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PDBsum entry 1klc
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Growth factor
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PDB id
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1klc
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Contents |
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* Residue conservation analysis
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PDB id:
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Growth factor
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Title:
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Solution structure of tgf-b1, nmr, minimized average structure
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Structure:
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Transforming growth factor-beta 1. Chain: a, b. Synonym: tgf-b1. Engineered: yes. Other_details: 1 mm (in dimer), ph 4.2
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Organ: ovary. Expressed in: cricetulus griseus. Expression_system_taxid: 10029
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NMR struc:
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1 models
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Authors:
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A.P.Hinck,S.J.Archer,S.W.Qian,A.B.Roberts,M.B.Sporn,J.A.Weatherbee, M.L.-S.Tsang,R.Lucas,B.-L.Zhang,J.Wenker,D.A.Torchia
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Key ref:
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A.P.Hinck
et al.
(1996).
Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2.
Biochemistry,
35,
8517-8534.
PubMed id:
DOI:
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Date:
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16-Jan-96
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Release date:
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17-Aug-96
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PROCHECK
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Headers
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References
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P01137
(TGFB1_HUMAN) -
Transforming growth factor beta-1 proprotein from Homo sapiens
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Seq:
Struc:
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390 a.a.
112 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Biochemistry
35:8517-8534
(1996)
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PubMed id:
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Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2.
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A.P.Hinck,
S.J.Archer,
S.W.Qian,
A.B.Roberts,
M.B.Sporn,
J.A.Weatherbee,
M.L.Tsang,
R.Lucas,
B.L.Zhang,
J.Wenker,
D.A.Torchia.
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ABSTRACT
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The three-dimensional solution structure of human transforming growth factor
beta 1 (TGF-beta 1) has been determined using multinuclear magnetic resonance
spectroscopy and a hybrid distance geometry/ simulated annealing algorithm. It
represents one of the first examples of a mammalian protein structure that has
been solved by isotopic labeling of the protein in a eukaryotic cell line and
multinuclear NMR spectroscopy. The solution structure of the 25 kDa
disulfide-linked TGF-beta 1 homodimer was calculated from over 3200 distance and
dihedral angle restraints. The final ensemble of 33 accepted structures had no
NOE or dihedral angle violations greater than 0.30 A and 5.0 degrees,
respectively. The RMSD of backbone atoms for the ensemble of 33 structures
relative to their mean structure was 1.1 A when all residues were used in the
alignment and 0.7 A when loop regions were omitted. The solution structure of
TGF-beta 1 follows two independently determined crystal structures of TGF-beta 2
(Daopin et al., 1992, 1993; Schlunegger & Grütter, 1992, 1993), providing
the first opportunity to examine structural differences between the two isoforms
at the molecular level. Although the structures are very similar, with an RMSD
in backbone atom positions of 1.4 A when loop regions are omitted in the
alignment and 1.9 A when all residues are considered, there are several notable
differences in structure and flexibility which may be related to function. The
clearest example of these is in the beta-turn from residues 69-72: the turn type
found in the solution structure of TGF-beta 1 falls into the category of type
II, whereas that present in the X-ray crystal structure of TGF-beta 2 is more
consistent with a type I turn conformation. This may be of functional
significance as studies using TGF-beta chimeras and deletion mutants indicate
that this portion of the molecule may be important in receptor binding.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.A.Beamish,
P.He,
K.Kottke-Marchant,
and
R.E.Marchant
(2010).
Molecular regulation of contractile smooth muscle cell phenotype: implications for vascular tissue engineering.
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Tissue Eng Part B Rev,
16,
467-491.
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L.Li,
B.P.Orner,
T.Huang,
A.P.Hinck,
and
L.L.Kiessling
(2010).
Peptide ligands that use a novel binding site to target both TGF-β receptors.
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Mol Biosyst,
6,
2392-2402.
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H.G.Laverty,
L.M.Wakefield,
N.L.Occleston,
S.O'Kane,
and
M.W.Ferguson
(2009).
TGF-beta3 and cancer: a review.
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Cytokine Growth Factor Rev,
20,
305-317.
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I.Tesseur,
H.Zhang,
W.Brecht,
J.Corn,
J.S.Gong,
K.Yanagisawa,
M.Michikawa,
K.Weisgraber,
Y.Huang,
and
T.Wyss-Coray
(2009).
Bioactive TGF-beta can associate with lipoproteins and is enriched in those containing apolipoprotein E3.
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J Neurochem,
110,
1254-1262.
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J.Nickel,
W.Sebald,
J.C.Groppe,
and
T.D.Mueller
(2009).
Intricacies of BMP receptor assembly.
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Cytokine Growth Factor Rev,
20,
367-377.
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K.P.Holbourn,
B.Perbal,
and
K.Ravi Acharya
(2009).
Proteins on the catwalk: modelling the structural domains of the CCN family of proteins.
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J Cell Commun Signal,
3,
25-41.
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Y.Xia,
and
A.L.Schneyer
(2009).
The biology of activin: recent advances in structure, regulation and function.
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J Endocrinol,
202,
1.
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C.Grütter,
T.Wilkinson,
R.Turner,
S.Podichetty,
D.Finch,
M.McCourt,
S.Loning,
L.Jermutus,
and
M.G.Grütter
(2008).
A cytokine-neutralizing antibody as a structural mimetic of 2 receptor interactions.
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Proc Natl Acad Sci U S A,
105,
20251-20256.
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PDB codes:
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K.P.Holbourn,
K.R.Acharya,
and
B.Perbal
(2008).
The CCN family of proteins: structure-function relationships.
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Trends Biochem Sci,
33,
461-473.
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C.L.Klaver,
and
M.R.Caplan
(2007).
Bioactive surface for neural electrodes: decreasing astrocyte proliferation via transforming growth factor-beta1.
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J Biomed Mater Res A,
81,
1011-1016.
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T.Shimanuki,
T.Hara,
T.Furuya,
T.Imamura,
and
K.Miyazono
(2007).
Modulation of the functional binding sites for TGF-beta on the type II receptor leads to suppression of TGF-beta signaling.
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Oncogene,
26,
3311-3320.
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A.M.Gressner,
and
R.Weiskirchen
(2006).
Modern pathogenetic concepts of liver fibrosis suggest stellate cells and TGF-beta as major players and therapeutic targets.
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J Cell Mol Med,
10,
76-99.
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B.Ren,
K.O.Yee,
J.Lawler,
and
R.Khosravi-Far
(2006).
Regulation of tumor angiogenesis by thrombospondin-1.
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Biochim Biophys Acta,
1765,
178-188.
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H.H.Keah,
and
M.T.Hearn
(2005).
A molecular recognition paradigm: promiscuity associated with the ligand-receptor interactions of the activin members of the TGF-beta superfamily.
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J Mol Recognit,
18,
385-403.
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G.D.Young,
and
J.E.Murphy-Ullrich
(2004).
Molecular interactions that confer latency to transforming growth factor-beta.
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J Biol Chem,
279,
38032-38039.
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G.D.Young,
and
J.E.Murphy-Ullrich
(2004).
The tryptophan-rich motifs of the thrombospondin type 1 repeats bind VLAL motifs in the latent transforming growth factor-beta complex.
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J Biol Chem,
279,
47633-47642.
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M.de Caestecker
(2004).
The transforming growth factor-beta superfamily of receptors.
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Cytokine Growth Factor Rev,
15,
1.
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S.J.Lee
(2004).
Regulation of muscle mass by myostatin.
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Annu Rev Cell Dev Biol,
20,
61-86.
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W.Sebald,
J.Nickel,
J.L.Zhang,
and
T.D.Mueller
(2004).
Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction.
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Biol Chem,
385,
697-710.
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C.Müller,
S.Richter,
and
U.Rinas
(2003).
Kinetics control preferential heterodimer formation of platelet-derived growth factor from unfolded A- and B-chains.
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J Biol Chem,
278,
18330-18335.
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K.C.Flanders,
and
J.K.Burmester
(2003).
Medical applications of transforming growth factor-beta.
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Clin Med Res,
1,
13-20.
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M.M.Cohen
(2003).
TGF beta/Smad signaling system and its pathologic correlates.
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Am J Med Genet A,
116,
1.
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T.B.Thompson,
T.K.Woodruff,
and
T.S.Jardetzky
(2003).
Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions.
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EMBO J,
22,
1555-1566.
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PDB codes:
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C.C.Boesen,
S.Radaev,
S.A.Motyka,
A.Patamawenu,
and
P.D.Sun
(2002).
The 1.1 A crystal structure of human TGF-beta type II receptor ligand binding domain.
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Structure,
10,
913-919.
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PDB code:
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E.V.Bocharov,
D.M.Korzhnev,
M.J.Blommers,
T.Arvinte,
V.Y.Orekhov,
M.Billeter,
and
A.S.Arseniev
(2002).
Dynamics-modulated biological activity of transforming growth factor beta3.
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J Biol Chem,
277,
46273-46279.
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P.J.Hart,
S.Deep,
A.B.Taylor,
Z.Shu,
C.S.Hinck,
and
A.P.Hinck
(2002).
Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex.
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Nat Struct Biol,
9,
203-208.
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PDB code:
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C.F.Gao,
X.T.Kong,
A.M.Gressner,
and
R.Weiskirchen
(2001).
The expression and antigenicity identification of recombinant rat TGF-beta1 in bacteria.
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Cell Res,
11,
95.
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F.Docagne,
N.Colloc'h,
V.Bougueret,
M.Page,
J.Paput,
M.Tripier,
P.Dutartre,
E.T.MacKenzie,
A.Buisson,
S.Komesli,
and
D.Vivien
(2001).
A soluble transforming growth factor-beta (TGF-beta ) type I receptor mimics TGF-beta responses.
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J Biol Chem,
276,
46243-46250.
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H.H.Keah,
N.Allen,
R.Clay,
R.I.Boysen,
T.Warner,
and
M.T.Hearn
(2001).
Total chemical synthesis of human activin beta(A)[12-116] and related large-loop polypeptides.
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Biopolymers,
60,
279-289.
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J.Yue,
and
K.M.Mulder
(2001).
Transforming growth factor-beta signal transduction in epithelial cells.
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Pharmacol Ther,
91,
1.
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P.K.Shah,
C.M.Buslje,
and
R.Sowdhamini
(2001).
Structural determinants of binding and specificity in transforming growth factor-receptor interactions.
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Proteins,
45,
408-420.
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Q.Liu,
T.Y.Ling,
H.S.Shieh,
F.E.Johnson,
J.S.Huang,
and
S.S.Huang
(2001).
Identification of the high affinity binding site in transforming growth factor-beta involved in complex formation with alpha 2-macroglobulin. Implications regarding the molecular mechanisms of complex formation between alpha 2-macroglobulin and growth factors, cytokines, and hormones.
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J Biol Chem,
276,
46212-46218.
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W.D.Fairlie,
P.K.Russell,
W.M.Wu,
A.G.Moore,
H.P.Zhang,
P.K.Brown,
A.R.Bauskin,
and
S.N.Breit
(2001).
Epitope mapping of the transforming growth factor-beta superfamily protein, macrophage inhibitory cytokine-1 (MIC-1): identification of at least five distinct epitope specificities.
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Biochemistry,
40,
65-73.
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C.H.Ezal,
C.D.Marion,
and
W.C.Smith
(2000).
Primary structure requirements for Xenopus nodal-related 3 and a comparison with regions required by Xenopus nodal-related 2.
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J Biol Chem,
275,
14124-14131.
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M.Böttner,
K.Krieglstein,
and
K.Unsicker
(2000).
The transforming growth factor-betas: structure, signaling, and roles in nervous system development and functions.
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J Neurochem,
75,
2227-2240.
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J.Pellaud,
U.Schote,
T.Arvinte,
and
J.Seelig
(1999).
Conformation and self-association of human recombinant transforming growth factor-beta3 in aqueous solutions.
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J Biol Chem,
274,
7699-7704.
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S.M.Leal,
S.S.Huang,
and
J.S.Huang
(1999).
Interactions of high affinity insulin-like growth factor-binding proteins with the type V transforming growth factor-beta receptor in mink lung epithelial cells.
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J Biol Chem,
274,
6711-6717.
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S.S.Huang,
M.Zhou,
F.E.Johnson,
H.S.Shieh,
and
J.S.Huang
(1999).
An active site of transforming growth factor-beta(1) for growth inhibition and stimulation.
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J Biol Chem,
274,
27754-27758.
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A.Colavita,
S.Krishna,
H.Zheng,
R.W.Padgett,
and
J.G.Culotti
(1998).
Pioneer axon guidance by UNC-129, a C. elegans TGF-beta.
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Science,
281,
706-709.
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C.Secombes,
J.Zou,
G.Daniels,
C.Cunningham,
A.Koussounadis,
and
G.Kemp
(1998).
Rainbow trout cytokine and cytokine receptor genes.
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Immunol Rev,
166,
333-340.
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J.Groppe,
K.Rumpel,
A.N.Economides,
N.Stahl,
W.Sebald,
and
M.Affolter
(1998).
Biochemical and biophysical characterization of refolded Drosophila DPP, a homolog of bone morphogenetic proteins 2 and 4.
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J Biol Chem,
273,
29052-29065.
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J.M.Connolly,
and
D.P.Rose
(1998).
Angiogenesis in two human prostate cancer cell lines with differing metastatic potential when growing as solid tumors in nude mice.
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J Urol,
160,
932-936.
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J.Massagué
(1998).
TGF-beta signal transduction.
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Annu Rev Biochem,
67,
753-791.
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S.S.Huang,
and
J.S.Huang
(1998).
A pentacosapeptide (CKS-25) homologous to retroviral envelope proteins possesses a transforming growth factor-beta activity.
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J Biol Chem,
273,
4815-4818.
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S.S.Huang,
M.A.Cerullo,
F.W.Huang,
and
J.S.Huang
(1998).
Activated thyroglobulin possesses a transforming growth factor-beta activity.
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J Biol Chem,
273,
26036-26041.
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A.Bergner,
T.Muta,
S.Iwanaga,
H.G.Beisel,
R.Delotto,
and
W.Bode
(1997).
Horseshoe crab coagulogen is an invertebrate protein with a nerve growth factor-like domain.
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Biol Chem,
378,
283-287.
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S.S.Huang,
Q.Liu,
F.E.Johnson,
Y.Konish,
and
J.S.Huang
(1997).
Transforming growth factor beta peptide antagonists and their conversion to partial agonists.
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J Biol Chem,
272,
27155-27159.
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Y.A.Muller,
H.W.Christinger,
B.A.Keyt,
and
A.M.de Vos
(1997).
The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding.
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Structure,
5,
1325-1338.
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PDB code:
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A.Bergner,
V.Oganessyan,
T.Muta,
S.Iwanaga,
D.Typke,
R.Huber,
and
W.Bode
(1996).
Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor.
|
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EMBO J,
15,
6789-6797.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
