Results 201 to 210 of about 16,730 (235)

Human tear lipocalin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Human tear prealbumin, now called tear lipocalin, was originally described as a major protein of human tear fluid, which was thought to be tear specific. However, recent investigations demonstrated that it is identical with lingual von Ebner's gland protein, and is also produced in prostate, nasal mucosa and tracheal mucosa.
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Iron, lipocalin, and kidney epithelia

American Journal of Physiology-Renal Physiology, 2003
Brilliant new discoveries in the field of iron metabolism have revealed novel transmembrane iron transporters, novel hormones that regulate iron traffic, and iron's control of gene expression. An important role for iron in the embryonic kidney was first identified by Ekblom, who studied transferrin (Landschulz W and Ekblom P.
Jun, Yang, Kiyoshi, Mori, Jau Yi, Li, Jonathan, Barasch   +3 more
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Glycodelin: a reproduction-related lipocalin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Glycodelin, a human lipocalin, is a major endometrial protein with at least two differentially glycosylated isoforms. Glycodelin-A (GdA) is purified from human mid-trimester amniotic fluid, where it is secreted from the decidualized endometrium. Glycodelin-S (GdS) is synthesized in the male reproductive tract, mainly in the seminal vesicles, and ...
M, Halttunen, M, Kämäräinen, H, Koistinen   +2 more
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Experimentally determined lipocalin structures

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Twelve structures of distinct members of the lipocalin protein family have been solved experimentally. These structures have revolutionised our understanding of the properties of the lipocalins. Many more members of the family have been crystallised and now await structure solution.
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Beyond the superfamily: the lipocalin receptors

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Lipocalins are characterized by multiple molecular recognition properties including the ability to bind to cell surface receptors. Receptors for a number of lipocalins have been identified. These include receptors for alpha-1-microglobulin, insecticyanin, glycodelin, retinol-binding protein, alpha-1-acid glycoprotein, beta-lactoglobulin and odorant ...
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Lipocalins: unity in diversity

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
B, Akerstrom, D R, Flower, J P, Salier
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Human plasma lipocalins and serum albumin: Plasma alternative carriers?

Journal of Controlled Release, 2016
A. di Masi, V. Trezza, Loris Leboffe, P. Ascenzi   +3 more
semanticscholar   +1 more source

Lipocalin structure and function

Biochemical Society Transactions, 1993
A, Sivaprasadarao, M, Boudjelal, J B, Findlay   +2 more
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The first prokaryotic lipocalins

Trends in Biochemical Sciences, 1995
D R, Flower, C E, Sansom, M E, Beck, T K, Attwood   +3 more
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The menagerie of human lipocalins: a natural protein scaffold for molecular recognition of physiological compounds.

Accounts of Chemical Research, 2015
A. Schiefner, A. Skerra
semanticscholar   +1 more source