Structures of peptides from α‐amino acids methylated at the α‐carbon,

Structural characteristics of .alpha.-helical peptide molecules containing Aib residues

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The Gramicidin A Transmembrane Channel: A Proposed π (L,D) Helix

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The polypeptide 310-helix

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Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational, topographical and dynamic considerations

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Structures of polypeptides from α-amino acids disubstituted at the α-carbon

Toniolo, C., & Benedetti, E. (1991) · Macromolecules · doi:10.1021/ma00014a006 · Cited by 428 · see citing works

Total Chemical Synthesis of a D-Enzyme: The Enantiomers of HIV-1 Protease Show Reciprocal Chiral Substrate Specificity

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A Chemical Approach to Protein Design—Template‐Assembled Synthetic Proteins (TASP)

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Intramolecularly Hydrogen-Bonded Peptide Conformation

Toniolo, C., & Benedetti, E. (1980) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238009105471 · Cited by 394 · see citing works

Conformation of gramicidin A

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The Stereochemistry of Peptides Containing α-Aminoisobutyric Aci

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Three-Dimensional Structure at 0.86 Å of the Uncomplexed form of the Transmembrane Ion Channel Peptide Gramicidin A

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3‐Amino‐2H‐Azirines. Synthons for α,α‐Disubstituted α‐Amino Acids in Heterocycle and Peptide Synthesis [New Analytical Methods (43)]

Heimgartner, H. (1991) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199102381 · Cited by 253 · see citing works

Conformationally restricted peptides through short‐range cyclizations

Toniolo, C. (1990) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1990.tb00052.x · Cited by 248 · see citing works

Preferred conformations of peptides containing α,α‐disubstituted α‐amino acids

Toniolo, C., Bonora, G. M., Bavoso, A., et al. (1983) · Biopolymers · doi:10.1002/bip.360220129 · Cited by 239 · see citing works

Alamethicin, a transmembrane channel

Nagaraj, R., & Balaram, P. (1981) · Accounts of Chemical Research · doi:10.1021/ar00071a005 · Cited by 220 · see citing works

Peptides—XI

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Peptaibol antibiotics: a study on the helical structure of the 2-9 sequence of emerimicins III and IV.

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Conformation of a 16-residue zervamicin IIA analog peptide containing three different structural features: 3(10)-helix, alpha-helix, and beta-bend ribbon.

Karle, I. L., Flippen-Anderson, J., Sukumar, M., et al. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5087 · Cited by 128 · see citing works

Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.

Karle, I. L., Flippen-Anderson, J., Agarwalla, S., et al. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.12.5307 · Cited by 127 · see citing works

Paracelsin, a peptide antibiotic containing α-aminoisobutyric acid, isolated fromTrichoderma ressei Simmons Part A

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Structural versatility of peptides from C α,α ‐dialkylated glycines. I. A conformational energy computation and x‐ray diffraction study of homo‐peptides from C α,α ‐diethylglycine

Benedetti, E., Barone, V., Bavoso, A., et al. (1988) · Biopolymers · doi:10.1002/bip.360270302 · Cited by 108 · see citing works

Characterization at atomic resolution of peptide helical structures

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Alamethicin and related membrane channel forming polypeptides

Mathew, M. K., & Balaram, P. (1983) · Molecular and Cellular Biochemistry · doi:10.1007/bf00225279 · Cited by 83 · see citing works

Structure of conformationally constrained peptides: From model compounds to bioactive peptides

Toniolo, C. (1989) · Biopolymers · doi:10.1002/bip.360280125 · Cited by 82 · see citing works

1160. Peptides. Part XVII. Synthesis of peptides and polymers of some sterically hindered amino-acids via oxazolone intermediates

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First observation of a helical peptide containing a chiral residue without a preferred screw sense

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Structures of the efrapeptins: potent inhibitors of mitochondrial ATPase from the fungus Tolypocladium niveum

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Structure of efrapeptins from the fungus Tolypocladium niveum: peptide inhibitors of mitochondrial ATPase

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Structure and activity of natural peptides

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Crystallographic characterization of conformation of 1-aminocyclopropane-1-carboxylic acid residue (Ac3c) in simple derivatives and peptides*

VALLE, G., Crisma, M., Toniolo, C., et al. (2009) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1989.tb01009.x · Cited by 61 · see citing works

Properties Of The Membrane Modifying Polypeptide Antibiotics Alamethicin And Trichotoxin A-40

Jung, G., Brückner, H. J., & Schmitt, H. (1981) · De Gruyter eBooks · doi:10.1515/9783110861631-006 · Cited by 51 · see citing works

Conformational effects of chiral α,α‐dialkyl amino acids I.C‐Terminal tetrapeptides of emerimicin containing α‐ethylalanine

Marshall, G. R., CLARK, J. D., Dunbar, J. B., et al. (1988) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1988.tb01386.x · Cited by 48 · see citing works

(−)-isovaline: confirmation of its D-(R)-configuration by X-ray analysis of its N-chloroacetyl derivative

Bosch, R., Brückner, H. J., Jung, G., et al. (1982) · Tetrahedron · doi:10.1016/0040-4020(82)80063-x · Cited by 48 · see citing works

Emerimicins III and IV and their ethylalanine12 epimers. Facilitated chemical-enzymatic synthesis and a qualitative evaluation of their solution structures

Słomczyńska, U., Beusen, D. D., Zabrocki, J., et al. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00037a010 · Cited by 47 · see citing works

New aspartame-like sweeteners containing L-(αMe)Phe

Polinelli, S., Broxterman, Q. B., Schoemaker, H., et al. (1992) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(00)80168-7 · Cited by 44 · see citing works

Konformationsanalysen von Modell‐Tripeptiden: Der Einfluss von α,α‐disubstituierten α‐Aminosäuren auf die Sekundärstruktur. Teil I. NMR‐ und CD‐Untersuchungen

Wipf, P., & Heimgartner, H. (1988) · Helvetica Chimica Acta · doi:10.1002/hlca.19880710129 · Cited by 42 · see citing works

A molecular mechanical study of the structure of poly(α‐aminoisobutyric acid)

Alemán, C., Subirana, J. A., & Pérez, J. J. (1992) · Biopolymers · doi:10.1002/bip.360320605 · Cited by 42 · see citing works

Peptides from chiral Cα,α‐disubstituted glycines Synthesis and characterization, conformational energy computations and solution conformational analysis of Cα‐methyl, Cα‐isopropylglycine [(αMe)Val] derivatives and model peptides*

Toniolo, C., Crisma, M., Bonora, G. M., et al. (1991) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1991.tb01435.x · Cited by 37 · see citing works

Conformational studies on host‐guest peptides containing chiral α‐methyl‐α‐amino acids

Altmann, E., Altmann, K., Nebel, K., et al. (1988) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1988.tb01269.x · Cited by 37 · see citing works

Peptides from chiral Cα,α‐disubstituted glycines

VALLE, G., Crisma, M., Toniolo, C., et al. (1991) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1991.tb00770.x · Cited by 36 · see citing works

β‐PLEATED SHEETS IN OLIGOPEPTIDE CRYSTALS

Ashida, T., Tanaka, I., & Yamane, T. (1981) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1981.tb01998.x · Cited by 36 · see citing works

Mise au point Modulations conformationnelles du repliement β en serie peptidique et pseudopeptidique

Aubry, A., Boussard, G., Cung, M. T., et al. (1988) · Journal de Chimie Physique · doi:10.1051/jcp/1988850345 · Cited by 35 · see citing works

A novel peptide conformation: First unequivocal observation of the oxy‐analog of a β‐bend

Toniolo, C., Valle, G., Bonora, G. M., et al. (1986) · Biopolymers · doi:10.1002/bip.360251203 · Cited by 30 · see citing works

Linear oligopeptides. 188.Crystallographic characterization of the conformation of the 1-aminocyclopentane-1-carboxylic acid residue in simple derivatives

Valle, G., Crisma, M., & Toniolo, C. (1988) · Canadian Journal of Chemistry · doi:10.1139/v88-404 · Cited by 29 · see citing works

Konformationsanalysen von Modell‐Tripeptiden: Der Einfluss von α,α‐disubstituierten α‐Aminosäuren auf die Sekundärstruktur. Teil II. Röntgenstrukturanalyse und Konformationsenergie‐Berechnungen

Wipf, P., Kunz, R. W., Prewo, R., et al. (1988) · Helvetica Chimica Acta · doi:10.1002/hlca.19880710130 · Cited by 28 · see citing works

Structural versatility of peptides from Cα,α‐disubstituted glycines: Preferred conformation of the chiral isovaline residue

Nebel, K., Altmann, E., Mutter, M., et al. (1991) · Biopolymers · doi:10.1002/bip.360311002 · Cited by 27 · see citing works

Structural versatility of peptides from Cα,α‐disubstituted glycines: Preferred conformation of the Cα,α‐diphenylglycine residue

Crisma, M., VALLE, G., Bonora, G. M., et al. (1990) · Biopolymers · doi:10.1002/bip.360300103 · Cited by 26 · see citing works

The Conformation of Polypeptides Containing Alternating l- and d-Amino Acids

Chandrasekaran, R., Prasad, B. V. V., & Kopple, K. D. (1978) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409237809177142 · Cited by 21 · see citing works

Bioorganic stereochemistry. A study of the peptide oxazolones from Z-(Aib)n-OH (n = 2-4) in the solid state*

Toniolo, C., Bonora, G. M., Crisma, M., et al. (2009) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1983.tb02135.x · Cited by 20 · see citing works

Monomer units for the β-bend ribbon structure: MeAib peptides

Moretto, V., VALLE, G., Crisma, M., et al. (1992) · International Journal of Biological Macromolecules · doi:10.1016/s0141-8130(05)80024-8 · Cited by 19 · see citing works

tert-Butoxycarbonyl-α-methyl- L -phenylalanyl- L -valine benzyl ester

Roey, P. V., Smith, G. D., Balasubramanian, T. M., et al. (1981) · Acta Crystallographica Section B · doi:10.1107/s0567740881007206 · Cited by 19 · see citing works

A conformation-activity study of the [L-(alpha Me)Phe]3 analog of the formyl methionyl tripeptide chemoattractant.

Toniolo, C., Crisma, M., Pegoraro, S., et al. (1992) · PubMed · Cited by 18 · see citing works

Structural Versatility of Homo‐peptides from Cα,α‐dialkylated Glycines

Toniolo, C. (1986) · British Polymer Journal · doi:10.1002/pi.4980180404 · Cited by 17 · see citing works

Molecular and Crystal Structures of Two Terminally Blocked Tripeptides Corresponding to the 3–5 Sequence of the Peptaibol Antibiotics Antiamoebins

Valle, G., Crisma, M., Toniolo, C., et al. (1989) · Liebigs Annalen der Chemie · doi:10.1002/jlac.198919890159 · Cited by 17 · see citing works

Crystal state conformation of three model monomer units for the β‐bend ribbon structure

VALLE, G., Bardi, R., Piazzesi, A. M., et al. (1991) · Biopolymers · doi:10.1002/bip.360311402 · Cited by 17 · see citing works

Structure of a peptide oxazolone: 2-(1'-benzyloxycarbonylamino-1'-methylethyl)-4,4-dimethyl-5-oxazolone

Nair, C. M. K., & Vijayan, M. (1980) · Acta Crystallographica Section B · doi:10.1107/s0567740880006395 · Cited by 12 · see citing works

Conformationally restricted analogues of anti-aspartame-type sweeteners

Formaggio, F., Crisma, M., Valle, G., et al. (1992) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/p29920001945 · Cited by 11 · see citing works

Synthesis, characterization, and solution conformational analysis of C alpha-methyl-, C alpha-benzylglycine [(alpha Me)Phe] model peptides.

Toniolo, C., Formaggio, F., Crisma, M., et al. (1992) · PubMed · Cited by 11 · see citing works

Activated Amino Acids – Structures of [α‐(Phthalimido)isobutyric] Anhydride, pentachlorophenyl α‐(tert‐Butyloxycarbonylamino)isobutanoate, and Pentachlorophenyl α‐(Benzyloxycarbonylamino)isobutanoate

Valle, G., Toniolo, C., & Jung, G. (1986) · Liebigs Annalen der Chemie · doi:10.1002/jlac.198619861101 · Cited by 10 · see citing works

Spectroscopic study of the secondary structures of enantiomeric N‐tert‐butyloxycarbonyl alanine methyl ester oligomers

Toniolo, C., & Bonora, G. M. (1976) · Journal of Polymer Science Polymer Chemistry Edition · doi:10.1002/pol.1976.170140223 · Cited by 10 · see citing works

Synthesis and conformation of artificial linear and cyclic model peptides containing α,α-disubstituted α-amino acids

Dannecker-Doerig, I., & Heimgartner, H. (1991) · Springer eBooks · doi:10.1007/978-94-011-3034-9_193 · Cited by 8 · see citing works

Crystal and molecular structures of two N-carboxy anhydrides of Cα,α-disubstituted glycines*

Valle, G., Crisma, M., Formaggio, F., et al. (1992) · Zeitschrift für Kristallographie · doi:10.1524/zkri.1992.199.3-4.229 · Cited by 6 · see citing works

Crystal structure of cyclo(C-α-methyl-phenylalanine-proline) (S,S)/(R,S) diastereomeric mixture, C15H18N2O2

VALLE, G., Formaggio, F., Crisma, M., et al. (1992) · Zeitschrift für Kristallographie · doi:10.1524/zkri.1992.202.1-2.168 · Cited by 5 · see citing works

Structure of Z-L-(αMe)Phe-(L-Ala)2-OMe monohydrate

Valle, G., Formaggio, F., Crisma, M., et al. (1993) · Acta Crystallographica Section C Crystal Structure Communications · doi:10.1107/s0108270192010023 · Cited by 4 · see citing works

Preferred conformation of (αMe) Val peptides

Toniolo, C., Crisma, M., Valle, G., et al. (1992) · Peptides · doi:10.1007/978-94-011-2264-1_86 · Cited by 2 · see citing works

Possible ion channel model in crystals of Leu-zervamicin

Karle, I. L., Flippen-Anderson, J. L., Agarwalla, S., et al. (1992) · Peptides · doi:10.1007/978-94-011-2264-1_60 · Cited by 1 · see citing works

Modulators of Protein–Protein Interactions

Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497 · see citing works

Solution Structure, Dimerization, and Dynamics of a Lipophilic α/3₁₀-Helical, C^α-Methylated Peptide. Implications for Folding of Membrane Proteins

Dehner, A., Planker, E., Gemmecker, G., Broxterman, Q. B., Bisson, W., Formaggio, F., Crisma, M., Toniolo, C., & Kessler, H. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010635d · Cited by 40 · see citing works

Cyclic depsipeptides as potential cancer therapeutics

Kitagaki, J., Shi, G., Miyauchi, S., Murakami, S., & Yang, Y. (2014) · Anti-Cancer Drugs · doi:10.1097/cad.0000000000000183 · Cited by 69 · see citing works

Mirabamides E−H, HIV-Inhibitory Depsipeptides from the Sponge Stelletta clavosa

Lu, Z., Wagoner, R. M. V., Harper, M. K., et al. (2011) · Journal of Natural Products · doi:10.1021/np100613p · Cited by 83 · see citing works

Biosynthesis of depsipeptides, or Depsi: The peptides with varied generations

Alonzo, D. A., & Schmeing, T. M. (2020) · Protein Science · doi:10.1002/pro.3979 · Cited by 59 · see citing works

Recent Developments in Depsipeptide Research

Ballard, C. E., Yu, H., & Wang, B. (2002) · Current Medicinal Chemistry · doi:10.2174/0929867023371049 · Cited by 99 · see citing works

The Bicyclic Depsipeptide Family of Histone Deacetylase Inhibitors

Townsend, P. A., Crabb, S. J., Davidson, S. M., Johnson, P., Packham, G., & Ganesan, A. (2007) · Chemical biology · doi:10.1002/9783527619375.ch12 · Cited by 10 · see citing works