132:-2, -5, -7, -10, -11, -14 and -15. Tandem galectins contain at least two distinct carbohydrate recognition domains (CRD) within one polypeptide, thus are considered intrinsically divalent. The CRDs are linked with a small peptide domain. Tandem galectins include galectin-4, -6, -8, -9 and -12. The final galectin is galectin-3 which is the only galectin found in the chimera category in vertebrates. Galectin-3 has one CRD and a long non-lectin domain. Galectin-3 can exist in monomeric form or can associate via the non-lectin domain into multivalent complexes up to a pentameric form. This allows galectin-3 to bridge effectively between different ligands and form adhesive networks. The formation of multimers is concentration dependent. When Galectin-3 is at a low concentration it is monomeric and likely to inhibit adhesion. It binds to adhesion proteins such as
656:, which on cancer cells changes expression from long core 2 type O-glycosylation to shorter core 1 type O-glycosylation. Core 2 glycans terminate in galactose or sialic acid, whereas core 1 is branched and has potential for large carbohydrate extensions. High levels of MUC-1 are associated with poor prognosis and increased potential of metastasis. This cancer-associated MUC-1 is a natural ligand for galectin-3. In normal cells, MUC-1 has distinct polarisation and acts as a protective barrier around the cell, reducing cell-cell interactions. In breast cancer cells, it is hypothesised that galectin-3 has high affinity for cancer-associated MUC-1, causing depolarisation and breaking the cell's protective shield. This exposes small adhesion molecules on the surface of the cell, which interact with adhesion proteins on
123:
20:
664:, promoting intravastion into the blood stream. Experiments shows that overexpression of MUC-1 alone is not enough to increase metastatic potential, and in fact it inhibits tumour cell entry into the blood stream. It requires the presence of upregulated galectin-3 in addition to MUC-1 to increase invasive and metastatic properties of the cancer. This is supported by other studies showing that inhibition of galectin-3 in human breast cancer cells lose their malignancy
365:. GnTV is the enzyme required to synthesise polylactosamine chains, which are the ligand for galectin-3 on T cell receptors. This knock-out means galectin-3 cannot prevent auto-activation of TCR so T cells are hypersensitive. Also within the immune system, galectins have been proven to act as chemoattractants to immune cells and activate secretion of inflammatory
377:
Galectins can both promote and inhibit integrin-mediated adhesion. To enhance integrin-mediated adhesion, they cross link between two glycans on different cells. This brings the cells closer together so integrin binding occurs. They can also hinder adhesion by binding to two glycans on the same cell,
680:
Galectin-8 has been shown to play a specific role in assessing endosomal integrity. After pathogens, such as bacteria or viruses, are engulfed by cells, they typically try to exit the endosome to gain access to nutrients in the cytosol. Galectin-8 specifically binds to glycosylation found within the
61:
for stability and carbohydrate binding. There have been about 15 galectins discovered in mammals, encoded by the LGALS genes, which are numbered in a consecutive manner. Only galectin-1, -2, -3, -4, -7, -7B, -8, -9, -9B, 9C, -10, -12, -13, -14, and -16 have been identified in humans. Galectin-5 and
131:
There are three different forms of galectin structure: dimeric, tandem or chimera. Dimeric galectins, also called prototypical galectins, are homodimers, consisting of two identical galectin subunits that have associated with one another. The galectins that fall under this category are galectin-1,
671:
Galectin-8, which increases integrin-mediated adhesion, has been shown to be downregulated in some cancers. This benefits the cancer since integrin interactions with the extracellular matrix prevent metastasis. Lung cancer studies, however, have demonstrated increased adhesion to galectin-8 with
758:
of T cells to prevent auto reactivity. When HIV is present, the galectin bridges between the CD4 co-receptor and gp120 ligands, thus facilitating HIV infection of the T cell. Galectin-1 is not essential for HIV infection but assists it by accelerating the binding kinetics between gp120 and CD4.
189:
interactions can occur between sugar and binding pocket. Carbohydrate binding is calcium independent, unlike C-type lectins. The strength of ligand binding is determined by a number of factors: The multivalency of both of ligand and the galectin, the length of the carbohydrate and the mode of
126:
The basic cartoon structures of dimeric, tandem and chimeric galectins. Dimeric galectins consist of two of the same subunit that have associated with one another. Tandem galectins have two distinct CRDs linked via a linker peptide domain. Chimera galectins, which consist of only galectin-3 in
136:
and blocks further binding to other cells or the extracellular matrix. When concentrations of galectin-3 are high it forms large complexes that assist in adhesion by bridging between cells or cells and the extracellular matrix. Many isoforms of galectins have been found due to different
767:, a cytosolic restriction factor against HIV acting during HIV capsid uncoating, although the precise role of this association remains to be determined. Several galectins bind other TRIMs some of which are known to contribute to antiviral restriction.
648:. It has also been identified bound to glycans on the surface of breast cancer cells. In cancer patients whose cancer has metastasised, galectin-3 is higher still, suggesting that this galectin has a crucial role in metastasis. Galectin-3 also binds to
685:
which activates antibacterial autophagy. Galectin-3, galectin 8 and galectin-9 have been shown to play additional roles in autophagy both through control of mTOR (galectin-8) and AMPK (galectin-9), and as a factor (galectin-3) in the assembly of the
157:. The two sheets are slightly bent with 6 strands forming the concave side and 5 strands forming the convex side. The concave side forms a groove in which the carbohydrate ligand can bind, and which is long enough to hold about a linear
246:
models. This is because there is substantial overlap for the essential functions. The list of functions for galectins is extensive and it is unlikely they have all been discovered. A handful of the main functions are described below.
759:
Knowledge of the mechanism between galectin and HIV may provide important therapeutic opportunities. A galectin-1 inhibitor can be used in conjunction with antiretroviral drugs to decrease the infectivity of the HIV and increase the
353:(TCR) activation. Crosslinking of T cell receptors and other glycoproteins by galectin-3 on the membrane of T cells prevents clustering of TCRs and ultimately suppresses activation. This prevents auto-activation. Experiments in
255:
Galectins are distinct in that they can regulate cell death both intracellularly and extracellularly. Extracellularly, they cross link glycans on the outside of cells and transduce signals across the membrane to directly cause
226:. Due to the nature of the binding pocket, galectins can bind terminal sugars or internal sugars within a glycan. This allows bridging between two ligands on the same cell or between two ligands on different cells.
181:-acetyllactosamine for significantly strong binding. Generally, the longer the sugar the stronger the interactions. For example, galectin-9 binds to polylactosamine chains with stronger affinity than to an
194:
depending on the tissue in which they are expressed and the function that they possess. However, in each case, galactose is essential for binding. Crystallisation experiments of galectins in complex with
467:, which in its active state resides on the cytosolic (cytofacial) side of lysosomal membranes. However, under lysosome damaging conditions leading to exposure of the exofacially, i.e., lumenaly, oriented
145:
encoding for both tandem and dimeric forms. The type of galectin-8 that is expressed is dependent on the tissue. Galectin-9 has three different isoforms which differ in the length of the linker region.
242:. Their expression and secretion is well regulated, suggesting they may be expressed at different times during development. There are no serious defects when individual galectin genes are deleted in
449:(AMPK) in response to lysosomal membrane damage. Lysosomal perforation and other endomembrane damage can be inflicted by various agents such as some chemicals yielding osmotically active products,
1810:
Jia, Jingyue; Claude-Taupin, Aurore; Gu, Yuexi; Choi, Seong Won; Peters, Ryan; Bissa, Bhawana; Mudd, Michal H.; Allers, Lee; Pallikkuth, Sandeep; Lidke, Keith A.; Salemi, Michelle (December 2019).
378:
which blocks the integrin binding site. Galectin-8 is specific for the glycans bound to integrin and has a direct role in adhesion as well as activating integrin-specific signaling cascades.
1286:
Lobsanov YD, Gitt MA, Leffler H, Barondes SH, Rini JM (December 1993). "X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution".
332:
Galectin-3 has been shown to be the only galectin with anti-apoptotic activity, proven by knock-out in mice increasing rates of apoptosis. Intracellularly, galectin-3 can associate with
580:
Galectins are abundant, distributed widely around the body and have some distinct functions. It is because of these that they are often implicated in a wide range of diseases such as
1864:
Radosavljevic G, Volarevic V, Jovanovic I, Milovanovic M, Pejnovic N, Arsenijevic N, Hsu DK, Lukic ML (April 2012). "The roles of
Galectin-3 in autoimmunity and tumor progression".
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proteins, an antiapoptotic family of proteins, and thus may enhance Bcl-2 binding to the target cell. On the other hand, galectin-3 can also be pro-apoptotic and mediate T cell and
2170:
Mandell MA, Jain A, Arko-Mensah J, Chauhan S, Kimura T, Dinkins C, Silvestri G, MĂĽnch J, Kirchhoff F, Simonsen A, Wei Y, Levine B, Johansen T, Deretic V (August 2014).
511:(RagA/B). This complex loses affinity for mTOR causing mTOR's inactivation and translocation from the lysosome to the cytosol. The damage-responsive complex containing
234:
Galectins are a large family with relatively broad specificity. Thus, they have a broad variety of functions including mediation of cell–cell interactions, cell–matrix
644:, which may give it additional tumorigenic properties. The concentration of galectin-3 is elevated in the circulation of patients with some types of cancer including
402:
with lactose resulted in loss of splicing activity. It appears that the splicing capability of galectins is independent of their sugar-binding specificities.
62:-6 are found in rodents, whereas galectin-11 and -15 are uniquely found in sheep and goats. Members of the galectin family have also been discovered in other
974:
Binds to integrins of the extracellular matrix. In the cytoplasm, alternatively binds to mTOR or forms the GALTOR complex with SLC38A9, LAMTOR1, and RagA/B
1013:
Enhances maturation of dendritic cells to secrete inflammatory cytokines. In the cytoplasm, associates upon lysosomal damage with AMPK and activates it
624:
and increased invasive properties of tumour cells. There is some significant evidence that galectin-3 is involved in cancer since it interacts with
122:
612:
The best understood galectin in terms of cancer is galectin-3. Evidence suggests that galectin-3 plays a considerable part in processes linked to
1705:
Jia J, Abudu YP, Claude-Taupin A, Gu Y, Kumar S, Choi SW, Peters R, Mudd MH, Allers L, Salemi M, Phinney B, Johansen T, Deretic V (April 2018).
459:; such injury can be modeled using membrane-permeant dipeptide precursors that polymerize in lysosomes,. Under resting, homeostatic conditions
446:
2376:
1343:
735:
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Graessler J, Spitzenberger F, Graessler A, Parpart B, Kuhlisch E, Kopprasch S, Schroeder HE (2000). "Genomic
Structure of Galectin-9 Gene".
750:-acetyllactosamine chains are ligands for galectin-1. Galectin-1 is expressed in the thymus. In particular it is secreted in abundance by
1553:
Zick Y, Eisenstein M, Goren RA, Hadari YR, Levy Y, Ronen D (2004). "Role of galectin-8 as a modulator of cell adhesion and cell growth".
1761:
Chauhan S, Kumar S, Jain A, Ponpuak M, Mudd MH, Kimura T, Choi SW, Peters R, Mandell M, Bruun JA, Johansen T, Deretic V (October 2016).
2508:
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Benatar, Alejandro F.; GarcĂa, Gabriela A.; Bua, Jacqeline; Cerliani, Juan P.; Postan, Miriam; Tasso, Laura M.; et al. (2015).
2094:
1262:
453:, possibly amyloid aggregates and cytoplasmic organic or inorganic crystals, as well as intracellular microbial pathogens such as
535:
that assembles autophagy initiation machinery on damaged lysosomes, whereas galectin-8 also interacts with the autophagy receptor
1912:"A combinatorial extracellular matrix platform identifies cell-extracellular matrix interactions that correlate with metastasis"
190:
presentation of ligand to carbohydrate recognition domain. Different galectins have distinct binding specificities for binding
110:
or in circulation. Although many galectins must be secreted, they do not have a typical signal peptide required for classical
2628:
950:
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studies to the carbohydrate recognition domain removes glycan binding but does not prevent association with the spliceosome.
292:. This is also mediated by galectin-1 and galectin-9. Galectin-1 binds many proteins on the T cell surface, but specifically
288:
in the thymus and mediate T cell apoptosis. T cell death is also necessary to kill activated and infected T cells after an
1763:"TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis"
2694:
706:
Galectin-1 has been shown to enhance HIV infection due to its galactose binding specificity. HIV preferentially infects
1050:
264:. Intracellularly, they can directly regulate proteins that control cell fate. Many galectins have roles in apoptosis:
2544:
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increased metastatic potential, which may be mediated by elevated surface expression and activation of integrin α3β1.
937:
455:
19:
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and activates downstream signalling that promotes proliferation. It can also regulate some of the proteins of the
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403:
2784:
2466:
895:
2400:
Jayaraman P, Sada-Ovalle I, Beladi S, Anderson AC, Dardalhon V, Hotta C, Kuchroo VK, Behar SM (October 2010).
1910:
Reticker-Flynn NE, Malta DF, Winslow MM, Lamar JM, Xu MJ, Underhill GH, Hynes RO, Jacks TE, Bhatia SN (2012).
1645:
Voss PG, Gray RM, Dickey SW, Wang W, Park JW, Kasai K, Hirabayashi J, Patterson RJ, Wang JL (October 2008).
399:
868:
711:
50:
46:
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Sturm A, Lensch M, André S, Kaltner H, Wiedenmann B, Rosewicz S, Dignass AU, Gabius HJ (September 2004).
2559:
2501:
1438:
Yang RY, Rabinovich GA, Liu FT (June 2008). "Galectins: structure, function and therapeutic potential".
1334:
Drickamer, K.; Taylor, M. (2011). "Chapter 9: Carbohydrate recognition in cell adhesion and signaling".
877:
597:
2035:
2026:
Sato S, Ouellet M, St-Pierre C, Tremblay MJ (April 2012). "Glycans, galectins, and HIV-1 infection".
1923:
1509:
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In the cytoplasm, helps form the ULK1-Beclin-1-ATG16L1-TRIM16 complex following endomembrane damage
668:. This may provide a clue towards developing therapeutics for cancer, such as galectin-3 inhibitors.
593:
107:
2746:
910:
Upregulation occurs in some cancers, including breast cancer, gives increased metastatic potential
793:
604:. The most studied and characterised mechanisms are for cancer and HIV, which are described below.
362:
311:
208:
186:
39:
1976:"Circulating galectin-3 promotes metastasis by modifying MUC1 localization on cancer cell surface"
2320:"Human galectin-2: novel inducer of T cell apoptosis with distinct profile of caspase activation"
2059:
1889:
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Secreted by immune cells such as by T helper cells in the thymus or by stromal cells surrounding
601:
589:
450:
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vertebrates, can exist as a monomer or in a multivalent form. Here it is expressed as a pentamer.
548:
The functional roles of galectins in cellular response to membrane damage are expanding, e.g.
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2005:
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1498:"Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion"
1465:
1395:
1339:
1303:
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1258:
1216:
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is known as GALTOR. Galectin-3 and galectin-8 also interact with autophagy receptor-regulator
387:
2172:"TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition"
495:
instead now binds to the mTOR-regulatory complex located on the lysosomal membrane including
280:. This process prevents the circulation of T cells that are self-reactive and recognise self
90:. Unlike the majority of lectins they are not membrane bound, but soluble proteins with both
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35:
1181:, Rabinovich GA (January 2010). "Galectins: regulators of acute and chronic inflammation".
743:
354:
350:
289:
243:
158:
58:
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Liu FT, Patterson RJ, Wang JL (September 2002). "Intracellular functions of galectins".
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St-Pierre C, Ouellet M, Giguère D, Ohtake R, Roy R, Sato S, Tremblay MJ (January 2012).
2039:
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functions. They have distinct but overlapping distributions but found primarily in the
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St-Pierre C, Ouellet M, Tremblay MJ, Sato S (2010). "Galectin-1 and HIV-1 Infection".
1152:
1135:
2778:
2758:
2536:
2120:"Galectin-1-specific inhibitors as a new class of compounds to treat HIV-1 infection"
2047:
1202:
784:, is reduced by galectin–1, which may also protect against apoptosis of the infected
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629:
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315:
235:
200:
142:
95:
91:
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730:. The gp120 glycoprotein contains two types of N-glycan, high mannose oligomers and
2684:
2613:
1582:
1228:
1022:
980:
913:
719:
472:
395:
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Galectin-1 and galectin-3 have been found, surprisingly, to associate with nuclear
319:
222:
because this sugar will not fit inside the carbohydrate recognition domain without
138:
103:
1991:
2482:
2363:. Advances in Experimental Medicine and Biology. Vol. 486. pp. 179–83.
2244:
2187:
1827:
1778:
1722:
2336:
2319:
1974:
Zhao Q, Guo X, Nash GB, Stone PC, Hilkens J, Rhodes JM, Yu LG (September 2009).
1647:"Dissociation of the carbohydrate-binding and splicing activities of galectin-1"
1178:
1080:
1037:
1031:
931:
755:
391:
215:
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114:. The mechanism and reason for this non-classical secretion pathway is unknown.
734:-acetyllactosamine chains on a trimannose core. The high mannose oligomers are
2719:
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989:
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150:
71:
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Thurston TL, Wandel MP, von
Muhlinen N, Foeglein A, Randow F (January 2012).
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625:
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423:
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261:
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111:
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27:-acetyllactosamine dimer, clearly showing the two carbohydrate binding sites
2435:
2386:
2345:
2301:
2263:
2205:
2153:
2104:
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2009:
1953:
1885:
1845:
1812:"Galectin-3 Coordinates a Cellular System for Lysosomal Repair and Removal"
1796:
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1631:
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1539:
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1220:
45:(Galβ1-3GlcNAc or Galβ1-4GlcNAc), which can be bound to proteins by either
1307:
1299:
1161:
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and its derivatives. However, physiologically, they are likely to require
2699:
2679:
2663:
2658:
2593:
2588:
2583:
2578:
2478:
2457:
2417:
2135:
1085:
792:-infected murine cardiomyocytes reduce the concentration of surface poly-
760:
682:
665:
637:
565:
561:
557:
536:
361:-acetylglucosamine transferase V (GnTV) have increased susceptibility to
204:
1521:
2736:
2653:
2648:
2643:
2638:
2633:
2517:
1935:
1460:
1211:
1136:"Galectins. Structure and function of a large family of animal lectins"
835:
804:-linked glycans, possibly creating a "Gal-1 resistant glycophenotype."
739:
695:
520:
516:
500:
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281:
273:
219:
174:
149:
The galectin carbohydrate recognition domain (CRD) is constructed from
99:
83:
63:
1046:
Essential role in immune system by suppression of T cell proliferation
754:
cells. In its normal function, galectin-1 binds to glycans on the CD4
2763:
2605:
2521:
1054:
581:
532:
484:
468:
442:
277:
87:
54:
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May have a role in apoptosis and cellular repair mediated by p53.
560:
can be repaired. This occurs before autophagy is induced to repair
2729:
2724:
2549:
873:
Binds selectively to β-galactosides of T cells to induce apoptosis
723:
715:
691:
653:
649:
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553:
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508:
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411:
333:
121:
67:
18:
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1374:"Ah, sweet mystery of death! Galectins and control of cell fate"
727:
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488:
464:
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419:
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301:
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75:
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2402:"Tim3 binding to galectin-9 stimulates antimicrobial immunity"
780:
infection of cardiac cells, the cause of heart involvement in
707:
585:
308:
293:
268:
One essential way galectins regulate apoptosis is to control
1707:"Galectins Control mTOR in Response to Endomembrane Damage"
1134:
Barondes SH, Cooper DN, Gitt MA, Leffler H (August 1994).
788:. Benatar et al. (2015) also demonstrated, however, that
349:
Galectin-3 has an essential role in negatively regulating
2081:. Methods in Enzymology. Vol. 480. pp. 267–94.
718:
that infects CD4 cells via binding of its viral envelope
218:
in the protein. They cannot bind to other sugars such as
698:
initiator complex on TRIM16 during endomembrane damage.
710:
and other cells of the immune system, immobilising the
394:. Studies revealed that galectin-1 and -3 are required
2473:
This article incorporates text from the public domain
2282:
Biochimica et
Biophysica Acta (BBA) - General Subjects
839:
Also found in abundance in muscle, neurons and kidney
141:
variants. For example, Galectin-8 has seven different
2224:"Galectin-1 Prevents Infection and Damage Induced by
2712:
2672:
2604:
2535:
2528:
2453:
Galectin: Definition and
History by Jun Hirabayashi
314:and may have a key role in regulating apoptosis of
199:-acetyllactosamine show that binding arises due to
34:are a class of proteins that bind specifically to
1905:
1903:
1859:
1857:
1855:
1596:Haudek KC, Patterson RJ, Wang JL (October 2010).
961:Implications in cancer Implications in psoriasis
284:. Both galectin-1 and galectin-9 are secreted by
185:-acetyllactosamine monomer. This is because more
1433:
1431:
1429:
1329:
1327:
1325:
1129:
1127:
1125:
1008:Functions as a urate transporter in the kidney
738:(PAMPs) and are recognised by the C-type lectin
169:Galectins essentially bind to glycans featuring
2313:
2311:
1427:
1425:
1423:
1421:
1419:
1417:
1415:
1413:
1411:
1409:
1244:
1242:
1240:
1238:
892:Can be pro- or anti-apoptotic (cell dependent)
843:Negatively regulate B cell receptor activation
260:or activate downstream signaling that triggers
2458:Handbook of Animal Lectins by David Kilpatrick
1969:
1967:
1965:
1963:
1598:"SR proteins and galectins: what's in a name?"
1010:Induces apoptosis of thymocytes and Th1 cells
934:suggesting a role in protein delivery to cells
23:Structure of human galectin-9 in complex with
16:Protein family binding to β-galactoside sugars
2502:
2275:
2273:
848:Suppression of Th1 and Th17 immune responses
8:
900:Contributes to nuclear splicing of pre-mRNA
851:Contributes to nuclear splicing of pre-mRNA
487:exposed due to membrane damage and releases
325:Galectin-12 expression induces apoptosis of
203:interactions from the carbon-4 and carbon-6
1367:
1365:
1363:
1361:
1359:
1357:
1355:
398:factors, since removal of the galectins by
2532:
2509:
2495:
2487:
2217:
2215:
2028:Annals of the New York Academy of Sciences
1257:(2nd ed.). Cold Spring Harbour (NY).
1249:Varki, A; Cummings, R.D.; Liu, F. (2009).
1183:Annals of the New York Academy of Sciences
1173:
1171:
2465:at the U.S. National Library of Medicine
2425:
2361:Purine and Pyrimidine Metabolism in Man X
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2021:
2019:
1999:
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1621:
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1338:(3rd ed.). Oxford University Press.
1210:
1151:
345:Suppression of T-cell receptor activation
318:after DNA damage, such as that caused by
811:
681:endosome, and recruits adapter molecule
1651:Archives of Biochemistry and Biophysics
1107:
1372:Hernandez JD, Baum LG (October 2002).
1071:Involved in adipocyte differentiation
2165:
2163:
2124:Antimicrobial Agents and Chemotherapy
1756:
1754:
1752:
1750:
1700:
1698:
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903:Crosslinking and adhesive properties
736:pathogen-associated molecular pattern
7:
2406:The Journal of Experimental Medicine
1491:
1489:
1487:
1440:Expert Reviews in Molecular Medicine
796:, a galectin-1 ligand, within their
207:groups of galactose and carbon-3 of
1288:The Journal of Biological Chemistry
1140:The Journal of Biological Chemistry
1118:. HUGO Gene Nomenclarute Committee.
1069:Stimulates apoptosis of adipocytes
894:Regulation of some genes including
1567:10.1023/B:GLYC.0000014081.55445.af
857:Found upregulated in tumour cells
307:Galectin-7 is expressed under the
14:
955:Differentiation of keratinocytes
2232:PLOS Neglected Tropical Diseases
2048:10.1111/j.1749-6632.2012.06475.x
1203:10.1111/j.1749-6632.2009.05131.x
616:, including transformation to a
1116:"Gene group: Galectins (LGALS)"
977:Downregulation in some cancers
676:Intracellular pathogen invasion
270:positive and negative selection
214:(GlcNAc) to the side chains of
2629:Myelin-associated glycoprotein
951:Stratified squamous epithelium
845:Activate apoptosis in T cells
763:of the drug. Galectin-3 binds
53:. They are also termed S-type
1:
2294:10.1016/S0304-4165(02)00313-6
2087:10.1016/S0076-6879(10)80013-8
1992:10.1158/0008-5472.CAN-09-1096
1153:10.1016/S0021-9258(17)31891-4
652:, a very large transmembrane
556:to damaged lysosomes so that
2695:N-Acetylglucosamine receptor
2245:10.1371/journal.pntd.0004148
2188:10.1016/j.devcel.2014.06.013
1828:10.1016/j.devcel.2019.10.025
1779:10.1016/j.devcel.2016.08.003
1723:10.1016/j.molcel.2018.03.009
1336:Introduction to Glycobiology
930:Binds with high affinity to
2545:Asialoglycoprotein receptor
2337:10.4049/jimmunol.173.6.3825
722:complex, which consists of
437:have been shown to control
57:due to their dependency on
2806:
2472:
1255:Essentials of Glycobiology
938:Inflammatory bowel disease
855:Can enhance HIV infection
483:recognizes the cytofacial
456:Mycobacterium tuberculosis
304:are involved in apoptosis.
2573:proteochondroitin sulfate
1878:10.1007/s12026-012-8286-6
1663:10.1016/j.abb.2008.07.003
1452:10.1017/S1462399408000719
568:lest they are removed by
404:Site-directed mutagenesis
382:Nuclear pre-mRNA splicing
2467:Medical Subject Headings
2369:10.1007/0-306-46843-3_37
1095:Pregnancy complications
808:Table of human galectins
410:Galectins in control of
390:complexes including the
240:transmembrane signalling
1251:"Chapter 33: Galectins"
1051:Charcot–Leyden crystals
824:Implication in disease
400:affinity chromatography
1555:Glycoconjugate Journal
869:Gastrointestinal tract
712:adaptive immune system
128:
51:O-linked glycosylation
28:
2560:Mannan-binding lectin
2324:Journal of Immunology
1916:Nature Communications
1614:10.1093/glycob/cwq097
1391:10.1093/glycob/cwf081
927:Intestine and stomach
878:myocardial infarction
598:graft vs host disease
576:Galectins and disease
125:
22:
2418:10.1084/jem.20100687
2136:10.1128/AAC.05595-11
1866:Immunologic Research
1018:Rheumatoid arthritis
594:chronic inflammation
539:(NDP52) recognizing
108:extracellular matrix
2747:Phytohaemagglutinin
2040:2012NYASA1253..133S
1928:2012NatCo...3.1122R
1522:10.1038/nature10744
1514:2012Natur.482..414T
1300:10.2210/pdb1hlc/pdb
1195:2010NYASA1183..158L
794:N-acetyllactosamine
363:autoimmune diseases
2176:Developmental Cell
1936:10.1038/ncomms2128
1816:Developmental Cell
1767:Developmental Cell
602:allergic reactions
590:autoimmune disease
545:-damaged vacuole.
451:crystalline silica
212:-acetylglucosamine
129:
43:-acetyllactosamine
29:
2772:
2771:
2708:
2707:
2378:978-0-306-46515-4
2228:on Cardiac Cells"
2226:Trypanosoma cruzi
1717:(1): 120–135.e8.
1345:978-0-19-956911-3
1099:
1098:
1091:Lysophospholipase
971:Wide distribution
889:Wide distribution
777:Trypanosoma cruzi
388:ribonucleoprotein
2797:
2752:Pokeweed mitogen
2567:Mannose receptor
2533:
2511:
2504:
2497:
2488:
2440:
2439:
2429:
2397:
2391:
2390:
2356:
2350:
2349:
2339:
2315:
2306:
2305:
2277:
2268:
2267:
2257:
2247:
2238:(10): e0004148.
2219:
2210:
2209:
2199:
2167:
2158:
2157:
2147:
2115:
2109:
2108:
2074:
2068:
2067:
2023:
2014:
2013:
2003:
1986:(17): 6799–806.
1971:
1958:
1957:
1947:
1907:
1898:
1897:
1861:
1850:
1849:
1839:
1807:
1801:
1800:
1790:
1758:
1745:
1744:
1734:
1702:
1685:
1684:
1674:
1642:
1636:
1635:
1625:
1608:(10): 1199–207.
1593:
1587:
1586:
1550:
1544:
1543:
1533:
1493:
1482:
1481:
1463:
1435:
1404:
1403:
1393:
1384:(10): 127R–36R.
1369:
1350:
1349:
1331:
1320:
1319:
1283:
1277:
1276:
1246:
1233:
1232:
1214:
1175:
1166:
1165:
1155:
1146:(33): 20807–10.
1131:
1120:
1119:
1112:
812:
658:endothelial cell
286:epithelial cells
224:steric hindrance
201:hydrogen bonding
192:oligosaccharides
59:disulphide bonds
38:sugars, such as
2805:
2804:
2800:
2799:
2798:
2796:
2795:
2794:
2785:Protein domains
2775:
2774:
2773:
2768:
2704:
2668:
2600:
2524:
2515:
2485:
2449:
2444:
2443:
2412:(11): 2343–54.
2399:
2398:
2394:
2379:
2358:
2357:
2353:
2317:
2316:
2309:
2288:(2–3): 263–73.
2279:
2278:
2271:
2221:
2220:
2213:
2169:
2168:
2161:
2117:
2116:
2112:
2097:
2076:
2075:
2071:
2025:
2024:
2017:
1980:Cancer Research
1973:
1972:
1961:
1909:
1908:
1901:
1872:(1–2): 100–10.
1863:
1862:
1853:
1822:(1): 69–87.e8.
1809:
1808:
1804:
1760:
1759:
1748:
1704:
1703:
1688:
1644:
1643:
1639:
1595:
1594:
1590:
1561:(7–9): 517–26.
1552:
1551:
1547:
1508:(7385): 414–8.
1495:
1494:
1485:
1437:
1436:
1407:
1371:
1370:
1353:
1346:
1333:
1332:
1323:
1294:(36): 27034–8.
1285:
1284:
1280:
1265:
1248:
1247:
1236:
1177:
1176:
1169:
1133:
1132:
1123:
1114:
1113:
1109:
1104:
810:
773:
744:dendritic cells
704:
678:
660:walls, such as
610:
578:
463:interacts with
427:
384:
375:
357:with deficient
355:transgenic mice
351:T cell receptor
347:
290:immune response
253:
244:knock-out mouse
232:
167:
159:tetrasaccharide
120:
17:
12:
11:
5:
2803:
2801:
2793:
2792:
2787:
2777:
2776:
2770:
2769:
2767:
2766:
2761:
2756:
2755:
2754:
2749:
2744:
2742:Concanavalin A
2734:
2733:
2732:
2727:
2716:
2714:
2710:
2709:
2706:
2705:
2703:
2702:
2697:
2692:
2687:
2682:
2676:
2674:
2670:
2669:
2667:
2666:
2661:
2656:
2651:
2646:
2641:
2636:
2631:
2626:
2621:
2616:
2610:
2608:
2602:
2601:
2599:
2598:
2597:
2596:
2591:
2586:
2581:
2569:
2564:
2563:
2562:
2552:
2547:
2541:
2539:
2537:C-type lectins
2530:
2526:
2525:
2516:
2514:
2513:
2506:
2499:
2491:
2471:
2470:
2460:
2455:
2448:
2447:External links
2445:
2442:
2441:
2392:
2377:
2351:
2330:(6): 3825–37.
2307:
2269:
2211:
2182:(4): 394–409.
2159:
2110:
2095:
2069:
2015:
1959:
1899:
1851:
1802:
1746:
1711:Molecular Cell
1686:
1637:
1588:
1545:
1483:
1405:
1351:
1344:
1321:
1278:
1263:
1234:
1167:
1121:
1106:
1105:
1103:
1100:
1097:
1096:
1093:
1088:
1083:
1077:
1076:
1073:
1067:
1066:Adipose tissue
1064:
1058:
1057:
1047:
1044:
1034:
1028:
1027:
1021:Implicated in
1015:
1006:
1000:Synovial fluid
992:
986:
985:
979:Implicated in
975:
972:
969:
963:
962:
959:
953:
948:
942:
941:
935:
928:
925:
919:
918:
912:Implicated in
908:
890:
887:
881:
880:
874:
871:
866:
860:
859:
853:
841:
832:
826:
825:
822:
819:
816:
815:Human galectin
809:
806:
786:cardiomyocytes
782:Chagas disease
772:
769:
703:
700:
677:
674:
609:
606:
577:
574:
426:
408:
383:
380:
374:
371:
346:
343:
342:
341:
330:
323:
305:
252:
249:
231:
228:
166:
165:Ligand binding
163:
119:
116:
15:
13:
10:
9:
6:
4:
3:
2:
2802:
2791:
2788:
2786:
2783:
2782:
2780:
2765:
2762:
2760:
2759:Legume lectin
2757:
2753:
2750:
2748:
2745:
2743:
2740:
2739:
2738:
2735:
2731:
2728:
2726:
2723:
2722:
2721:
2718:
2717:
2715:
2711:
2701:
2698:
2696:
2693:
2691:
2688:
2686:
2683:
2681:
2678:
2677:
2675:
2671:
2665:
2662:
2660:
2657:
2655:
2652:
2650:
2647:
2645:
2642:
2640:
2637:
2635:
2632:
2630:
2627:
2625:
2622:
2620:
2617:
2615:
2612:
2611:
2609:
2607:
2603:
2595:
2592:
2590:
2587:
2585:
2582:
2580:
2577:
2576:
2575:
2574:
2570:
2568:
2565:
2561:
2558:
2557:
2556:
2553:
2551:
2548:
2546:
2543:
2542:
2540:
2538:
2534:
2531:
2527:
2523:
2519:
2512:
2507:
2505:
2500:
2498:
2493:
2492:
2489:
2484:
2480:
2476:
2468:
2464:
2461:
2459:
2456:
2454:
2451:
2450:
2446:
2437:
2433:
2428:
2423:
2419:
2415:
2411:
2407:
2403:
2396:
2393:
2388:
2384:
2380:
2374:
2370:
2366:
2362:
2355:
2352:
2347:
2343:
2338:
2333:
2329:
2325:
2321:
2314:
2312:
2308:
2303:
2299:
2295:
2291:
2287:
2283:
2276:
2274:
2270:
2265:
2261:
2256:
2251:
2246:
2241:
2237:
2233:
2229:
2227:
2218:
2216:
2212:
2207:
2203:
2198:
2193:
2189:
2185:
2181:
2177:
2173:
2166:
2164:
2160:
2155:
2151:
2146:
2141:
2137:
2133:
2130:(1): 154–62.
2129:
2125:
2121:
2114:
2111:
2106:
2102:
2098:
2096:9780123809995
2092:
2088:
2084:
2080:
2073:
2070:
2065:
2061:
2057:
2053:
2049:
2045:
2041:
2037:
2034:(1): 133–48.
2033:
2029:
2022:
2020:
2016:
2011:
2007:
2002:
1997:
1993:
1989:
1985:
1981:
1977:
1970:
1968:
1966:
1964:
1960:
1955:
1951:
1946:
1941:
1937:
1933:
1929:
1925:
1921:
1917:
1913:
1906:
1904:
1900:
1895:
1891:
1887:
1883:
1879:
1875:
1871:
1867:
1860:
1858:
1856:
1852:
1847:
1843:
1838:
1833:
1829:
1825:
1821:
1817:
1813:
1806:
1803:
1798:
1794:
1789:
1784:
1780:
1776:
1772:
1768:
1764:
1757:
1755:
1753:
1751:
1747:
1742:
1738:
1733:
1728:
1724:
1720:
1716:
1712:
1708:
1701:
1699:
1697:
1695:
1693:
1691:
1687:
1682:
1678:
1673:
1668:
1664:
1660:
1656:
1652:
1648:
1641:
1638:
1633:
1629:
1624:
1619:
1615:
1611:
1607:
1603:
1599:
1592:
1589:
1584:
1580:
1576:
1572:
1568:
1564:
1560:
1556:
1549:
1546:
1541:
1537:
1532:
1527:
1523:
1519:
1515:
1511:
1507:
1503:
1499:
1492:
1490:
1488:
1484:
1479:
1475:
1471:
1467:
1462:
1457:
1453:
1449:
1445:
1441:
1434:
1432:
1430:
1428:
1426:
1424:
1422:
1420:
1418:
1416:
1414:
1412:
1410:
1406:
1401:
1397:
1392:
1387:
1383:
1379:
1375:
1368:
1366:
1364:
1362:
1360:
1358:
1356:
1352:
1347:
1341:
1337:
1330:
1328:
1326:
1322:
1317:
1313:
1309:
1305:
1301:
1297:
1293:
1289:
1282:
1279:
1274:
1270:
1266:
1264:9780879697709
1260:
1256:
1252:
1245:
1243:
1241:
1239:
1235:
1230:
1226:
1222:
1218:
1213:
1208:
1204:
1200:
1196:
1192:
1189:(1): 158–82.
1188:
1184:
1180:
1174:
1172:
1168:
1163:
1159:
1154:
1149:
1145:
1141:
1137:
1130:
1128:
1126:
1122:
1117:
1111:
1108:
1101:
1094:
1092:
1089:
1087:
1084:
1082:
1079:
1078:
1074:
1072:
1068:
1065:
1063:
1060:
1059:
1056:
1052:
1048:
1045:
1043:
1039:
1036:Expressed in
1035:
1033:
1030:
1029:
1026:
1024:
1019:
1016:
1014:
1011:
1007:
1005:
1002:
1001:
997:
993:
991:
988:
987:
984:
982:
976:
973:
970:
968:
965:
964:
960:
958:
954:
952:
949:
947:
944:
943:
939:
936:
933:
929:
926:
924:
921:
920:
917:
915:
909:
907:
904:
901:
898:
897:
891:
888:
886:
883:
882:
879:
875:
872:
870:
867:
865:
862:
861:
858:
854:
852:
849:
846:
842:
840:
837:
833:
831:
828:
827:
823:
820:
817:
814:
813:
807:
805:
803:
799:
795:
791:
787:
783:
779:
778:
770:
768:
766:
762:
757:
753:
749:
745:
741:
737:
733:
729:
725:
721:
717:
713:
709:
701:
699:
697:
693:
689:
684:
675:
673:
669:
667:
663:
659:
655:
651:
647:
646:breast cancer
643:
639:
635:
631:
627:
623:
619:
615:
614:tumorigenesis
607:
605:
603:
599:
595:
591:
587:
583:
575:
573:
571:
567:
563:
559:
555:
551:
546:
544:
543:
538:
534:
530:
526:
522:
518:
514:
510:
506:
502:
498:
494:
490:
486:
482:
478:
474:
473:glycoproteins
470:
466:
462:
458:
457:
452:
448:
444:
440:
436:
432:
425:
421:
417:
413:
409:
407:
405:
401:
397:
393:
389:
381:
379:
372:
370:
368:
364:
360:
356:
352:
344:
339:
335:
331:
328:
324:
321:
317:
316:keratinocytes
313:
310:
306:
303:
299:
295:
291:
287:
283:
279:
275:
271:
267:
266:
265:
263:
259:
250:
248:
245:
241:
237:
229:
227:
225:
221:
217:
213:
211:
206:
202:
198:
193:
188:
187:Van der Waals
184:
180:
176:
172:
164:
162:
160:
156:
153:of about 135
152:
147:
144:
140:
135:
124:
117:
115:
113:
109:
105:
101:
97:
96:extracellular
93:
89:
85:
81:
77:
73:
69:
65:
60:
56:
52:
48:
44:
42:
37:
36:β-galactoside
33:
26:
21:
2689:
2685:Calreticulin
2614:Sialoadhesin
2571:
2409:
2405:
2395:
2360:
2354:
2327:
2323:
2285:
2281:
2235:
2231:
2225:
2179:
2175:
2127:
2123:
2113:
2079:Glycobiology
2078:
2072:
2031:
2027:
1983:
1979:
1919:
1915:
1869:
1865:
1819:
1815:
1805:
1773:(1): 13–27.
1770:
1766:
1714:
1710:
1657:(1): 18–25.
1654:
1650:
1640:
1605:
1602:Glycobiology
1601:
1591:
1558:
1554:
1548:
1505:
1501:
1443:
1439:
1381:
1378:Glycobiology
1377:
1335:
1291:
1287:
1281:
1254:
1186:
1182:
1143:
1139:
1110:
1070:
1023:tuberculosis
1020:
1012:
1009:
1004:Macrophages
1003:
998:
995:
981:tuberculosis
978:
956:
914:tuberculosis
911:
905:
902:
899:
893:
856:
850:
847:
844:
838:
801:
797:
789:
775:
774:
747:
731:
720:glycoprotein
705:
679:
670:
611:
579:
547:
540:
454:
429:Cytoplasmic
428:
385:
376:
358:
348:
320:UV radiation
254:
233:
209:
196:
182:
178:
168:
148:
130:
40:
31:
30:
24:
2720:Toxalbumins
2266:. e0004148.
1461:11336/25865
1212:11336/14677
1081:Galectin-13
1075:None found
1062:Galectin-12
1038:eosinophils
1032:Galectin-10
932:lipid rafts
756:co-receptor
714:. HIV is a
708:CD4 T cells
600:(GVHD) and
477:glycolipids
392:spliceosome
216:amino acids
155:amino acids
86:, and some
2779:Categories
1102:References
990:Galectin-9
967:Galectin-8
946:Galectin-7
923:Galectin-4
885:Galectin-3
864:Galectin-2
830:Galectin-1
662:E-selectin
636:, such as
634:cell cycle
622:metastasis
550:Galectin-3
542:Salmonella
513:galectin-8
493:Galectin-8
481:galectin-8
461:galectin-8
435:galectin-9
431:galectin-8
338:neutrophil
327:adipocytes
258:cell death
151:beta-sheet
72:amphibians
2555:Collectin
2483:IPR001079
1049:Found in
1042:basophils
742:found on
626:oncogenes
618:malignant
570:autophagy
566:lysosomes
562:endosomes
558:lysosomes
552:recruits
424:autophagy
367:cytokines
262:apoptosis
251:Apoptosis
171:galactose
134:integrins
118:Structure
112:secretion
80:nematodes
32:Galectins
2737:Mitogens
2700:Selectin
2690:Galectin
2680:Calnexin
2664:SIGLEC12
2659:SIGLEC10
2594:Neurocan
2589:Brevican
2584:Versican
2579:Aggrecan
2479:InterPro
2463:Galectin
2436:20937702
2387:11783481
2346:15356130
2302:12223274
2264:26451839
2206:25127057
2154:22064534
2105:20816214
2064:22981610
2056:22524424
2010:19690136
1954:23047680
1922:: 1122.
1894:35482823
1886:22418727
1846:31813797
1797:27693506
1741:29625033
1681:18662664
1632:20574110
1575:14758075
1540:22246324
1478:24193126
1470:18549522
1400:12244068
1316:44347534
1273:20301264
1221:20146714
1086:Placenta
1025:defense
983:defense
916:defense
876:Risk of
821:Function
818:Location
790:T. cruzi
761:efficacy
692:Beclin 1
683:CALCOCO2
666:in vitro
638:cyclin E
628:such as
537:CALCOCO2
396:splicing
373:Adhesion
312:promoter
236:adhesion
230:Function
205:hydroxyl
139:splicing
47:N-linked
2790:Lectins
2654:SIGLEC9
2649:SIGLEC8
2644:SIGLEC7
2639:SIGLEC6
2634:SIGLEC5
2522:lectins
2518:Protein
2427:2964580
2255:4599936
2197:4146662
2145:3256073
2036:Bibcode
2001:2741610
1945:3794716
1924:Bibcode
1837:6997950
1788:5104201
1732:5911935
1672:2590671
1623:2934707
1583:4953379
1531:3343631
1510:Bibcode
1446:: e17.
1308:8262940
1229:5861095
1191:Bibcode
1162:8063692
996:Thymus
994:Kidney
836:B cells
740:DC-SIGN
696:ATG16L1
521:LAMTOR1
517:SLC38A9
501:LAMTOR1
497:SLC38A9
485:glycans
469:glycans
282:antigen
276:in the
274:T cells
220:mannose
175:lactose
104:nucleus
100:cytosol
84:sponges
64:mammals
55:lectins
2764:BanLec
2606:SIGLEC
2529:Animal
2469:(MeSH)
2434:
2424:
2385:
2375:
2344:
2300:
2262:
2252:
2204:
2194:
2152:
2142:
2103:
2093:
2062:
2054:
2008:
1998:
1952:
1942:
1892:
1884:
1844:
1834:
1795:
1785:
1739:
1729:
1679:
1669:
1630:
1620:
1581:
1573:
1538:
1528:
1502:Nature
1476:
1468:
1398:
1342:
1314:
1306:
1271:
1261:
1227:
1219:
1179:Liu FT
1160:
1055:asthma
940:(IBD)
800:- and
771:Chagas
765:TRIM5α
746:. The
620:form,
608:Cancer
582:cancer
554:ESCRTs
533:TRIM16
523:, and
503:, and
445:) and
443:mTORC1
422:, and
340:death.
278:thymus
92:intra-
2730:Ricin
2725:Abrin
2713:Plant
2673:Other
2550:KLRD1
2060:S2CID
1890:S2CID
1579:S2CID
1474:S2CID
1312:S2CID
1225:S2CID
724:gp120
716:virus
654:mucin
650:MUC-1
642:c-myc
529:RRAGB
525:RRAGA
509:RRAGB
505:RRAGA
447:PRKAA
412:ESCRT
334:Bcl-2
143:mRNAs
88:fungi
68:birds
2624:CD33
2619:CD22
2477:and
2475:Pfam
2432:PMID
2383:PMID
2373:ISBN
2342:PMID
2298:PMID
2286:1572
2260:PMID
2202:PMID
2150:PMID
2101:PMID
2091:ISBN
2052:PMID
2032:1253
2006:PMID
1950:PMID
1882:PMID
1842:PMID
1793:PMID
1737:PMID
1677:PMID
1628:PMID
1571:PMID
1536:PMID
1466:PMID
1396:PMID
1340:ISBN
1304:PMID
1269:PMID
1259:ISBN
1217:PMID
1187:1183
1158:PMID
1040:and
896:JNK1
728:gp41
726:and
688:ULK1
640:and
564:and
489:mTOR
475:and
465:mTOR
439:mTOR
433:and
420:AMPK
416:mTOR
302:CD45
300:and
298:CD43
238:and
94:and
76:fish
2422:PMC
2414:doi
2410:207
2365:doi
2332:doi
2328:173
2290:doi
2250:PMC
2240:doi
2192:PMC
2184:doi
2140:PMC
2132:doi
2083:doi
2044:doi
1996:PMC
1988:doi
1940:PMC
1932:doi
1874:doi
1832:PMC
1824:doi
1783:PMC
1775:doi
1727:PMC
1719:doi
1667:PMC
1659:doi
1655:478
1618:PMC
1610:doi
1563:doi
1526:PMC
1518:doi
1506:482
1456:hdl
1448:doi
1386:doi
1296:doi
1292:268
1207:hdl
1199:doi
1148:doi
1144:269
1053:in
752:Th1
702:HIV
630:Ras
586:HIV
491:.
479:),
309:p53
294:CD7
272:of
177:or
49:or
2781::
2520::
2481::
2430:.
2420:.
2408:.
2404:.
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322:.
210:N
197:N
183:N
179:N
41:N
25:N
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