922-338x(97)80356-x ◽

1998 ◽

Vol 85 (1) ◽

pp. 69-73 ◽

Cited By ~ 2

Author(s):

Yoshiyuki Ishii ◽

Kaoru Murakami ◽

Hiroaki I.-Ogawa ◽

Akihiko Kondo ◽

Yasuhiko Kato

Keyword(s):

Fusion Protein ◽

Binding Protein ◽

Protein Refolding ◽

Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein

10.1016/s0021-9258(18)50020-x ◽

1992 ◽

Vol 267 (32) ◽

pp. 22813-22820

Author(s):

Y Zhang ◽

C Conway ◽

M Rosato ◽

Y Suh ◽

M.D. Manson

Keyword(s):

Binding Protein ◽

Maltose Binding Protein ◽

Terminal Domains

Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane.

10.1016/s0021-9258(19)83799-7 ◽

1982 ◽

Vol 257 (10) ◽

pp. 5455-5461

Author(s):

H A Shuman

Keyword(s):

Escherichia Coli ◽

Active Transport ◽

Cytoplasmic Membrane ◽

Binding Protein ◽

Substrate Recognition ◽

Maltose Binding Protein ◽

Recognition Site ◽

Escherichia Coli K12

Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein

Protein Science ◽

10.1002/pro.5560071010 ◽

1998 ◽

Vol 7 (10) ◽

pp. 2136-2142 ◽

Cited By ~ 19

Author(s):

Sébastien Raffy ◽

Nathalie Sassoon ◽

Maurice Hofnung ◽

Jean-Michel Betton

Keyword(s):

Tertiary Structure ◽

Binding Protein ◽

Maltose Binding Protein ◽

Structure Dependence

The leader region of pre-maltose binding protein binds amphiphiles. A model for self-assembly in protein export.

10.1016/s0021-9258(17)36346-9 ◽

1985 ◽

Vol 260 (29) ◽

pp. 15919-15924 ◽

Cited By ~ 1

Author(s):

R Dierstein ◽

W Wickner

Keyword(s):

Self Assembly ◽

Binding Protein ◽

Maltose Binding Protein ◽

Protein Export ◽

Leader Region

Physical interaction between the phage lambda receptor protein and the carrier-immobilized maltose-binding protein of Escherichia coli.

10.1016/s0021-9258(19)68406-1 ◽

1981 ◽

Vol 256 (22) ◽

pp. 11385-11388

Author(s):

P. Bavoil ◽

H. Nikaido

Keyword(s):

Escherichia Coli ◽

Binding Protein ◽

Maltose Binding Protein ◽

Receptor Protein ◽

Physical Interaction ◽

Phage Lambda

Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo.

10.1016/s0021-9258(18)48419-0 ◽

1992 ◽

Vol 267 (2) ◽

pp. 1231-1238

Author(s):

G A Barkocy-Gallagher ◽

P J Bassford

Keyword(s):

Escherichia Coli ◽

Cleavage Site ◽

Binding Protein ◽

Maltose Binding Protein ◽

Signal Peptidase ◽

Signal Peptidase I