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

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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 von Tytler, E M, Segrest, J P, Epand, R M, Nie, S Q, Epand, R F, Mishra, V K, Venkatachalapathi, Y V, Anantharamaiah, G M

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Effect of end group blockage on the properties of a class A amphipathic helical peptide von Venkatachalapathi, Y. V., Phillips, Michael C., Epand, Richard M., Epand, Raquel F., Tytler, Ewan M., Segrest, Jere P., Anantharamaiah, G. M.

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Apolipoprotein A-I decreases neutrophil degranulation and superoxide production von Blackburn, WD, Dohlman, JG, Venkatachalapathi, YV, Pillion, DJ, Koopman, WJ, Segrest, JP, Anantharamaiah, GM

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Conformational analysis of small disulfide loops. Spectroscopic and theoretical studies on a synthetic cyclic tetrapeptide containing cystine von Venkatachalapathi, Y. V, Prasad, B. V. Venkataram, Balaram, P

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Inhibition of virus-induced cell fusion by apolipoprotein A-I and its amphipathic peptide analogs von Srinivas, R. V., Rui, Zheng, Owens, R. J., Compans, R. W., Venkatachalapathi, Y. V., Gupta, K. B., Srinivas, S. K., Anantharamaiah, G. M., Segrest, J. P.

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Nuclear magnetic resonance investigation of the interactions with phospholipid of an amphipathic alpha-helix-forming peptide of the apolipoprotein class von LUND-KATZ, S, ANANTHARAMAIAH, G. M, VENKATACHALAPTHI, Y. V, SEGREST, J. P, PHILLIPS, M. C

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Determination of beta-turn conformation by laser Raman spectroscopy von Ishizaki, H., Balaram, P., Nagaraj, R., Venkatachalapathi, Y.V., Tu, A.T.

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Gas-phase IR spectra of substituted alkylamides von Venkatachalapathi, Yalamoori V., Mierke, Dale F., Taulane, Joseph P., Goodman, Murray

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X-Pro peptides: Synthesis and solution conformation of benzyloxycarbonyl-(Aib-Pro)4methyl ester. Evidence for a novel helical structure von Venkatachalapathi, Y. V., Balaram, P.

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TURNOVER OF SYNTHETIC CLASS-A AMPHIPATHIC PEPTIDE ANALOGS OF EXCHANGEABLE APOLIPOPROTEINS IN RATS - CORRELATION WITH PHYSICAL-PROPERTIES von GARBER, DW, VENKATACHALAPATHI, YV, GUPTA, KB, IBDAH, J, PHILLIPS, MC, HAZELRIG, JB, SEGREST, JP, ANANTHARAMAIAH, GM

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X‐Pro peptides: Synthesis and solution conformation of benzyloxycarbonyl‐(Aib‐Pro) 4 methyl ester. Evidence for a novel helical structure von Venkatachalapathi, Y. V., Balaram, P.

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An incipient 310 helix in Piv-Pro-Pro-Ala-NHMe as a model for peptide folding von Venkatachalapathi, Y. V., Balaram, P.

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X‐Pro peptides: Solution and solid‐state conformation of benzyloxycarbonyl‐(Aib‐Pro) 2 methyl ester, a type I β‐turn von Venkatachalapathi, Y. V., Nair, C. M. K., Vijayan, M., Balaram, P.

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Temperature dependence of peptide NH chemical shifts in benzene: Delineation of solvent-shielded and exposed amide protons von Venkatachalapathi, Y. V., Balaram, P.

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A guest-host approach to oligodepsipeptide structure von 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 von Anantharamaiah, G M, Venkatachalapathi, Y V, Brouillette, C G, Segrest, J P

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X-Pro Peptides: Synthesis and Solution Conformation of Benzyloxycarbonyl-(Aib-Pro) sub(4)- Methyl Ester). Evidence for a Novel Helical Structure von Balaram, P, Venkatachalapathi, Y V

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An incipient 3 10 helix in Piv-Pro-Pro-Ala-NHMe as a model for peptide folding von Venkatachalapathi, Y. V, Balaram, P

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An incipient 3(10) helix in Piv-Pro-Pro-Ala-NHMe as a model for peptide folding von Venkatachalapathi, Y V, Balaram, P

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