Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 227,741,291 papers from all fields of science
Search
Sign In
Create Free Account
Post-Translational Protein Processing
Known as:
Post Translational Modification
, Amino Acid Modification, Post-Translational
, Posttranslational Modification
Expand
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include…
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
50 relations
Narrower (1)
Biotinylation
ERO1A gene
ERO1L wt Allele
FRAG1 wt Allele
HERC5 wt Allele
Expand
Broader (1)
Gene Expression
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2002
Highly Cited
2002
Potentiation of glucocorticoid receptor transcriptional activity by sumoylation.
Y. Le Dréan
,
Nathalie Mincheneau
,
P. Le Goff
,
D. Michel
Endocrinology
2002
Corpus ID: 23301280
The glucocorticoid receptor (GR) is a transcription factor, subject to several types of posttranslational modifications including…
Expand
Review
1997
Review
1997
GPI-anchor synthesis in mammalian cells: genes, their products, and a deficiency.
T. Kinoshita
,
K. Ohishi
,
J. Takeda
Journal of Biochemistry (Tokyo)
1997
Corpus ID: 32480693
Protein GPI anchors are ubiquitous in eukaryotic cells. More than 50 mammalian proteins are anchored to the membrane via GPI. GPI…
Expand
Highly Cited
1995
Highly Cited
1995
CXC Chemokines Connective Tissue Activating Peptide-III and Neutrophil Activating Peptide-2 are Heparin/Heparan Sulfate-degrading Enzymes (*)
A. Hoogewerf
,
J. Leone
,
+4 authors
S. Ledbetter
Journal of Biological Chemistry
1995
Corpus ID: 7488129
Heparan sulfate proteoglycans at cell surfaces or in extracellular matrices bind diverse molecules, including growth factors and…
Expand
Review
1995
Review
1995
Phosphorylation of transcription factors and control of the cell cycle.
T. Boulikas
Critical Reviews in Eukaryotic Gene Expression
1995
Corpus ID: 2899376
Protein phosphorylation has evolved as the most versatile posttranslational modification widely used by cells. Signal…
Expand
Highly Cited
1991
Highly Cited
1991
Variations in the cytoskeletal interaction and posttranslational modification of the CD44 homing receptor in macrophages
Robert L. Camp
,
Thomas A. Kraus
,
Ellen Pur
Journal of Cell Biology
1991
Corpus ID: 6343010
Murine CD44 is a cell surface glycoprotein that is thought to play a role in leukocyte migration. We studied the structure and…
Expand
Highly Cited
1991
Highly Cited
1991
Interleukin-6 signals activating junB and TIS11 gene transcription in a B-cell hybridoma
Koichi NAKAJIMA't
,
And Randolph
,
'. Wall
Molecular and Cellular Biology
1991
Corpus ID: 37433868
The events in interleukin-6 (IL-6) signal transduction leading to primary response gene activation were analyzed in murine B-cell…
Expand
Highly Cited
1988
Highly Cited
1988
Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER
M. Geetha-Habib
,
R. Noiva
,
H. Kaplan
,
W. Lennarz
Cell
1988
Corpus ID: 24445586
Review
1987
Review
1987
The covalent modification of eukaryotic proteins with lipid
Bartholomew M Seflon
,
J. Buss
Journal of Cell Biology
1987
Corpus ID: 15863054
surprisingly large number of proteins in eukaryotic ceils are now known to contain covalently bound lipid. Several cell surface…
Expand
Highly Cited
1986
Highly Cited
1986
Ultrastructural colocalization of tyrosinated and detyrosinated alpha- tubulin in interphase and mitotic cells
Gustaaf Geuens
,
G. G. Gundersen
,
R. Nuydens
,
F. Cornelissen
,
Bulinski
,
M. DeBrabander
Journal of Cell Biology
1986
Corpus ID: 6578518
Immunofluorescence with specific peptide antibodies has previously established that tyrosinated (Tyr) and detyrosinated (Glu…
Expand
Highly Cited
1978
Highly Cited
1978
Stage-specific mRNAs coding for subtypes of H2A and H2B histones in the sea urchin embryo
K. Newrock
,
L. H. Cohen
,
M. Hendricks
,
R. Donnelly
,
E. Weinberg
Cell
1978
Corpus ID: 12374500
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE