✦ LIBER ✦

Characterization of calmodulin binding domains in TRPV2 and TRPV5 C-tails

✍ Scribed by Blanka Holakovska; Lenka Grycova; Jan Bily; Jan Teisinger

Publisher: Springer
Year: 2010
Tongue: English
Weight: 469 KB
Volume: 40
Category: Article
ISSN: 0939-4451
DOI: 10.1007/s00726-010-0712-2

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Characterization of novel calmodulin bin

Characterization of novel calmodulin binding domains within IQ motifs of IQGAP1

✍ Deok-Jin Jang; Byungkwan Ban; Jin-A Lee 📂 Article 📅 2011 🏛 Korean Society for Molecular and Cellular Biology 🌐 English ⚖ 662 KB

In Vivo Characterization of Tandem C-Ter

In Vivo Characterization of Tandem C-Terminal Thioesterase Domains in Arthrofactin Synthetase

✍ Niran Roongsawang; Kenji Washio; Masaaki Morikawa 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 849 KB

## Abstract Macrocyclization of a peptide or a lipopeptide occurs at the last step of synthesis and is usually catalyzed by a single C‐terminal thioesterase (Te) domain. Arthrofactin synthetase (Arf) from __Pseudomonas__ sp. MIS38 represents a novel type of nonribosomal peptide synthetase that cont

Photolysis of the cyclopentadienyl(hydri

Photolysis of the cyclopentadienyl(hydrido) Complexes C5H5M(CO)3H (M = Cr, Mo, W) in Matrices and in Solution: Characterization of [C5H5W(CO)2H]2 and [C5Me5W(CO)2H]2

✍ Priv.-Doz. Dr. Helmut G. Alt; Khalil A. Mahmoud; Dr. Antony J. Rest 📂 Article 📅 1983 🏛 John Wiley and Sons 🌐 English ⚖ 244 KB 👁 2 views

Binding of ethylene and acetylene to S2−

Binding of ethylene and acetylene to S2− in C5H5MoS4MoC5H5 and on crystalline MoS2: molecular orbital theory

✍ Jenwei Yu; Alfred B. Anderson 📂 Article 📅 1990 🏛 Elsevier Science ⚖ 621 KB

Structures of the PKC-ι kinase domain in

Structures of the PKC-ι kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533–551 in the C-terminal tail and their roles in ATP binding

✍ Takimura, Tetsuo ;Kamata, Kenji ;Fukasawa, Kazuhiro ;Ohsawa, Hirokazu ;Komatani, 📂 Article 📅 2010 🏛 International Union of Crystallography 🌐 English ⚖ 455 KB

Protein kinase C (PKC) plays an essential role in a wide range of cellular functions. Although crystal structures of the PKC-θ, PKC-ι and PKC-βII kinase domains have previously been determined in complexes with small-molecule inhibitors, no structure of a PKC–substrate complex has been determined. I

Characterization of specific interaction

Characterization of specific interactions of coenzymes, regulatory nucleotides and cibacron blue with nucleotide binding domains of enzymes by analytical affinity chromatography

✍ Wayne C. Thresher; Harold E. Swaisgood 📂 Article 📅 1990 🏛 John Wiley and Sons 🌐 English ⚖ 966 KB

## Abstract The dissociation constant for the complex of rhodanese and Cibacron Blue, determined by analytical affinity chromatography using rhodanese immobilized on controlled‐pore glass (CPG) beads (200 nm pore diameter) and aminohexyl‐Cibacron Blue, was 44 μM which agreed well with the kinetic i