PDBsum entry 1bar

Go to PDB code: 
protein Protein-protein interface(s) links
Growth factor PDB id
Protein chains
127 a.a. *
138 a.a. *
Waters ×36
* Residue conservation analysis
PDB id:
Name: Growth factor
Title: Three-dimensional structures of acidic and basic fibroblast growth factors
Structure: Acidic fibroblast growth factor. Chain: a, b. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Tetramer (from PQS)
2.70Å     R-factor:   0.177    
Authors: X.Zhu,H.Komiya,A.Chirino,S.Faham,G.M.Fox,T.Arakawa,B.T.Hsu, D.C.Rees
Key ref: X.Zhu et al. (1991). Three-dimensional structures of acidic and basic fibroblast growth factors. Science, 251, 90-93. PubMed id: 1702556 DOI: 10.1126/science.1702556
29-Sep-92     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P03968  (FGF1_BOVIN) -  Fibroblast growth factor 1
155 a.a.
127 a.a.*
Protein chain
Pfam   ArchSchema ?
P03968  (FGF1_BOVIN) -  Fibroblast growth factor 1
155 a.a.
138 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   7 terms 
  Biological process     mesonephric epithelium development   18 terms 
  Biochemical function     S100 protein binding     6 terms  


DOI no: 10.1126/science.1702556 Science 251:90-93 (1991)
PubMed id: 1702556  
Three-dimensional structures of acidic and basic fibroblast growth factors.
X.Zhu, H.Komiya, A.Chirino, S.Faham, G.M.Fox, T.Arakawa, B.T.Hsu, D.C.Rees.
Members of the fibroblast growth factor (FGF) family of proteins stimulate the proliferation and differentiation of a variety of cell types through receptor-mediated pathways. The three-dimensional structures of two members of this family, bovine acidic FGF and human basic FGF, have been crystallographically determined. These structures contain 12 antiparallel beta strands organized into a folding pattern with approximate threefold internal symmetry. Topologically equivalent folds have been previously observed for soybean trypsin inhibitor and interleukins-1 beta and -1 alpha. The locations of sequences implicated in receptor and heparin binding by FGF are presented. These sites include beta-sheet strand 10, which is adjacent to the site of an extended sequence insertion in several oncogene proteins of the FGF family, and which shows sequence conservation among the FGF family and interleukin-1 beta.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21506104 N.A.Sunmonu, K.Li, and J.Y.Li (2011).
Numerous isoforms of Fgf8 reflect its multiple roles in the developing brain.
  J Cell Physiol, 226, 1722-1726.  
21339643 T.M.Marin, K.Keith, B.Davies, D.A.Conner, P.Guha, D.Kalaitzidis, X.Wu, J.Lauriol, B.Wang, M.Bauer, R.Bronson, K.G.Franchini, B.G.Neel, and M.I.Kontaridis (2011).
Rapamycin reverses hypertrophic cardiomyopathy in a mouse model of LEOPARD syndrome-associated PTPN11 mutation.
  J Clin Invest, 121, 1026-1043.  
20492474 J.L.Dreyfuss, C.V.Regatieri, M.A.Lima, E.J.Paredes-Gamero, A.S.Brito, S.F.Chavante, R.Belfort, M.E.Farah, and H.B.Nader (2010).
A heparin mimetic isolated from a marine shrimp suppresses neovascularization.
  J Thromb Haemost, 8, 1828-1837.  
20640153 S.Li, E.Bock, and V.Berezin (2010).
Neuritogenic and neuroprotective properties of Peptide agonists of the fibroblast growth factor receptor.
  Int J Mol Sci, 11, 2291-2305.  
19267679 M.E.Gasparian, P.A.Elistratov, N.I.Drize, I.N.Nifontova, D.A.Dolgikh, and M.P.Kirpichnikov (2009).
Overexpression in Escherichia coli and purification of human fibroblast growth factor (FGF-2).
  Biochemistry (Mosc), 74, 221-225.  
19574212 M.Zakrzewska, A.Wiedlocha, A.Szlachcic, D.Krowarsch, J.Otlewski, and S.Olsnes (2009).
Increased protein stability of FGF1 can compensate for its reduced affinity for heparin.
  J Biol Chem, 284, 25388-25403.  
18701883 O.Alsmadi, B.F.Meyer, F.Alkuraya, S.Wakil, F.Alkayal, H.Al-Saud, K.Ramzan, and M.Al-Sayed (2009).
Syndromic congenital sensorineural deafness, microtia and microdontia resulting from a novel homoallelic mutation in fibroblast growth factor 3 (FGF3).
  Eur J Hum Genet, 17, 14-21.  
18773489 S.Liao, J.Bodmer, D.Pietras, M.Azhar, T.Doetschman, and J.e.l. .J.Schultz (2009).
Biological functions of the low and high molecular weight protein isoforms of fibroblast growth factor-2 in cardiovascular development and disease.
  Dev Dyn, 238, 249-264.  
17786931 I.Prudovsky, F.Tarantini, M.Landriscina, D.Neivandt, R.Soldi, A.Kirov, D.Small, K.M.Kathir, D.Rajalingam, and T.K.Kumar (2008).
Secretion without Golgi.
  J Cell Biochem, 103, 1327-1343.  
  17277441 N.Kulahin, V.Kiselyov, A.Kochoyan, O.Kristensen, J.S.Kastrup, V.Berezin, E.Bock, and M.Gajhede (2007).
Structure of rat acidic fibroblast growth factor at 1.4 A resolution.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 65-68.
PDB code: 2j3p
17339340 R.Goetz, A.Beenken, O.A.Ibrahimi, J.Kalinina, S.K.Olsen, A.V.Eliseenkova, C.Xu, T.A.Neubert, F.Zhang, R.J.Linhardt, X.Yu, K.E.White, T.Inagaki, S.A.Kliewer, M.Yamamoto, H.Kurosu, Y.Ogawa, M.Kuro-o, B.Lanske, M.S.Razzaque, and M.Mohammadi (2007).
Molecular insights into the klotho-dependent, endocrine mode of action of fibroblast growth factor 19 subfamily members.
  Mol Cell Biol, 27, 3417-3428.
PDB codes: 2p23 2p39
16995857 A.Canales, R.Lozano, B.López-Méndez, J.Angulo, R.Ojeda, P.M.Nieto, M.Martín-Lomas, G.Giménez-Gallego, and J.Jiménez-Barbero (2006).
Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue.
  FEBS J, 273, 4716-4727.
PDB code: 2erm
16806456 D.B.Pike, S.Cai, K.R.Pomraning, M.A.Firpo, R.J.Fisher, X.Z.Shu, G.D.Prestwich, and R.A.Peattie (2006).
Heparin-regulated release of growth factors in vitro and angiogenic response in vivo to implanted hyaluronan hydrogels containing VEGF and bFGF.
  Biomaterials, 27, 5242-5251.  
  17142906 M.Azarkan, A.Garcia-Pino, R.Dibiani, L.Wyns, R.Loris, and D.Baeyens-Volant (2006).
Crystallization and preliminary X-ray analysis of a protease inhibitor from the latex of Carica papaya.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1239-1242.  
16374783 Y.J.Huang, R.Tejero, R.Powers, and G.T.Montelione (2006).
A topology-constrained distance network algorithm for protein structure determination from NOESY data.
  Proteins, 62, 587-603.  
15954154 H.Yin, and A.D.Hamilton (2005).
Strategies for targeting protein-protein interactions with synthetic agents.
  Angew Chem Int Ed Engl, 44, 4130-4163.  
15863029 M.Mohammadi, S.K.Olsen, and O.A.Ibrahimi (2005).
Structural basis for fibroblast growth factor receptor activation.
  Cytokine Growth Factor Rev, 16, 107-137.  
15924284 Q.Wu, J.Wang, L.Zhang, A.Hong, and J.Ren (2005).
Molecular recognition of basic fibroblast growth factor by polyoxometalates.
  Angew Chem Int Ed Engl, 44, 4048-4052.  
15382229 M.J.Bernett, T.Somasundaram, and M.Blaber (2004).
An atomic resolution structure for human fibroblast growth factor 1.
  Proteins, 57, 626-634.
PDB code: 1rg8
12717444 C.Bossard, H.Laurell, L.Van den Berghe, S.Meunier, C.Zanibellato, and H.Prats (2003).
Translokin is an intracellular mediator of FGF-2 trafficking.
  Nat Cell Biol, 5, 433-439.  
14502567 C.Ito, Y.Saitoh, Y.Fujita, Y.Yamazaki, T.Imamura, S.Oka, and S.Suzuki (2003).
Decapeptide with fibroblast growth factor (FGF)-5 partial sequence inhibits hair growth suppressing activity of FGF-5.
  J Cell Physiol, 197, 272-283.  
14627732 S.R.Brych, J.Kim, T.M.Logan, and M.Blaber (2003).
Accommodation of a highly symmetric core within a symmetric protein superfold.
  Protein Sci, 12, 2704-2718.
PDB codes: 1jy0 1m16 1nzk 1p63
11964220 D.G.Vanselow (2002).
Role of constraint in catalysis and high-affinity binding by proteins.
  Biophys J, 82, 2293-2303.  
11964252 M.Zamai, C.Hariharan, D.Pines, M.Safran, A.Yayon, V.R.Caiolfa, R.Cohen-Luria, E.Pines, and A.H.Parola (2002).
Nature of Interaction between basic fibroblast growth factor and the antiangiogenic drug 7,7-(carbonyl-bis[imino-N-methyl-4,2-pyrrolecarbonylimino[N-methyl-4,2-pyrrole]-carbonylimino])-bis-(1,3-naphtalene disulfonate). II. Removal of polar interactions affects protein folding.
  Biophys J, 82, 2652-2664.  
12385863 R.C.Melcangi, L.Martini, and M.Galbiati (2002).
Growth factors and steroid hormones: a complex interplay in the hypothalamic control of reproductive functions.
  Prog Neurobiol, 67, 421-449.  
  11276432 D.M.Ornitz, and N.Itoh (2001).
Fibroblast growth factors.
  Genome Biol, 2, REVIEWS3005.  
11223514 H.J.Hecht, R.Adar, B.Hofmann, O.Bogin, H.Weich, and A.Yayon (2001).
Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces.
  Acta Crystallogr D Biol Crystallogr, 57, 378-384.
PDB code: 1g82
11378392 J.Schoorlemmer, and M.Goldfarb (2001).
Fibroblast growth factor homologous factors are intracellular signaling proteins.
  Curr Biol, 11, 793-797.  
11785766 L.Pellegrini (2001).
Role of heparan sulfate in fibroblast growth factor signalling: a structural view.
  Curr Opin Struct Biol, 11, 629-634.  
11486033 P.Bellosta, A.Iwahori, A.N.Plotnikov, A.V.Eliseenkova, C.Basilico, and M.Mohammadi (2001).
Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis.
  Mol Cell Biol, 21, 5946-5957.
PDB code: 1ijt
11714927 S.R.Brych, S.I.Blaber, T.M.Logan, and M.Blaber (2001).
Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.
  Protein Sci, 10, 2587-2599.
PDB codes: 1jqz 1jt3 1jt4 1jt5 1jt7 1jtc
11724555 S.Ye, Y.Luo, W.Lu, R.B.Jones, R.J.Linhardt, I.Capila, T.Toida, M.Kan, H.Pelletier, and W.L.McKeehan (2001).
Structural basis for interaction of FGF-1, FGF-2, and FGF-7 with different heparan sulfate motifs.
  Biochemistry, 40, 14429-14439.
PDB codes: 1qqk 1qql
11259845 T.Arakawa, S.J.Prestrelski, W.C.Kenney, and J.F.Carpenter (2001).
Factors affecting short-term and long-term stabilities of proteins.
  Adv Drug Deliv Rev, 46, 307-326.  
10618369 D.J.Stauber, A.D.DiGabriele, and W.A.Hendrickson (2000).
Structural interactions of fibroblast growth factor receptor with its ligands.
  Proc Natl Acad Sci U S A, 97, 49-54.
PDB code: 1djs
11101304 E.Doss-Pepe, P.Deprez, N.C.Inestrosa, and B.Brodsky (2000).
Interaction of collagen-like peptide models of asymmetric acetylcholinesterase with glycosaminoglycans: spectroscopic studies of conformational changes and stability.
  Biochemistry, 39, 14884-14892.  
10819962 R.M.Lozano, A.Pineda-Lucena, C.Gonzalez, M.Angeles Jiménez, P.Cuevas, M.Redondo-Horcajo, J.M.Sanz, M.Rico, and G.Giménez-Gallego (2000).
1H NMR structural characterization of a nonmitogenic, vasodilatory, ischemia-protector and neuromodulatory acidic fibroblast growth factor.
  Biochemistry, 39, 4982-4993.
PDB codes: 1dzc 1dzd
10748229 Y.Liu, A.J.Chirino, Z.Misulovin, C.Leteux, T.Feizi, M.C.Nussenzweig, and P.J.Bjorkman (2000).
Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand.
  J Exp Med, 191, 1105-1116.
PDB codes: 1dqg 1dqo
10490103 A.N.Plotnikov, J.Schlessinger, S.R.Hubbard, and M.Mohammadi (1999).
Structural basis for FGF receptor dimerization and activation.
  Cell, 98, 641-650.
PDB code: 1cvs
10097093 G.Venkataraman, R.Raman, V.Sasisekharan, and R.Sasisekharan (1999).
Molecular characteristics of fibroblast growth factor-fibroblast growth factor receptor-heparin-like glycosaminoglycan complex.
  Proc Natl Acad Sci U S A, 96, 3658-3663.  
10051565 G.Venkataraman, Z.Shriver, J.C.Davis, and R.Sasisekharan (1999).
Fibroblast growth factors 1 and 2 are distinct in oligomerization in the presence of heparin-like glycosaminoglycans.
  Proc Natl Acad Sci U S A, 96, 1892-1897.  
10328267 J.K.Dattagupta, A.Podder, C.Chakrabarti, U.Sen, D.Mukhopadhyay, S.K.Dutta, and M.Singh (1999).
Refined crystal structure (2.3 A) of a double-headed winged bean alpha-chymotrypsin inhibitor and location of its second reactive site.
  Proteins, 35, 321-331.
PDB code: 2wbc
10413500 K.M.Patrie, M.J.Botelho, K.Franklin, and I.M.Chiu (1999).
Site-directed mutagenesis and molecular modeling identify a crucial amino acid in specifying the heparin affinity of FGF-1.
  Biochemistry, 38, 9264-9272.  
10026256 W.J.LaRochelle, K.Sakaguchi, N.Atabey, H.G.Cheon, Y.Takagi, T.Kinaia, R.M.Day, T.Miki, W.H.Burgess, and D.P.Bottaro (1999).
Heparan sulfate proteoglycan modulates keratinocyte growth factor signaling through interaction with both ligand and receptor.
  Biochemistry, 38, 1765-1771.  
9634702 F.Vallée, A.Kadziola, Y.Bourne, M.Juy, K.W.Rodenburg, B.Svensson, and R.Haser (1998).
Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution.
  Structure, 6, 649-659.
PDB code: 1ava
9675169 M.Zamai, V.R.Caiolfa, D.Pines, E.Pines, and A.H.Parola (1998).
Nature of interaction between basic fibroblast growth factor and the antiangiogenic drug 7,7-(Carbonyl-bis[imino-N-methyl-4, 2-pyrrolecarbonylimino[N-methyl-4,2-pyrrole]-carbonylimino] )bis-(1, 3-naphthalene disulfonate).
  Biophys J, 75, 672-682.  
9636026 P.J.Kim, K.Sakaguchi, H.Sakamoto, C.Saxinger, R.Day, P.McPhie, J.S.Rubin, and D.P.Bottaro (1998).
Colocalization of heparin and receptor binding sites on keratinocyte growth factor.
  Biochemistry, 37, 8853-8862.  
9818261 S.Faham, R.J.Linhardt, and D.C.Rees (1998).
Diversity does make a difference: fibroblast growth factor-heparin interactions.
  Curr Opin Struct Biol, 8, 578-586.  
  10082365 T.D.Osslund, R.Syed, E.Singer, E.W.Hsu, R.Nybo, B.L.Chen, T.Harvey, T.Arakawa, L.O.Narhi, A.Chirino, and C.F.Morris (1998).
Correlation between the 1.6 A crystal structure and mutational analysis of keratinocyte growth factor.
  Protein Sci, 7, 1681-1690.  
9843417 Y.Luo, W.Lu, K.A.Mohamedali, J.H.Jang, R.B.Jones, J.L.Gabriel, M.Kan, and W.L.McKeehan (1998).
The glycine box: a determinant of specificity for fibroblast growth factor.
  Biochemistry, 37, 16506-16515.  
9125499 F.J.Moy, M.Safran, A.P.Seddon, D.Kitchen, P.Böhlen, D.Aviezer, A.Yayon, and R.Powers (1997).
Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor.
  Biochemistry, 36, 4782-4791.  
9208921 J.M.Sanz, and G.Giménez-Gallego (1997).
A partly folded state of acidic fibroblast growth factor at low pH.
  Eur J Biochem, 246, 328-335.  
9180161 M.Azuma, T.Yuki, K.Motegi, and M.Sato (1997).
Enhancement of bFGF export associated with malignant progression of human salivary gland cell clones.
  Int J Cancer, 71, 891-896.  
9122212 R.D.Burdine, E.B.Chen, S.F.Kwok, and M.J.Stern (1997).
egl-17 encodes an invertebrate fibroblast growth factor family member required specifically for sex myoblast migration in Caenorhabditis elegans.
  Proc Natl Acad Sci U S A, 94, 2433-2437.  
9334739 T.R.Transue, A.K.Smith, H.Mo, I.J.Goldstein, and M.A.Saper (1997).
Structure of benzyl T-antigen disaccharide bound to Amaranthus caudatus agglutinin.
  Nat Struct Biol, 4, 779-783.
PDB codes: 1jlx 1jly
8917442 A.Romero, A.Pineda-Lucena, and G.Giménez-Gallego (1996).
X-ray structure of native full-length human fibroblast-growth factor at 0.25-nm resolution.
  Eur J Biochem, 241, 453-461.  
8968609 B.S.Chang, R.M.Beauvais, T.Arakawa, L.O.Narhi, A.Dong, D.I.Aparisio, and J.F.Carpenter (1996).
Formation of an active dimer during storage of interleukin-1 receptor antagonist in aqueous solution.
  Biophys J, 71, 3399-3406.  
8885834 F.J.Moy, A.P.Seddon, P.Böhlen, and R.Powers (1996).
High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy.
  Biochemistry, 35, 13552-13561.
PDB codes: 1bla 1bld
  9017109 G.Grassi, and J.C.Marini (1996).
Ribozymes: structure, function, and potential therapy for dominant genetic disorders.
  Ann Med, 28, 499-510.  
8570646 G.Venkataraman, V.Sasisekharan, A.B.Herr, D.M.Ornitz, G.Waksman, C.L.Cooney, R.Langer, and R.Sasisekharan (1996).
Preferential self-association of basic fibroblast growth factor is stabilized by heparin during receptor dimerization and activation.
  Proc Natl Acad Sci U S A, 93, 845-850.  
  8702264 H.Su, F.Blain, R.A.Musil, J.J.Zimmermann, K.Gu, and D.C.Bennett (1996).
Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum.
  Appl Environ Microbiol, 62, 2723-2734.  
8652550 M.Blaber, J.DiSalvo, and K.A.Thomas (1996).
X-ray crystal structure of human acidic fibroblast growth factor.
  Biochemistry, 35, 2086-2094.
PDB codes: 1afg 2afg
9023055 M.Goldfarb (1996).
Functions of fibroblast growth factors in vertebrate development.
  Cytokine Growth Factor Rev, 7, 311-325.  
8739851 M.Rusnati, and M.Presta (1996).
Interaction of angiogenic basic fibroblast growth factor with endothelial cell heparan sulfate proteoglycans. Biological implications in neovascularization.
  Int J Clin Lab Res, 26, 15-23.  
8790420 P.M.Smallwood, I.Munoz-Sanjuan, P.Tong, J.P.Macke, S.H.Hendry, D.J.Gilbert, N.G.Copeland, N.A.Jenkins, and J.Nathans (1996).
Fibroblast growth factor (FGF) homologous factors: new members of the FGF family implicated in nervous system development.
  Proc Natl Acad Sci U S A, 93, 9850-9857.  
8610159 Y.Kato, T.Muto, T.Tomura, H.Tsumura, H.Watarai, T.Mikayama, K.Ishizaka, and R.Kuroki (1996).
The crystal structure of human glycosylation-inhibiting factor is a trimeric barrel with three 6-stranded beta-sheets.
  Proc Natl Acad Sci U S A, 93, 3007-3010.
PDB code: 1gif
  7815139 G.J.Redekop, and C.C.Naus (1995).
Transfection with bFGF sense and antisense cDNA resulting in modification of malignant glioma growth.
  J Neurosurg, 82, 83-90.  
7867645 H.A.Schreuder, J.M.Rondeau, C.Tardif, A.Soffientini, E.Sarubbi, A.Akeson, T.L.Bowlin, S.Yanofsky, and R.W.Barrett (1995).
Refined crystal structure of the interleukin-1 receptor antagonist. Presence of a disulfide link and a cis-proline.
  Eur J Biochem, 227, 838-847.
PDB code: 1ilr
8521464 J.Schlessinger, I.Lax, and M.Lemmon (1995).
Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors?
  Cell, 83, 357-360.  
7596347 R.R.Padua, R.Sethi, N.S.Dhalla, and E.Kardami (1995).
Basic fibroblast growth factor is cardioprotective in ischemia-reperfusion injury.
  Mol Cell Biochem, 143, 129-135.  
7860646 R.Z.Florkiewicz, R.A.Majack, R.D.Buechler, and E.Florkiewicz (1995).
Quantitative export of FGF-2 occurs through an alternative, energy-dependent, non-ER/Golgi pathway.
  J Cell Physiol, 162, 388-399.  
  8575190 S.Ernst, R.Langer, C.L.Cooney, and R.Sasisekharan (1995).
Enzymatic degradation of glycosaminoglycans.
  Crit Rev Biochem Mol Biol, 30, 387-444.  
7579653 S.R.Price, and K.Nagai (1995).
Protein engineering as a tool for crystallography.
  Curr Opin Biotechnol, 6, 425-430.  
8590594 T.Arakawa, P.Holst, L.O.Narhi, J.S.Philo, J.Wen, S.J.Prestrelski, X.Zhu, D.C.Rees, and G.M.Fox (1995).
The importance of Arg40 and 45 in the mitogenic activity and structural stability of basic fibroblast growth factor: effects of acidic amino acid substitutions.
  J Protein Chem, 14, 263-274.  
7742376 T.Imamura, S.A.Friedman, S.Gamble, Y.Tokita, S.R.Opalenik, J.A.Thompson, and T.Maciag (1995).
Identification of the domain within fibroblast growth factor-1 responsible for heparin-dependence.
  Biochim Biophys Acta, 1266, 124-130.  
8575426 Y.J.Buechler, B.A.Sosnowski, K.D.Victor, Z.Parandoosh, S.J.Bussell, C.Shen, M.Ryder, and L.L.Houston (1995).
Synthesis and characterization of a homogeneous chemical conjugate between basic fibroblast growth factor and saporin.
  Eur J Biochem, 234, 706-713.  
7517355 A.Pineda-Lucena, I.Núñez De Castro, R.M.Lozano, I.Muñoz-Willery, M.Zazo, and G.Giménez-Gallego (1994).
Effect of low pH and heparin on the structure of acidic fibroblast growth factor.
  Eur J Biochem, 222, 425-431.  
  7508860 B.Yang, B.L.Yang, R.C.Savani, and E.A.Turley (1994).
Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein.
  EMBO J, 13, 286-296.  
8024698 D.F.Kusewitt, C.L.Sabourin, C.L.Budge, T.E.Sherburn, and R.D.Ley (1994).
Characterization of cDNA encoding basic fibroblast growth factor of the marsupial Monodelphis domestica.
  DNA Cell Biol, 13, 549-554.  
8190116 I.Cosic, A.E.Drummond, J.R.Underwood, and M.T.Hearn (1994).
In vitro inhibition of the actions of basic FGF by a novel 16 amino acid peptide.
  Mol Cell Biochem, 130, 1-9.  
7886237 K.D.Beck (1994).
Functions of brain-derived neurotrophic factor, insulin-like growth factor-I and basic fibroblast growth factor in the development and maintenance of dopaminergic neurons.
  Prog Neurobiol, 44, 497-516.  
8108444 S.Garfinkel, S.Brown, J.H.Wessendorf, and T.Maciag (1994).
Post-transcriptional regulation of interleukin 1 alpha in various strains of young and senescent human umbilical vein endothelial cells.
  Proc Natl Acad Sci U S A, 91, 1559-1563.  
  7691311 A.E.Eriksson, L.S.Cousens, and B.W.Matthews (1993).
Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.
  Protein Sci, 2, 1274-1284.
PDB codes: 1fga 4fgf
7504274 A.Yayon, D.Aviezer, M.Safran, J.L.Gross, Y.Heldman, S.Cabilly, D.Givol, and E.Katchalski-Katzir (1993).
Isolation of peptides that inhibit binding of basic fibroblast growth factor to its receptor from a random phage-epitope library.
  Proc Natl Acad Sci U S A, 90, 10643-10647.  
8508806 D.Coltrini, M.Rusnati, G.Zoppetti, P.Oreste, A.Isacchi, P.Caccia, L.Bergonzoni, and M.Presta (1993).
Biochemical bases of the interaction of human basic fibroblast growth factor with glycosaminoglycans. New insights from trypsin digestion studies.
  Eur J Biochem, 214, 51-58.  
8387532 P.Bellosta, D.Talarico, D.Rogers, and C.Basilico (1993).
Cleavage of K-FGF produces a truncated molecule with increased biological activity and receptor binding affinity.
  J Cell Biol, 121, 705-713.  
7520817 X.Zhu, B.T.Hsu, and D.C.Rees (1993).
Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidic fibroblast growth factor.
  Structure, 1, 27-34.
PDB code: 1afc
  1281450 A.Wiedlocha, I.H.Madshus, H.Mach, C.R.Middaugh, and S.Olsnes (1992).
Tight folding of acidic fibroblast growth factor prevents its translocation to the cytosol with diphtheria toxin as vector.
  EMBO J, 11, 4835-4842.  
1639857 F.T.Stevenson, F.Torrano, R.M.Locksley, and D.H.Lovett (1992).
Interleukin 1: the patterns of translation and intracellular distribution support alternative secretory mechanisms.
  J Cell Physiol, 152, 223-231.  
1281822 J.P.Chanoine, G.S.Stein, L.E.Braverman, V.Shalhoub, J.B.Lian, C.A.Huber, and W.J.DeVito (1992).
Acidic fibroblast growth factor modulates gene expression in the rat thyroid in vivo.
  J Cell Biochem, 50, 392-399.  
1541279 P.Caccia, G.Nitti, O.Cletini, P.Pucci, M.Ruoppolo, F.Bertolero, B.Valsasina, F.Roletto, C.Cristiani, and G.Cauet (1992).
Stabilization of recombinant human basic fibroblast growth factor by chemical modifications of cysteine residues.
  Eur J Biochem, 204, 649-655.  
1369391 P.R.Young (1992).
Protein hormones and their receptors.
  Curr Opin Biotechnol, 3, 408-421.  
1368488 U.Rinas, L.B.Tsai, D.Lyons, G.M.Fox, G.Stearns, J.Fieschko, D.Fenton, and J.E.Bailey (1992).
Cysteine to serine substitutions in basic fibroblast growth factor: effect on inclusion body formation and proteolytic susceptibility during in vitro refolding.
  Biotechnology (N Y), 10, 435-440.  
1664701 A.Seddon, M.Decker, T.Müller, D.Armellino, I.Kovesdi, Y.Gluzman, and P.Böhlen (1991).
Structure/activity relationships in basic FGF.
  Ann N Y Acad Sci, 638, 98.  
  1833184 C.J.McMahan, J.L.Slack, B.Mosley, D.Cosman, S.D.Lupton, L.L.Brunton, C.E.Grubin, J.M.Wignall, N.A.Jenkins, and C.I.Brannan (1991).
A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types.
  EMBO J, 10, 2821-2832.  
2001586 E.Ruoslahti, and Y.Yamaguchi (1991).
Proteoglycans as modulators of growth factor activities.
  Cell, 64, 867-869.  
1849658 J.D.Zhang, L.S.Cousens, P.J.Barr, and S.R.Sprang (1991).
Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta.
  Proc Natl Acad Sci U S A, 88, 3446-3450.
PDB code: 2fgf
1717155 J.Kandel, E.Bossy-Wetzel, F.Radvanyi, M.Klagsbrun, J.Folkman, and D.Hanahan (1991).
Neovascularization is associated with a switch to the export of bFGF in the multistep development of fibrosarcoma.
  Cell, 66, 1095-1104.  
1924307 K.A.Hogquist, M.A.Nett, E.R.Unanue, and D.D.Chaplin (1991).
Interleukin 1 is processed and released during apoptosis.
  Proc Natl Acad Sci U S A, 88, 8485-8489.  
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 code is shown on the right.