@article {2395,
	title = {The crystal structure of the C-terminus of adseverin reveals the actin-binding interface},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {106},
	number = {33},
	year = {2009},
	note = {ISI Document Delivery No.: 484WETimes Cited: 0Cited Reference Count: 21Chumnarnsilpa, Sakesit Lee, Wei Lin Nag, Shalini Kannan, Balakrishnan Larsson, Marten Burtnick, Leslie D. Robinson, Robert C.},
	month = {Aug},
	pages = {13719-13724},
	type = {Article},
	abstract = {Adseverin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins. Adseverin comprises 6 homologous domains (A1-A6), which share 60\% identity with the 6 domains from gelsolin (G1-G6). Adseverin is truncated in comparison to gelsolin, lacking the C-terminal extension that masks the F-actin binding site in calcium-free gelsolin. Biochemical assays have indicated differences in the interaction of the C-terminal halves of adseverin and gelsolin with actin. Gelsolin contacts actin through a major site on G4 and a minor site on G6, whereas adseverin uses a site on A5. Here, we present the X-ray structure of the activated C-terminal half of adseverin (A4-A6). This structure is highly similar to that of the activated form of the C-terminal half of gelsolin (G4-G6), both in arrangement of domains and in the 3 bound calcium ions. Comparative analysis of the actin-binding surfaces observed in the G4-G6/actin structure suggests that adseverin in this conformation will also be able to interact with actin through A4 and A6, whereas the A5 surface is obscured. A single residue mutation in A4-A6 located at the predicted A4/actin interface completely abrogates actin sequestration. A model of calcium-free adseverin, constructed from the structure of gelsolin, predicts that in the absence of a gelsolin-like C-terminal extension the interaction between A2 and A6 provides the steric inhibition to prevent interaction with F-actin. We propose that calcium binding to the N terminus of adseverin dominates the activation process to expose the F-actin binding site on A2.},
	keywords = {74-KDA PROTEIN, ACTIVATION, calcium activated, EXOCYTOSIS, gelsolin, HALF, LOCALIZATION, SCINDERIN, SITE, TIRF},
	isbn = {0027-8424},
	url = {<Go to ISI>://000269078700019},
	author = {Chumnarnsilpa, S. and Lee, W. L. and Nag, S. and Kannan, B. and Larsson, M. and Burtnick, L. D. and Robinson, R. C.}
}
@article {450,
	title = {Structural investigation of Silicalite-I loaded with n-hexane by X-ray diffraction, Si-29 MAS NMR, and molecular modeling},
	journal = {Chemistry of Materials},
	volume = {14},
	number = {5},
	year = {2002},
	note = {ISI Document Delivery No.: 555JCTimes Cited: 23Cited Reference Count: 25},
	month = {May},
	pages = {2192-2198},
	type = {Article},
	abstract = {{The room temperature (298 K) structure of zeolite Silicalite-I loaded with approximately eight n-hexane molecules per unit cell was solved from twinned single-crystal X-ray diffraction (XRD) data in the monoclinic space group P12(1)/n1 with a = 19.8247(2) Angstrom},
	keywords = {ADSORPTION, ALKANES, ENERGY-MINIMIZATION CALCULATIONS, LOCALIZATION, NAPHTHALENE, ORTHORHOMBIC FRAMEWORK, POWDER DIFFRACTION, SIMULATIONS, ZEOLITE H-ZSM-5, ZSM-5},
	isbn = {0897-4756},
	url = {<Go to ISI>://000175790100041},
	author = {Morell, H. and Angermund, K. and Lewis, A. R. and Brouwer, D. H. and Fyfe, C. A. and Gies, H.}
}
@article {5048,
	title = {Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe, interacts with a phosphatidylinositol 4-kinase},
	journal = {Journal of Biological Chemistry},
	volume = {276},
	number = {8},
	year = {2001},
	note = {ISI Document Delivery No.: 404RUTimes Cited: 27Cited Reference Count: 35},
	month = {Feb},
	pages = {5932-5942},
	type = {Article},
	abstract = {The proposed function of Cdc4p, an essential contractile ring protein in Schizosaccharomyces pombe, is that of a myosin essential light chain. However, five conditionally lethal cdc4 alleles exhibit complementation in diploids. Such interallelic complementation is not readily explained if the sole function of Cde4p is that of a myosin essential light chain. Complementation of cdc4 alleles could occur only if different mutant forms can assemble into an active oligomeric complex or if Cdc4p has more than one essential function. To search for other proteins that may interact with Cdc4p, we performed a two-hybrid screen and identified two such candidates: one similar to Saccharomyces cerevisiae Vps27p and the other a putative phosphatidylinositol (PI) 4-kinase. finding of Cdc4p to the latter and to myosin heavy chain (Myo2p) was confirmed by immunosorbent assays. Deletion studies demonstrated interaction between the Cdc4p C-terminal domain and the PI 4-kinase C-terminal domain. Furthermore, interaction was abolished by the Cdc4p C-terminal domain point mutation, Gly(107) to Ser. This allele also causes failure of cytokinesis. Ectopic expression of the PI 4-kinase C-terminal domain caused cytokinesis defects that were most extreme in cells carrying the G107S allele. We suggest that Cdc4p plays multiple roles in cytokinesis and that interaction with a PI I-kinase may be important for contractile ring assembly and/or function.},
	keywords = {ACTOMYOSIN RING, BINDING, CELL-DIVISION CYCLE, F-ACTIN, FISSION YEAST, GENE, IDENTIFICATION, LIGHT-CHAIN, LOCALIZATION, MYOSIN HEAVY-CHAIN},
	isbn = {0021-9258},
	url = {<Go to ISI>://000167115100071},
	author = {Desautels, M. and Den Haese, J. P. and Slupsky, C. M. and McIntosh, L. P. and Hemmingsen, S. M.}
}
@article {3106,
	title = {CLONING, SEQUENCING, AND VISCOMETRIC ADHESION ANALYSIS OF HEAT-RESISTANT AGGLUTININ 1, AN INTEGRAL MEMBRANE HEMAGGLUTININ FROM ESCHERICHIA-COLI-O9-H10-K99},
	journal = {Infection and Immunity},
	volume = {62},
	number = {11},
	year = {1994},
	note = {ISI Document Delivery No.: PN304Times Cited: 13Cited Reference Count: 45},
	month = {Nov},
	pages = {5020-5026},
	type = {Article},
	abstract = {The gene encoding a mannose-resistant hemagglutinating protein was cloned from Escherichia coli 09:H10:K99. The hemagglutinin is different from two other mannose-resistant hemagglutinins in this strain, K99 and F41. The agglutinin, named heat-resistant agglutinin 1 (HRA1) since heating to 70 degrees C does not destroy its aggregative properties, strongly agglutinates human, pig, and dog erythrocytes, shows little or no affinity towards cow and chicken erythrocytes, but agglutinates human colon adenocarcinoma 201 (COLO 201) cells. The hra1 gene present on the recombinant plasmid pETE1 was localized by subcloning, and its nucleotide sequence was determined. The gene consists of a 792-bp open reading frame coding for a putative protein of 29 kDa with a predicted N-terminal secretory signal sequence. HRA1 shares no significant identity with data base protein sequences. HRA1 is strongly associated with the bacterial membrane, resisting sonication and isolation attempts based upon standard adhesin purification techniques. N-terminal sequencing of a unique 25-kDa band present in polyacrylamide gels of outer membrane preparations of bacteria harboring pETE1 correlated with the predicted N-terminal amino acid sequence of HRA1 after cleavage of the signal peptide. A viscometric agglutination assay sensitive to the strength of bacterial adhesion shows that the agglutination mediated by bacteria expressing HRA1 is weaker than that of bacteria bearing the F41 adhesin, probably because of the high-molecular-weight, multivalent nature of the latter adhesin. Our observations suggest that HRA1 is a monomeric outer membrane agglutinin.},
	keywords = {ANTIGEN, BACTERIA, DNA, K99, LOCALIZATION, NONFIMBRIAL, OUTER-MEMBRANE, PROTEINS, PURIFICATION, STRAINS},
	isbn = {0019-9567},
	url = {<Go to ISI>://A1994PN30400046},
	author = {Lutwyche, P. and Rupps, R. and Cavanagh, J. and Warren, R. A. J. and Brooks, D. E.}
}
@inbook {3163,
	title = {MUON SPIN RELAXATION STUDIES OF CYCLOHEXADIENYL RADICALS IN NAUSY},
	booktitle = {Zeolites and Related Microporous Materials: State of the Art 1994},
	series = {Studies in Surface Science and Catalysis},
	volume = {84},
	year = {1994},
	note = {ISI Document Delivery No.: BD02ETimes Cited: 3Cited Reference Count: 22Proceedings Paper10th International Zeolite ConferenceJUL 17-22, 1994GARMISCH PARTENKIR, GERMANYSARA BURGERHARTSTRAAT 25, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	pages = {469-475},
	publisher = {Elsevier Science Publ B V},
	organization = {Elsevier Science Publ B V},
	address = {Amsterdam},
	abstract = {The avoided level crossing muon spin resonance (ALC-mu SR) technique is a promising new tool that can be used as a highly sensitive microscopic probe of radical motions in zeolites. We report a recent experiment in which this technique was used to identify a muonated cyclohexadienyl radical (C(6)H(6)Mu) and explore its reorientational dynamics in NaUSY. The observed evolution of the Delta M=1 ALC resonance lines are interpreted in terms of the site exchange dynamics of the radical.},
	keywords = {benzene, DIFFUSION, LEVEL-CROSSING RESONANCE, LOCALIZATION, MOLECULAR-DYNAMICS, NAX, NMR, NUCLEAR MAGNETIC-RESONANCE, SODIUM-Y ZEOLITE},
	isbn = {0-444-81847-2},
	url = {<Go to ISI>://A1994BD02E00057},
	author = {Shelley, M. and Arseneau, D. J. and Senba, M. and Pan, J. J. and Snooks, R. and Kreitzman, S. R. and Fleming, Donald G. and Roduner, E.},
	editor = {Weitkamp, J. and Karge, H. G. and Pfeifer, H. and Holderich, W.}
}
