Search Results - "Venkatachalapathi, Y V"

The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function by Segrest, JP, Jones, MK, De Loof, H, Brouillette, CG, Venkatachalapathi, YV, Anantharamaiah, GM

“…Site-directed mutagenesis and other molecular biology-based techniques are now available for probing the amphipathic alpha helix structural motif in the…”
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Effect of end group blockage on the properties of a class A amphipathic helical peptide by Venkatachalapathi, Y V, Phillips, M C, Epand, R M, Epand, R F, Tytler, E M, Segrest, J P, Anantharamaiah, G M

“…In a recent classification of biologically active amphipathic alpha-helixes, the lipid-associating domains in exchangeable plasma apolipoproteins have been…”
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Reciprocal effects of apolipoprotein and lytic peptide analogs on membranes. Cross-sectional molecular shapes of amphipathic alpha helixes control membrane stability by Tytler, E M, Segrest, J P, Epand, R M, Nie, S Q, Epand, R F, Mishra, V K, Venkatachalapathi, Y V, Anantharamaiah, G M

“…Apolipoprotein (class A) amphipathic helixes are postulated to act as detergents by virtue of their cross-section being wedge-shaped. Using computer analysis…”
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Apolipoprotein A-I decreases neutrophil degranulation and superoxide production by Blackburn, WD, Dohlman, JG, Venkatachalapathi, YV, Pillion, DJ, Koopman, WJ, Segrest, JP, Anantharamaiah, GM

“…Neutrophils participate in the acute phase response and are often associated with tissue injury in a number of inflammatory disorders. The acute phase response…”
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Conformational analysis of small disulfide loops. Spectroscopic and theoretical studies on a synthetic cyclic tetrapeptide containing cystine by Venkatachalapathi, Y. V, Prasad, B. V. Venkataram, Balaram, P

“…The conformational analysis of the synthetic peptide (formula, see text) has been carried out, as a model for small disulfide loops, in biologically active…”
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Nuclear magnetic resonance investigation of the interactions with phospholipid of an amphipathic alpha-helix-forming peptide of the apolipoprotein class by LUND-KATZ, S, ANANTHARAMAIAH, G. M, VENKATACHALAPTHI, Y. V, SEGREST, J. P, PHILLIPS, M. C

“…To further understand the packing of amphipathic alpha-helices of apolipoproteins in serum lipoproteins, we have investigated the interactions with dimyristoyl…”
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Inhibition of virus-induced cell fusion by apolipoprotein A-I and its amphipathic peptide analogs by Srinivas, R V, Venkatachalapathi, Y V, Rui, Z, Owens, R J, Gupta, K B, Srinivas, S K, Anantharamaiah, G M, Segrest, J P, Compans, R W

“…Apolipoprotein A-I (apoA-I), the major protein component of serum high-density lipoproteins (HDL), was found to inhibit herpes simplex virus (HSV)-induced cell…”
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Determination of beta-turn conformation by laser Raman spectroscopy by Ishizaki, H., Balaram, P., Nagaraj, R., Venkatachalapathi, Y.V., Tu, A.T.

“…To correlate the Raman frequencies of the amide I and III bands to beta-turn structures, three peptides shown to contain beta-turn structure by x-ray…”
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Gas-phase IR spectra of substituted alkylamides by Venkatachalapathi, Y V, Mierke, D F, Taulane, J P, Goodman, M

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Turnover of synthetic class A amphipathic peptide analogues of exchangeable apolipoproteins in rats. Correlation with physical properties by Garber, D W, Venkatachalapathi, Y V, Gupta, K B, Ibdah, J, Phillips, M C, Hazelrig, J B, Segrest, J P, Anantharamaiah, G M

“…Peptide analogues of the class A amphipathic helixes from exchangeable apolipoproteins mimic apolipoprotein (apo) A-I in a number of ways, including the…”
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An incipient 310 helix in Piv-Pro-Pro-Ala-NHMe as a model for peptide folding by Venkatachalapathi, Y. V., Balaram, P.

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Role of amphipathic helixes in HDL structure/function by Anantharamaiah, G M, Brouillette, C G, Engler, J A, De Loof, H, Venkatachalapathi, Y V, Boogaerts, J, Segrest, J P

“…In a recent analysis we classified amphipathic helix domains into a minimum of seven distinct classes. Four amphipathic helix classes are found in…”
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A guest-host approach to oligodepsipeptide structure by Goodman, M., Venkatachalapathi, Y. V., Mammi, S., Katakai, R.

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Use of synthetic peptide analogues to localize lecithin:cholesterol acyltransferase activating domain in apolipoprotein A-I by Anantharamaiah, G M, Venkatachalapathi, Y V, Brouillette, C G, Segrest, J P

“…The major protein of high density lipoprotein (HDL), apolipoprotein (apo) A-I, is the major activator of the plasma enzyme lecithin:cholesterol acyltransferase…”
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An incipient 3(10) helix in Piv-Pro-Pro-Ala-NHMe as a model for peptide folding by Venkatachalapathi, Y V, Balaram, P

“…The molecular mechanism of helix nucleation in peptides and proteins is not yet understood and the question of whether sharp turns in the polypeptide backbone…”
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An incipient 3 10 helix in Piv-Pro-Pro-Ala-NHMe as a model for peptide folding by Venkatachalapathi, Y. V, Balaram, P

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Rotational isomerism about the C alpha-CO bond in proline derivatives. 1H and 13C N.m.r. studies of benzyloxycarbonyl-Pro-N-methylamide and pivaloyl-pro-N-methylamide by Nagaraj, R, Venkatachalapathi, Y V, Balaram, P

“…The 270 MHz 1H n.m.r. spectrum of benzyloxycarbonyl-Pro-N-methylamide in CDCl3 is exchange broadened at 293 degrees K. Spectral lines due to two species are…”
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Turnover of synthetic class A amphiphatic peptide analogues of exchangeable apolipoproteins in rats : correlation with physical properties by GARBER, D. W, VENKATACHALAPATHI, Y. V, GUPTA, K. B, IBDAH, J, PHILLIPS, M. C, HAZELRIG, J. B, SEGREST, J. P, ANANTHARAMAIAH, G. M

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