scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.M202327200 |
P698 | PubMed publication ID | 11960990 |
P50 | author | Christian Cambillau | Q5109395 |
Silvia Spinelli | Q28037071 | ||
Serge Muyldermans | Q39183359 | ||
Lode Wyns | Q48739361 | ||
P2093 | author name string | Francoise Payan | |
Aline Desmyter | |||
Marc Lauwereys | |||
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Camelid heavy-chain variable domains provide efficient combining sites to haptens | Q27621499 | ||
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Lateral recognition of a dye hapten by a llama VHH domain | Q27633538 | ||
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Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodies | Q30766668 | ||
The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formation | Q30803385 | ||
Anatomy of the antibody molecule | Q34060425 | ||
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Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains | Q34662422 | ||
Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrate | Q38333730 | ||
Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire | Q40387210 | ||
T-cell receptor structure and TCR complexes | Q41685092 | ||
Potent enzyme inhibitors derived from dromedary heavy-chain antibodies | Q41782789 | ||
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P433 | issue | 26 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 23645-50 | |
P577 | publication date | 2002-06-28 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology | |
P478 | volume | 277 |
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