scholarly journals Site-specific PEGylation of lidamycin and its antitumor activity

2015 ◽  
Vol 5 (3) ◽  
pp. 264-269 ◽  
Author(s):  
Liang Li ◽  
Boyang Shang ◽  
Lei Hu ◽  
Rongguang Shao ◽  
Yongsu Zhen
Keyword(s):  
Antitumor Activity ◽  
Site Specific

scholarly journals Site-Specific PEGylation Enhances the Pharmacokinetic Properties and Antitumor Activity of Interferon Beta-1b

2013 ◽  
Vol 33 (12) ◽  
pp. 769-777 ◽  
Author(s):  
Ji I. Lee ◽  
Stephen P. Eisenberg ◽  
Mary S. Rosendahl ◽  
Elizabeth A. Chlipala ◽  
Jacquelyn D. Brown ◽  
...  
Keyword(s):  
Antitumor Activity ◽  
Interferon Beta ◽  
Site Specific ◽  
Pharmacokinetic Properties

scholarly journals Site-specific PEGylation endows a mammalian ribonuclease with antitumor activity

2011 ◽  
Vol 12 (3) ◽  
pp. 208-214 ◽  
Author(s):  
Thomas J. Rutkoski ◽  
John A. Kink ◽  
Laura E. Strong ◽  
Ronald T. Raines
Keyword(s):  
Antitumor Activity ◽  
Site Specific

scholarly journals Site-Specific PEGylation of Anti-Mesothelin Recombinant Immunotoxins Increases Half-life and Antitumor Activity

2019 ◽  
Vol 19 (3) ◽  
pp. 812-821 ◽  
Author(s):  
Zeliang Zheng ◽  
Ryuhei Okada ◽  
Hisataka Kobayashi ◽  
Tadanobu Nagaya ◽  
Junxia Wei ◽  
...  
Keyword(s):  
Antitumor Activity ◽  
Half Life ◽  
Site Specific ◽  
Recombinant Immunotoxins

scholarly journals Site-Specific Lipidation of a Small-Sized Protein Binder Enhances the Antitumor Activity through Extended Blood Half-Life

ACS Omega ◽  
2020 ◽  
Vol 5 (31) ◽  
pp. 19778-19784
Author(s):  
Tae Yoon Kim ◽  
You Ree Nam ◽  
Jin Ho Park ◽  
Dong-Eun Lee ◽  
Hak-Sung Kim
Keyword(s):  
Antitumor Activity ◽  
Half Life ◽  
Site Specific

scholarly journals Antitumor Activity of Ribonuclease Multimers Created by Site-Specific Covalent Tethering

2010 ◽  
Vol 21 (9) ◽  
pp. 1691-1702 ◽  
Author(s):  
Thomas J. Rutkoski ◽  
John A. Kink ◽  
Laura E. Strong ◽  
Christine I. Schilling ◽  
Ronald T. Raines
Keyword(s):  
Antitumor Activity ◽  
Site Specific

A Glycosylated Nitric Oxide Donor, β-Gal-NONOate, and its Site-specific Antitumor Activity

2006 ◽  
Vol 339 (7) ◽  
pp. 366-371 ◽  
Author(s):  
Chang Chen ◽  
Yanqiu Shi ◽  
Song Li ◽  
Qingsheng Qi ◽  
Li Gu ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Antitumor Activity ◽  
Nitric Oxide Donor ◽  
Site Specific

Enhanced Circulating Half-Life and Antitumor Activity of a Site-Specific Pegylated Interferon-α Protein Therapeutic

2008 ◽  
Vol 19 (1) ◽  
pp. 299-305 ◽  
Author(s):  
Stacie J. Bell ◽  
Christine M. Fam ◽  
Elizabeth A. Chlipala ◽  
Sharon J. Carlson ◽  
Ji I. Lee ◽  
...  
Keyword(s):  
Antitumor Activity ◽  
Half Life ◽  
Pegylated Interferon ◽  
Interferon Α ◽  
Site Specific ◽  
Protein Therapeutic ◽  
A Site

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.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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