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J. Van Beeumen

Researcher at Ghent University

Publications -  160
Citations -  6394

J. Van Beeumen is an academic researcher from Ghent University. The author has contributed to research in topics: Peptide sequence & Penicillin binding proteins. The author has an hindex of 44, co-authored 160 publications receiving 6184 citations. Previous affiliations of J. Van Beeumen include University of Edinburgh & Universidade Nova de Lisboa.

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A novel, NH2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity.

TL;DR: A factor able to induce an early local inflammation in rabbit skin was detected in the supernatant of mitogen-stimulated human blood leukocytes, different from IL-1 which was chemically separable from the factor and induced a late rather than an early skin response.
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Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry

TL;DR: PYP is the first example of a protein containing p-coumaric acid, a metabolite previously found only in plants, as a prosthetic group and establishes the photoactive yellow proteins as a new type of photochemically active receptor molecule.
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Homogeneous interferon-inducing 22K factor is related to endogenous pyrogen and interleukin-1

TL;DR: The complete purification and partial sequencing of the 22K factor are reported, finding that the amino-acid sequence of this factor is at least partially homologous to a complementary DNA-derived IL-1 sequence, and it is postulate that the 23K factor also belongs to theIL-1 family.
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Ampd, Essential for Both Beta-Lactamase Regulation and Cell Wall Recycling, Is a Novel Cytosolic N-Acetylmuramyl-L-Alanine Amidase

TL;DR: It is shown here that the AmpD protein is a novel N‐acetylmuramyl‐L‐alanine amidase (E.C.3.5.28) participating in the intracellular recycling of peptido‐glycan fragments and exhibits an exclusive specificity for substrates containing anhydro muramic acid.
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Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23.

TL;DR: It is suggested that structure flexibility and lower sensitivity of secondary structure to temperature variations in the low temperature range are the main structural adaptations of the psychrotrophic enzyme.