Results 1 - 4 of 4

1 An Investigation of DNA-binding Properties of the Non-Receptor

by Tyrosine Kinase Rlk, Beth E. Miskimins
"... Rlk, along with Tec family members Btk and Itk, are predominantly cytoplasmic, but have also been found localized in the nucleus. Rlk has been shown to have a specific DNA-binding relationship with the IFN-? promoter region –56/-36 region. In this study we investigate a shorter isoform of Rlk, one m ..."
Abstract - Add to MetaCart
missing the cysteine-string motif of the N-terminus, and its capacity for DNA-binding.

Mutational analysis of cysteine-string protein function in insulin exocytosis

by Hui Zhang, William L. Kelley, Luke H. Chamberlain, Robert D. Burgoyne, Jochen Lang , 1999
"... Cysteine-string proteins (Csps) are vesicle proteins involved in neurotransmission. They contain at least four domains: an N-terminal J-domain which can interact with the chaperone Hsc70, an adjacent linker region, the defining cysteine rich domain and a variable C terminus. As the relevance of thes ..."
Abstract - Cited by 8 (1 self) - Add to MetaCart
Cysteine-string proteins (Csps) are vesicle proteins involved in neurotransmission. They contain at least four domains: an N-terminal J-domain which can interact with the chaperone Hsc70, an adjacent linker region, the defining cysteine rich domain and a variable C terminus. As the relevance

DOI 10.1007/s00239-009-9234-5 Conservation of Silk Genes in Trichoptera and Lepidoptera

by Toshiki Tamura Æ Frantisˇek Sehnal, N. Yonemura, K. Mita, T. Tamura, N. Yonemura, F. Sehnal
"... Ó The Author(s) 2009. This article is published with open access at Springerlink.com Abstract Larvae of the sister orders Trichoptera and Lepidoptera are characterized by silk secretion from a pair of labial glands. In both orders the silk filament consists of heavy (H)- and light (L)-chain fibroins ..."
Abstract - Add to MetaCart
residues are conserved, including cysteines that were shown to link the L-fibroin and H-fibroin by a disulfide bridge in Lepidoptera. The long internal part of H-fibroins is composed of short motifs arranged in speciesspecific repeats. They are extremely uniform in R. obliterata. Motifs (SX)n, GGX

Identification of a major microfibrilassociated glycoprotein-1-binding domain in fibrillin-2

by Claudio C Werneck , Barbara Crippes Trask , Thomas J Broekelmann , Timothy M Trask , Timothy M Ritty , Fernando Segadeʈ , Robert P Mecham - J. Biol. Chem , 2004
"... Microfibrils are found in the extracellular matrices of most tissues where they serve several functional roles, including the binding and sequestration of growth factors, supplying informational signals through receptor signaling, and providing the basic structural elements for elastic fiber assemb ..."
Abstract - Cited by 3 (0 self) - Add to MetaCart
, although these sites have not been mapped in great detail. In this study, we used a biochemical and molecular approach to precisely identify a prominent MAGP-1-binding site in fibrillin-2. The binding site maps to an 8-cysteine motif, encoded by
Results 1 - 4 of 4