FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2405778599> ?p ?o ?g. }

• W2405778599 abstract "level: intermediAte New biological entities (NBEs, therapeutic proteins such as interferons or antibodies) are much more complex than new chemical entities (NCEs), the classic “chemical” active ingredients. First, they are much larger. The average molecular weight of antibodies is ~150,000 g/mol. Second, most NBEs contain three-dimensional structural elements — with the protein secondary and tertiary structure being the most prominent, but quaternary structures are also known for some. The 3D structures are essential for correct bioactivity (1), but they are not rigid, “frozen” structures. Most proteins show a certain structural f lexibility, which enables their correct molecular interactions (e.g., of an antibody with its antigen or receptor). The extreme conformational states of that f lexibility go from the native, correctly folded conformation to a completely denatured state, in which the protein adopts a more or less random conformation. Various interim conformational states can also be adopted. The large size and complex structure of proteins make them prone to instabilities caused by chemical and biological degradations. In addition, a colloidal (physical) instability is often encountered, which can manifest as protein particle formation, aggregation, association, precipitation, and/or adsorption to materials used in, for example, medical devices, primary packaging, and tubing during filling. Colloidal instability and protein aggregate formation present a major problem for long-term storage stability, shipping, and handling (2). Aggregates are defined as protein assemblies of higher molecular order formed by unfolded (denatured) and/ or partially unfolded monomers. By contrast, protein associates are built up of native monomers (Figure 1) and can be redissolved to yield those native monomers again (1). The term protein particles refers to all protein-containing assemblies, independent of the nature and structure of the protein. Figure 1 represents schematically the formation of protein particles. Protein associates are formed by physical association of native protein monomers, whereas aggregates are made of irreversibly or partially denatured monomers. Protein association — the first step in the formation of protein associates — can be studied using the osmotic second virial coefficient (3, 4). It depends strongly on the solution conditions of a formulation. The size of protein particles varies from dimers to extremely large Aggregation" @default.
• W2405778599 created "2016-06-24" @default.
• W2405778599 creator A5042228448 @default.
• W2405778599 creator A5063751301 @default.
• W2405778599 date "2010-01-01" @default.
• W2405778599 modified "2023-09-27" @default.
• W2405778599 title "Protein Therapeutics and Aggregates Characterized By Photon Correlation Spectroscopy An Application for High-Concentration Liquid Formulations" @default.
• W2405778599 cites W1500937540 @default.
• W2405778599 cites W1634384702 @default.
• W2405778599 cites W1973816937 @default.
• W2405778599 cites W1987557110 @default.
• W2405778599 cites W1997140899 @default.
• W2405778599 cites W1998987881 @default.
• W2405778599 cites W2007002347 @default.
• W2405778599 cites W2007228224 @default.
• W2405778599 cites W2014262451 @default.
• W2405778599 cites W2019094632 @default.
• W2405778599 cites W2027397388 @default.
• W2405778599 cites W2034956766 @default.
• W2405778599 cites W2037128898 @default.
• W2405778599 cites W2039898279 @default.
• W2405778599 cites W2045276693 @default.
• W2405778599 cites W2048883633 @default.
• W2405778599 cites W2054133907 @default.
• W2405778599 cites W2054336721 @default.
• W2405778599 cites W2069520354 @default.
• W2405778599 cites W2072119680 @default.
• W2405778599 cites W2090824156 @default.
• W2405778599 cites W2106357609 @default.
• W2405778599 cites W2109798607 @default.
• W2405778599 cites W2129365134 @default.
• W2405778599 cites W2343891719 @default.
• W2405778599 cites W2410106448 @default.
• W2405778599 cites W2479408982 @default.
• W2405778599 cites W2494402508 @default.
• W2405778599 cites W2788291502 @default.
• W2405778599 hasPublicationYear "2010" @default.
• W2405778599 type Work @default.
• W2405778599 sameAs 2405778599 @default.
• W2405778599 citedByCount "2" @default.
• W2405778599 countsByYear W24057785992012 @default.
• W2405778599 countsByYear W24057785992018 @default.
• W2405778599 crossrefType "journal-article" @default.
• W2405778599 hasAuthorship W2405778599A5042228448 @default.
• W2405778599 hasAuthorship W2405778599A5063751301 @default.
• W2405778599 hasConcept C107054158 @default.
• W2405778599 hasConcept C118493188 @default.
• W2405778599 hasConcept C121332964 @default.
• W2405778599 hasConcept C12554922 @default.
• W2405778599 hasConcept C136238340 @default.
• W2405778599 hasConcept C153294291 @default.
• W2405778599 hasConcept C166940927 @default.
• W2405778599 hasConcept C178790620 @default.
• W2405778599 hasConcept C185592680 @default.
• W2405778599 hasConcept C19472624 @default.
• W2405778599 hasConcept C47701112 @default.
• W2405778599 hasConcept C521977710 @default.
• W2405778599 hasConcept C55493867 @default.
• W2405778599 hasConcept C59789625 @default.
• W2405778599 hasConcept C62614982 @default.
• W2405778599 hasConcept C75599170 @default.
• W2405778599 hasConcept C8010536 @default.
• W2405778599 hasConcept C86803240 @default.
• W2405778599 hasConceptScore W2405778599C107054158 @default.
• W2405778599 hasConceptScore W2405778599C118493188 @default.
• W2405778599 hasConceptScore W2405778599C121332964 @default.
• W2405778599 hasConceptScore W2405778599C12554922 @default.
• W2405778599 hasConceptScore W2405778599C136238340 @default.
• W2405778599 hasConceptScore W2405778599C153294291 @default.
• W2405778599 hasConceptScore W2405778599C166940927 @default.
• W2405778599 hasConceptScore W2405778599C178790620 @default.
• W2405778599 hasConceptScore W2405778599C185592680 @default.
• W2405778599 hasConceptScore W2405778599C19472624 @default.
• W2405778599 hasConceptScore W2405778599C47701112 @default.
• W2405778599 hasConceptScore W2405778599C521977710 @default.
• W2405778599 hasConceptScore W2405778599C55493867 @default.
• W2405778599 hasConceptScore W2405778599C59789625 @default.
• W2405778599 hasConceptScore W2405778599C62614982 @default.
• W2405778599 hasConceptScore W2405778599C75599170 @default.
• W2405778599 hasConceptScore W2405778599C8010536 @default.
• W2405778599 hasConceptScore W2405778599C86803240 @default.
• W2405778599 hasLocation W24057785991 @default.
• W2405778599 hasOpenAccess W2405778599 @default.
• W2405778599 hasPrimaryLocation W24057785991 @default.
• W2405778599 hasRelatedWork W1029620603 @default.
• W2405778599 hasRelatedWork W1563133817 @default.
• W2405778599 hasRelatedWork W1576747645 @default.
• W2405778599 hasRelatedWork W1943882461 @default.
• W2405778599 hasRelatedWork W2005524843 @default.
• W2405778599 hasRelatedWork W2008976260 @default.
• W2405778599 hasRelatedWork W2014541368 @default.
• W2405778599 hasRelatedWork W2033921779 @default.
• W2405778599 hasRelatedWork W2075770210 @default.
• W2405778599 hasRelatedWork W2079852318 @default.
• W2405778599 hasRelatedWork W2094995459 @default.
• W2405778599 hasRelatedWork W2099506163 @default.
• W2405778599 hasRelatedWork W2158919479 @default.
• W2405778599 hasRelatedWork W2167353640 @default.
• W2405778599 hasRelatedWork W2342430885 @default.
• W2405778599 hasRelatedWork W2418835340 @default.

• next