L G Frenken
Overview
Explore the profile of L G Frenken including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
15
Citations
599
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Szynol A, de Soet J, Sieben-van Tuyl E, Bos J, Frenken L
Antimicrob Agents Chemother
. 2004 Aug;
48(9):3390-5.
PMID: 15328101
Enzymes such as lactoperoxidase and glucose oxidase (GOx) are used as antimicrobial agents in oral care products. Their low specificities and substantiveness can be reduced by covalent coupling of antimicrobial...
2.
Harmsen M, Ruuls R, Nijman I, Niewold T, Frenken L, de Geus B
Mol Immunol
. 2001 Feb;
37(10):579-90.
PMID: 11163394
In addition to conventional antibodies (Abs), camelids possess Abs consisting of only heavy chains. The variable domain of such a heavy-chain Ab (VHH) is fully capable of antigen (Ag) binding....
3.
Perez J, Renisio J, Prompers J, van Platerink C, Cambillau C, Darbon H, et al.
Biochemistry
. 2001 Jan;
40(1):74-83.
PMID: 11141058
Camelids produce functional "heavy chain" antibodies which are devoid of light chains and CH1 domains [Hamers-Casterman, C., et al. (1993) Nature 363, 446-448]. It has been shown that the variable...
4.
Frenken L, van der Linden R, Hermans P, Bos J, Ruuls R, de Geus B, et al.
J Biotechnol
. 2000 Mar;
78(1):11-21.
PMID: 10702907
Recently the existence of 'heavy chain' immunoglobulins in Camelidae has been described. However, as yet there is no data on the binding of this type of antibody to haptens. In...
5.
Spinelli S, Frenken L, Hermans P, Verrips T, Brown K, Tegoni M, et al.
Biochemistry
. 2000 Feb;
39(6):1217-22.
PMID: 10684599
Camelids can produce antibodies devoid of light chains and CH1 domains (Hamers-Casterman, C. et al. (1993) Nature 363, 446-448). Camelid heavy-chain variable domains (VHH) have high affinities for protein antigens...
6.
Woolven B, Frenken L, van der Logt P, Nicholls P
Immunogenetics
. 1999 Oct;
50(1-2):98-101.
PMID: 10541815
No abstract available.
7.
van der Linden R, Frenken L, de Geus B, Harmsen M, Ruuls R, Stok W, et al.
Biochim Biophys Acta
. 1999 Apr;
1431(1):37-46.
PMID: 10209277
Antigen specific llama VHH antibody fragments were compared to antigen specific mouse monoclonal antibodies with respect to specificity, affinity and stability. The llama VHH antibody fragments and the mouse monoclonal...
8.
Frenken L, Hessing J, van den Hondel C, Verrips C
Res Immunol
. 1998 Dec;
149(6):589-99.
PMID: 9835423
No abstract available.
9.
Egmond M, Antheunisse W, van Bemmel C, Ravestein P, Frenken L
Ann N Y Acad Sci
. 1995 Mar;
750:195-201.
PMID: 7785849
No abstract available.
10.
Noble M, Cleasby A, Johnson L, Egmond M, Frenken L
Protein Eng
. 1994 Apr;
7(4):559-62.
PMID: 8029212
The lipase produced by Pseudomonas glumae is monomeric in the crystalline state and has a serine protease-like catalytic triad; Ser87-His285-Asp263. The largest domain of the protein resembles closely a subset...