Pluda S., Mazzocato Y. and A. Angelini (2021). “Peptide-based inhibitors of ADAM and ADAMTS metalloproteinases”. Frontiers in Molecular Biosciences. 8, 703715

Maso L., Trande M., Liberi S., Moro G., Daems E., Linciano S., Sobott F., Covaceuszach S., Cassetta A., Fasolato S., Moretto L.M., De Wael K., Cendron L. and A. Angelini (2021). “Unveiling the binding mode of perfluorooctanoic acid to human serum albumin”. Protein Science. 30, 830-41 

Daems E., Moro G., Berghmans H., Moretto L.M., Dewilde S., Angelini A., Sobott F. and K. De Wael (2021). “Native mass spectrometry for the design and selection of protein bioreceptors for perfluorinated compounds”. Analyst. 146, 2065-73

Mothukuri G.K., Kale S.S., Stenbratt C.L., Zorzi A., Vesin J., Bortoli Chapalay J., Deyle K., Turcatti G., Cendron L., Angelini A. and C. Heinis (2020). “Macrocycle synthesis strategy based on step-wise "adding and reacting" three components enables screening of large combinatorial libraries”. Chemical Science. 11, 7858-63

Moro G., Bottari F., Liberi S., Covaceuszach S., Cassetta A., Angelini A., De Wael K. and L.M. Moretto (2020). “Covalent immobilization of delipidated human serum albumin on poly(pyrrole-2-carboxylic) acid film for the impedimetric detection of perfluorooctanoic acid”. Bioelectrochemistry. 134, 107540

Mesin L., Schiepers A., Ersching J., Barbulescu A., Battaglioni Cavazzoni C., Angelini A., Okada T., Kurosaki T. and G. D. Victora (2020). “Restricted clonality and limited germinal center reentry characterize memory B cell reactivation by boosting”. Cell. 180, 92-106

Linciano S., Pluda S., Bacchin A. and A. Angelini (2019). “Molecular evolution of peptides by yeast surface display technology”. Medicinal Chemistry Communications. 10, 1569-80

Kale S.S., Bergeron-Brlek M., Wu Y., Kumar M.G., Pham M.V., Chapalay J.B., Vesin J., Kong X., Machado J.F., Deyle K., Gonschorek P., Turcatti G., Cendron L., Angelini A. and C. Heinis (2019). “Thiol-to-amine cyclization reaction enables screening of large libraries of macrocyclic compounds and the generation of sub-kilodalton ligands”. Science Advances. 5, eaaw2851

Zorzi A., Linciano S. and A. Angelini (2019). “Non-covalent albumin-binding ligands to extend the circulating half-life of small biotherapeutics”. Medicinal Chemistry Communications. 10, 1068-81

Angelini A., Miyabe Y., Newsted D., Kwan B.H., Kelly R.L., Miyabe C., Jamy M.N., Luster A.D. and K.D. Wittrup (2018). “Directed evolution of broadly crossreactive chemokine-blocking antibodies efficacious in a murine model of arthritis”. Nature Communications. 9, 1461

Kwan B.H., Zhu E.F., Tzeng A., Sugito H.R., Eltahir, A.A., Ma B., Delaney M.K., Murphy P.A., Kauke M.J., Angelini A., Maragh A.M., Hynes R.O., Dranoff G., Cochran, J.R. and K.D. Wittrup (2017). “Integrin-targeted cancer immunotherapy elicits protective adaptive immune responses”. Journal of Experimental Medicine. 214, 1679-90

Pasqual G., Angelini A. and G.D. Victora (2015). “Triggering positive selection of germinal centre B cells by antigen targeting to DEC-205”. Methods in Molecular Biology. 1291, 125-34

Angelini A., Chen T.F., De Picciotto S., Yang N.J., Tzeng A., Santos M.S., Van Deventer J.A., Traxlmayr M.W. and K.D. Wittrup (2015). “Protein engineering and selection using yeast surface display”. Methods in Molecular Biology. 1319, 3-36

Zhu E.F., Gai S.A., Opel C.F., Kwan B.H., Surana R., Mihm M.C., Kauke M.J., Moynihan K.D., Angelini A., Williams R.T., Stephan M.T., Kim J.S., Yaffe M.B., Irvine D.J., Weiner L.M., Dranoff G., K.D. Wittrup (2015). “Synergistic innate and adaptive immune response to combination immunotherapy with anti-tumor antigen antibodies and extended serum half-life IL-2”. Cancer Cell. 27, 489-501

Burg J.S., Ingram J.R., Venkatakrishnan A.J., Jude K.M., Dukkipati A., Feinberg E.N., Angelini A., Waghray D., Dror R.O., Ploegh H.L. and K.C. Garcia (2015). “Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor”. Science. 347, 1113-7

Pollaro L., Raghunathan S., Morales-Sanfrutos J., Angelini A., Kontos S. and C. Heinis (2015). ”Bicyclic peptides conjugated to an albumin-binding tag diffuse efficiently into solid tumors”. Molecular Cancer Therapeutics. 14, 151-61

Chen S., Bertoldo D., Angelini A., Pojer F. and C. Heinis (2014). “Peptide ligands stabilized by small molecules". Angewandte Chemie International Edition. 53, 1602-6

Adalsteinsson V., Tahirova N., Tallapragada N., Yao X., Campiom L., Angelini A., Douce T., Huang C., Kwon D., Wittrup K.D. and J.C. Love (2013). “Single cells from human primary colorectal tumors exhibit polyfunctional heterogeneity in secretions of ELR+ CXC chemokines”. Integrative Biology. 5, 1272-81

Rentero Rebollo I., Angelini A. and C. Heinis (2013). “Phage display libraries of differently sized bicyclic peptides”. Medicinal Chemistry Communications. 4, 145-50

Angelini A., Morales-Sanfrutos J., Diderich P., Chen S. and C. Heinis (2012). “Bicyclization and tethering to albumin yields long-acting peptide antagonists”. Journal of Medicinal Chemistry. 55, 10187-97

Angelini A., Diderich P., Morales-Sanfrutos J., Thurnheer S., Hacker D., Menin L. and C. Heinis (2012). “Chemical macrocyclization of peptides fused to antibody Fc fragments”. Bioconjugate Chemistry. 23, 1856-63

Salvi N., Buratto A., Bornet A., Ulzega S., Rentero Rebollo I., Angelini A., Heinis C. and G. Bodenhausen (2012). “Boosting the sensitivity of ligand-protein screening by NMR of long-lived states”. Journal of the American Chemical Society. 134, 11076–9

Pollaro L., Diderich P., Angelini A., Bellotto S., Wegner H. and C. Heinis (2012). “Measuring net protease activities in biological samples using selective peptidic inhibitors”. Analytical Biochemistry. 427, 18-20

Chen S., Morales-Sanfrutos J., Angelini A., Cutting B. and C. Heinis (2012). “Structurally diverse cyclisation linkers impose different backbone conformations in bicyclic peptides”. ChemBioChem. 13, 1032-8

Angelini A., Cendron L., Chen S., Touati J., Winter G., Zanotti G. and C. Heinis (2012). “Bicyclic peptide inhibitor reveals large contact interface with a protease target”. ACS Chemical Biology. 7, 817–21

Angelini A. and C. Heinis (2011). “Post-translational modification of genetically encoded polypeptide libraries”. Current Opinion in Chemical Biology. 15, 355-61

Touati J., Angelini A., Hinner M.J. and C. Heinis (2011). “Enzymatic cyclisation of peptides with a transglutaminase”. ChemBioChem. 12, 38-42

Angelini A., Cendron L., Seydel A., Barison N., Battistutta R. and G. Zanotti (2009). “Towards the understanding of molecular aspects of Helicobacter pylori cag-PAI”. Book Title: Synchrotron Radiation and Structural Proteomics, Pan Stanford Series on Nanobiotechnology. Edited by C. Riekel and E. Pechkova

Angelini A., Tosi T., Mas P., Acajjaoui S., Zanotti G., Terradot L. and D.J. Hart (2009). “Expression of Helicobacter pylori CagA domains by library-based construct screening”. FEBS Journal. 276, 816-24

Cendron L., Couturier M., Angelini A., Barison N., Stein M. and G. Zanotti (2009). “The Helicobacter pylori CagD (HP0525, Cag24) protein is essential for CagA translocation and maximal induction of interleukin-8 secretion”. Journal of Molecular Biology. 386, 204-17

Angelini A., Cendron L., Goncalves S., Zanotti G. and L. Terradot (2008). “Structural and enzymatic characterisation of HP0496, a YbgC thioesterase from Helicobacter pylori”. Proteins. 72, 1212-21

Cendron L., Tasca E., Seraglio T., Seydel A., Angelini A., Battistutta R., Montecucco C. and G. Zanotti (2007). “The crystal structure of CagS from the Helicobacter pylori pathogenicity island”. Proteins. 69, 440-3 

Cendron L., Seydel A., Angelini A., Battistutta R. and G. Zanotti (2004). “Crystal structure of CagZ, a protein from the Helicobacter pylori pathogenicity island that encodes for a type IV secretion system”. Journal of Molecular Biology. 340, 881-9