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1
Single-domain antibody fragments with high conformational stability
Single-domain antibody fragments with high conformational stability
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Single-domain antibody fragments with high conformational stability

Dumoulin, Mireille ; Conrath, Katja ; Van Meirhaeghe, Annemie ; Meersman, Filip ; Heremans, Karel ; Frenken, Leon G J ; Muyldermans, Serge ; Wyns, Lode ; Matagne, André

Protein science, 2002-03, Vol.11 (3), p.500-15 [Periódico revisado por pares]

Bristol: Cold Spring Harbor Laboratory Press

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2
Facile Generation of Heat-Stable Antiviral and Antitoxin Single Domain Antibodies from a Semisynthetic Llama Library
Facile Generation of Heat-Stable Antiviral and Antitoxin Single Domain Antibodies from a Semisynthetic Llama Library
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Facile Generation of Heat-Stable Antiviral and Antitoxin Single Domain Antibodies from a Semisynthetic Llama Library

Goldman, Ellen R ; Anderson, George P ; Liu, Jinny L ; Delehanty, James B ; Sherwood, Laura J ; Osborn, Lisa E ; Cummins, Larry B ; Hayhurst, Andrew

Analytical chemistry (Washington), 2006-12, Vol.78 (24), p.8245-8255 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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3
Isotype and glycoform selection for antibody therapeutics
Isotype and glycoform selection for antibody therapeutics
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Isotype and glycoform selection for antibody therapeutics

Jefferis, Roy

Archives of biochemistry and biophysics, 2012-10, Vol.526 (2), p.159-166 [Periódico revisado por pares]

United States: Elsevier Inc

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4
Immunological applications of single-domain llama recombinant antibodies isolated from a naïve library
Immunological applications of single-domain llama recombinant antibodies isolated from a naïve library
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Immunological applications of single-domain llama recombinant antibodies isolated from a naïve library

Monegal, Ana ; Ami, Diletta ; Martinelli, Chiara ; Huang, He ; Aliprandi, Marisa ; Capasso, Paola ; Francavilla, Chiara ; Ossolengo, Giuseppe ; de Marco, Ario

Protein engineering, design and selection, 2009-04, Vol.22 (4), p.273-280 [Periódico revisado por pares]

England: Oxford University Press

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5
Broadly Neutralizing Alphavirus Antibodies Bind an Epitope on E2 and Inhibit Entry and Egress
Broadly Neutralizing Alphavirus Antibodies Bind an Epitope on E2 and Inhibit Entry and Egress
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Broadly Neutralizing Alphavirus Antibodies Bind an Epitope on E2 and Inhibit Entry and Egress

Fox, Julie M. ; Long, Feng ; Edeling, Melissa A. ; Lin, Hueylie ; van Duijl-Richter, Mareike K.S. ; Fong, Rachel H. ; Kahle, Kristen M. ; Smit, Jolanda M. ; Jin, Jing ; Simmons, Graham ; Doranz, Benjamin J. ; Crowe, James E. ; Fremont, Daved H. ; Rossmann, Michael G. ; Diamond, Michael S.

Cell, 2015-11, Vol.163 (5), p.1095-1107 [Periódico revisado por pares]

United States: Elsevier Inc

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6
Recombinant human antibodies against aldehyde-modified apolipoprotein B-100 peptide sequences inhibit atherosclerosis
Recombinant human antibodies against aldehyde-modified apolipoprotein B-100 peptide sequences inhibit atherosclerosis
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Recombinant human antibodies against aldehyde-modified apolipoprotein B-100 peptide sequences inhibit atherosclerosis

SCHIOPU, Alexandru ; BENGTSSON, Jenny ; SÖDERBERG, Ingrid ; JANCIAUSKIENE, Sabina ; LINDGREN, Stefan ; ARES, Mikko P. S ; SHAH, Prediman K ; CARLSSON, Roland ; NILSSON, Jan ; FREDRIKSON, Gunilla Nordin

Circulation (New York, N.Y.), 2004-10, Vol.110 (14), p.2047-2052 [Periódico revisado por pares]

Hagerstown, MD: Lippincott Williams & Wilkins

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7
The B7 family member B7-H6 is a tumor cell ligand for the activating natural killer cell receptor NKp30 in humans
The B7 family member B7-H6 is a tumor cell ligand for the activating natural killer cell receptor NKp30 in humans
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The B7 family member B7-H6 is a tumor cell ligand for the activating natural killer cell receptor NKp30 in humans

Brandt, Cameron S ; Baratin, Myriam ; Yi, Eugene C ; Kennedy, Jacob ; Gao, Zeren ; Fox, Brian ; Haldeman, Betty ; Ostrander, Craig D ; Kaifu, Tomonori ; Chabannon, Christian ; Moretta, Alessandro ; West, Robert ; Xu, Wenfeng ; Vivier, Eric ; Levin, Steven D

The Journal of experimental medicine, 2009-07, Vol.206 (7), p.1495-1503 [Periódico revisado por pares]

United States: The Rockefeller University Press

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8
A bacterial-two-hybrid selection system for one-step isolation of intracellularly functional Nanobodies
A bacterial-two-hybrid selection system for one-step isolation of intracellularly functional Nanobodies
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A bacterial-two-hybrid selection system for one-step isolation of intracellularly functional Nanobodies

Pellis, Mireille ; Pardon, Els ; Zolghadr, Kourosh ; Rothbauer, Ulrich ; Vincke, Cécile ; Kinne, Joerg ; Dierynck, Inge ; Hertogs, Kurt ; Leonhardt, Heinrich ; Messens, Joris ; Muyldermans, Serge ; Conrath, Katja

Archives of biochemistry and biophysics, 2012-10, Vol.526 (2), p.114-123 [Periódico revisado por pares]

United States: Elsevier Inc

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9
High-Affinity, Human Antibody-Like Antibody Fragment (Single-Chain Variable Fragment) Neutralizing the Lethal Factor (LF) of Bacillus anthracis by Inhibiting Protective Antigen-LF Complex Formation
High-Affinity, Human Antibody-Like Antibody Fragment (Single-Chain Variable Fragment) Neutralizing the Lethal Factor (LF) of Bacillus anthracis by Inhibiting Protective Antigen-LF Complex Formation
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High-Affinity, Human Antibody-Like Antibody Fragment (Single-Chain Variable Fragment) Neutralizing the Lethal Factor (LF) of Bacillus anthracis by Inhibiting Protective Antigen-LF Complex Formation

PELAT, Thibaut ; HUST, Michael ; LALLLY, Emmanuelle ; CONDEMINE, Florence ; BOTTEX, Chantal ; VIDAL, Dominique ; LEFRANC, Marie-Paule ; DÜBEL, Stefan ; THULLIER, Philippe

Antimicrobial Agents and Chemotherapy, 2007-08, Vol.51 (8), p.2758-2764 [Periódico revisado por pares]

Washington, DC: American Society for Microbiology

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10
Identification of a receptor required for the anti-inflammatory activity of IVIG
Identification of a receptor required for the anti-inflammatory activity of IVIG
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Identification of a receptor required for the anti-inflammatory activity of IVIG

Anthony, Robert M ; Wermeling, Fredrik ; Karlsson, Mikael C.I ; Ravetch, Jeffrey V

Proceedings of the National Academy of Sciences - PNAS, 2008-12, Vol.105 (50), p.19571-19578 [Periódico revisado por pares]

United States: National Academy of Sciences

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