C H Schmelzer
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Explore the profile of C H Schmelzer including associated specialties, affiliations and a list of published articles.
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Articles
23
Citations
141
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Recent Articles
1.
De Young L, Schmelzer C, Burton L
Protein Sci
. 1999 Dec;
8(11):2513-8.
PMID: 10595557
The recombinant human nerve growth factor (hNGF), brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), neurotrophin 4/5 (NT4/5), and murine NGF (mNGF) dimers all undergo rapid unfolding and dissociation to monomer in...
2.
De Young L, Burton L, Liu J, Powell M, Schmelzer C, Skelton N
Protein Sci
. 1996 Aug;
5(8):1554-66.
PMID: 8844846
The unfolding of recombinant human beta-NGF (NGF) in guanidine hydrochloride (GdnHCl) was found to be time dependent with the denaturation midpoint moving to lower GdnHCl concentration over time. Dissociation and...
3.
Shih A, Laramee G, Schmelzer C, Burton L, Winslow J
J Biol Chem
. 1994 Nov;
269(44):27679-86.
PMID: 7961687
Limited proteolysis and site-directed mutagenesis of human nerve growth factor (hNGF) was utilized to determine the role of the NH2 terminus in p140TrkA (TrkA) receptor function. Purified (6-118)hNGF, representing deletion...
4.
Schmelzer C, Harris R, Butler D, Yedinak C, Wagner K, Burton L
Arch Biochem Biophys
. 1993 May;
302(2):484-9.
PMID: 8489250
This report describes the post-translational modifications of recombinant human differentiation-stimulating factor, a 180-residue glycoprotein that is secreted from transfected Chinese hamster ovary cells. Peptide peptides containing six potential N-glycosylation sites...
5.
Kim K, Alphonso M, Schmelzer C, Lowe D
J Immunol Methods
. 1992 Nov;
156(1):9-17.
PMID: 1385538
Leukemia inhibitory factor (LIF) is known to exhibit multiple functions by regulating the growth and differentiation of multiple normal cell types as well as malignant cells. To have a better...
6.
Kahle P, Burton L, Schmelzer C, Hertel C
J Biol Chem
. 1992 Nov;
267(32):22707-10.
PMID: 1429622
The amino terminus of nerve growth factor (NGF) is susceptible to proteolytic cleavage. A comparison of the bioactivity of highly purified full-length recombinant human (1-118)rhNGF and NH2-terminal truncated (10-118)rhNGF revealed...
7.
Burton L, Schmelzer C, Szonyi E, Yedinak C, Gorrell A
J Neurochem
. 1992 Nov;
59(5):1937-45.
PMID: 1402932
Purified recombinant human nerve growth factor (rhNGF) and submaxillary gland-derived murine NGF (muNGF) were characterized by amino acid composition, polyacrylamide gel electrophoresis (PAGE), reversed-phase HPLC (RP-HPLC), and high-performance ion-exchange chromatography...
8.
Schmelzer C, Burton L, Chan W, Martin E, Gorman C, Ling V, et al.
J Neurochem
. 1992 Nov;
59(5):1675-83.
PMID: 1402913
Recombinant human nerve growth factor (rhNGF) was expressed and secreted by Chinese hamster ovary cells and purified to homogeneity using ion-exchange and reversed-phase (RP) chromatography. The isolated product was shown...
9.
Corrigan A, Bilezikjian L, Carroll R, Bald L, Schmelzer C, Fendly B, et al.
Endocrinology
. 1991 Mar;
128(3):1682-4.
PMID: 1900235
Activins, dimers of inhibin beta subunits, are potent stimulators of FSH secretion in vivo and in vitro and of FSH beta mRNA expression in rat anterior pituitary cultures. In this...
10.
Schmelzer C, Burton L, Tamony C
Protein Expr Purif
. 1990 Sep;
1(1):54-62.
PMID: 2152185
Recombinant human differentiation-stimulating factor (rhD-factor) has been isolated to greater than 95% purity from Chinese hamster ovary cells. RhD-factor is a glycoprotein with an apparent molecular weight of 45.6 kDa...