Site-Specific Protein Cross-Linking by Peroxidase-Catalyzed Activation of a Tyrosine-Containing Peptide Tag

2011 ◽  
Vol 22 (1) ◽  
pp. 74-81 ◽  
Author(s):  
Kosuke Minamihata ◽  
Masahiro Goto ◽  
Noriho Kamiya
Keyword(s):  
Specific Protein ◽  
Cross Linking ◽  
Site Specific ◽  
Peptide Tag ◽  
Protein Cross Linking

scholarly journals Site-specific Protein Cross-Linking with Genetically Incorporated 3,4-Dihydroxy-L-Phenylalanine

ChemBioChem ◽  
2009 ◽  
Vol 10 (8) ◽  
pp. 1302-1304 ◽  
Author(s):  
Aiko Umeda ◽  
Gabrielle Nina Thibodeaux ◽  
Jie Zhu ◽  
YungAh Lee ◽  
Zhiwen Jonathan Zhang
Keyword(s):  
Specific Protein ◽  
Cross Linking ◽  
Site Specific ◽  
Protein Cross Linking

scholarly journals Site-specific Protein Cross-Linking with Genetically Incorporated 3,4-Dihydroxy-L-Phenylalanine

ChemBioChem ◽  
2009 ◽  
Vol 10 (9) ◽  
pp. 1426-1426
Author(s):  
Aiko Umeda ◽  
Gabrielle Nina Thibodeaux ◽  
Jie Zhu ◽  
YungAh Lee ◽  
Zhiwen Jonathan Zhang
Keyword(s):  
Specific Protein ◽  
Cross Linking ◽  
Site Specific ◽  
Protein Cross Linking

Kinetic Analysis of Site-specific Photoaptamer–Protein Cross-linking

2004 ◽  
Vol 336 (5) ◽  
pp. 1159-1173 ◽  
Author(s):  
Tad H. Koch ◽  
Drew Smith ◽  
Eduardo Tabacman ◽  
Dominic A. Zichi
Keyword(s):  
Kinetic Analysis ◽  
Cross Linking ◽  
Site Specific ◽  
Protein Cross Linking

scholarly journals Mapping Precursor-binding Site on TatC Subunit of Twin Arginine-specific Protein Translocase by Site-specific Photo Cross-linking

2012 ◽  
Vol 287 (16) ◽  
pp. 13430-13441 ◽  
Author(s):  
Stefan Zoufaly ◽  
Julia Fröbel ◽  
Patrick Rose ◽  
Tobias Flecken ◽  
Carlo Maurer ◽  
...  
Keyword(s):  
Binding Site ◽  
Specific Protein ◽  
Cross Linking ◽  
Site Specific

scholarly journals TFIIIB subunit locations on U6 gene promoter DNA mapped by site-specific protein-DNA photo-cross-linking

FEBS Letters ◽  
2016 ◽  
Vol 590 (10) ◽  
pp. 1488-1497 ◽  
Author(s):  
Jin Joo Kang ◽  
Yoon Soon Kang ◽  
William E. Stumph
Keyword(s):  
Gene Promoter ◽  
Specific Protein ◽  
Cross Linking ◽  
Site Specific ◽  
Promoter Dna ◽  
U6 Gene

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

Transglutaminases: Protein Cross-Linking Enzymes in Tissues and Body Fluids

1994 ◽  
Vol 71 (04) ◽  
pp. 402-415 ◽  
Author(s):  
Daniel Aeschlimann ◽  
Mats Paulsson
Keyword(s):  
Body Fluids ◽  
Cross Linking ◽  
Protein Cross Linking

Tridegin, a Novel Peptidic Inhibitor of Factor XIIIa from the Leech, Haementeria ghilianii, Enhances Fibrinolysis In Vitro

1997 ◽  
Vol 77 (05) ◽  
pp. 0959-0963 ◽  
Author(s):  
Lisa Seale ◽  
Sarah Finney ◽  
Roy T Sawyer ◽  
Robert B Wallis
Keyword(s):  
Potent Inhibitor ◽  
Platelet Rich Plasma ◽  
Factor Xiiia ◽  
Cross Linking ◽  
Fibrinolytic Enzymes ◽  
Small Polypeptide ◽  
Tissue Plasminogen ◽  
Protein Cross Linking

SummaryTridegin is a potent inhibitor of factor Xllla from the leech, Haementeria ghilianii, which inhibits protein cross-linking. It modifies plasmin-mediated fibrin degradation as shown by the absence of D-dimer and approximately halves the time for fibrinolysis. Plasma clots formed in the presence of Tridegin lyse more rapidly when either streptokinase, tissue plasminogen activator or hementin is added 2 h after clot formation. The effect of Tridegin is markedly increased if clots are formed from platelet-rich plasma. Platelet-rich plasma clots are lysed much more slowly by the fibrinolytic enzymes used and if Tridegin is present, the rate of lysis returns almost to that of platelet- free clots. These studies indicate the important role of platelets in conferring resistance to commonly used fibrinolytic enzymes and suggest that protein cross-linking is an important step in this effect. Moreover they indicate that Tridegin, a small polypeptide, may have potential as an adjunct to thrombolytic therapy.

Systematic Engineering of a Protein Nanocage for High-Yield, Site-Specific Modification

2018 ◽  
Author(s):  
Daniel D. Brauer ◽  
Emily C. Hartman ◽  
Daniel L.V. Bader ◽  
Zoe N. Merz ◽  
Danielle Tullman-Ercek ◽  
...  
Keyword(s):  
Small Molecules ◽  
Protein Modification ◽  
Positive Charge ◽  
Specific Protein ◽  
High Yield ◽  
Site Specific ◽  
Protein Cage ◽  
Protein Carriers ◽  
Site Selective ◽  
Targeted Library

<div> <p>Site-specific protein modification is a widely-used strategy to attach drugs, imaging agents, or other useful small molecules to protein carriers. N-terminal modification is particularly useful as a high-yielding, site-selective modification strategy that can be compatible with a wide array of proteins. However, this modification strategy is incompatible with proteins with buried or sterically-hindered N termini, such as virus-like particles like the well-studied MS2 bacteriophage coat protein. To assess VLPs with improved compatibility with these techniques, we generated a targeted library based on the MS2-derived protein cage with N-terminal proline residues followed by three variable positions. We subjected the library to assembly, heat, and chemical selections, and we identified variants that were modified in high yield with no reduction in thermostability. Positive charge adjacent to the native N terminus is surprisingly beneficial for successful extension, and over 50% of the highest performing variants contained positive charge at this position. Taken together, these studies described nonintuitive design rules governing N-terminal extensions and identified successful extensions with high modification potential.</p> </div>

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