pBAD/gIII Kit - Citations

pBAD/gIII Kit - Citations

View additional product information for pBAD/gIII Kit - Citations (V45001)

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Citations & References
Abstract
Inhibition of adipocyte differentiation by resistin-like molecule alpha. Biochemical characterization of its oligomeric nature.
Authors Blagoev Blagoy; Kratchmarova Irina; Nielsen Mogens M; Fernandez Minerva M; Voldby Jesper; Andersen Jens S; Kristiansen Karsten; Pandey Akhilesh; Mann Matthias;
JournalJ Biol Chem
PubMed ID12189153
A novel family of cysteine-rich secreted proteins with unique tissue distribution has recently been identified. One of the members, resistin (for
The COOH Terminus of Arylamine N-Acetyltransferase from Salmonella typhimurium Controls Enzymic Activity.
Authors Mushtaq Adeel; Payton Mark; Sim Edith;
JournalJ Biol Chem
PubMed ID11799105
Arylamine N-acetyltransferases (NATs) are a homologous family of enzymes, which acetylate arylamines, arylhydroxylamines, and arylhydrazines by acetyl transfer from acetyl-coenzyme A (Ac-CoA) and are found in many organisms. NAT was first identified as the enzyme responsible for the inactivation of the anti-tubercular drug isoniazid in humans. The three-dimensional structure of ... More
Specificity determinants and diversification of the Brassica self-incompatibility pollen ligand.
AuthorsChookajorn T, Kachroo A, Ripoll DR, Clark AG, Nasrallah JB,
JournalProc Natl Acad Sci U S A
PubMed ID14694189
Self-incompatibility in crucifers is effected by allele-specific interactions between the highly polymorphic stigmatic S locus receptor kinase (SRK) and its pollen ligand, the S locus cysteine-rich protein (SCR). Here we show that specificity in SCR function is determined by four contiguous amino acids in one variant, indicating that the minimum ... More
A general method for greatly improving the affinity of antibodies by using combinatorial libraries.
AuthorsRajpal A, Beyaz N, Haber L, Cappuccilli G, Yee H, Bhatt RR, Takeuchi T, Lerner RA, Crea R,
JournalProc Natl Acad Sci U S A
PubMed ID15939870
Look-through mutagenesis (LTM) is a multidimensional mutagenesis method that simultaneously assesses and optimizes combinatorial mutations of selected amino acids. The process focuses on a precise distribution within one or more complementarity determining region (CDR) domains and explores the synergistic contribution of amino acid side-chain chemistry. LTM was applied to an ... More